Browse result page of ThPDB2
This is the result page of the browse module of ThPDB2. This page gives the information about the query submitted by the user as per the browse category. Further details of the entries can be seen by clicking on the ID or THPP_ID. Further the user can sort the entries on the basis of various fields by clicking on the respective headers. The user can also download the results in various formats.
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| ID | THPP_ID | Therapeutic Name | Sequence | Molecular Weight | Chemical Formula | Isoelectric Point | Hydrophobicity | Melting Point | Half Life | Description | Disease/Indication | Pharmacodynamics | Mechanism of Action | Toxicity | Metabolism | Absorption | Volume of Distribution | Clearance | Categories | Patent Number | Date of Issue | Date of Expiry | Drug Interaction | Target | Brand Name | Company | Brand Description | Prescribed for | Chemical Name | Formulation | Physical Appearance | Route of Administation | Recommended Dosage | Contraindication | Side Effects | Useful Links 1 | Useful Links 2 | Remarks |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 10001 | Th1001 | Lepirudin | >Th1001_Lepirudin LTYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ | 6979 | C287H440N80O111S6 | 3.7 | -0.777 | 65 | Approximately 1.3 hours | Lepirudin is identical to natural hirudin except for substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. It is produced via yeast cells. | For the treatment of heparin-induced thrombocytopenia. | Lepirudin is used to break up clots and to reduce thrombocytopenia. It binds to thrombin and prevents thrombus or clot formation. It is a highly potent, selective, and essentially irreversible inhibitor of thrombin and clot-bond thrombin. Lepirudin requires no cofactor for its anticoagulant action. Lepirudin is a recombinant form of hirudin, an endogenous anticoagulant found in medicinal leeches. | Lepirudin forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen and initiate the clotting cascade. The inhibition of thrombin prevents the blood clotting cascade. | In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased. | Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. However, conclusive data are not available. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) | Bioavailability is 100% following injection. | 12.2 L [Healthy young subjects (n = 18, age 18-60 years)] | 164 ml/min [Healthy 18-60 yrs] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombin Proteins, Antithrombins, Blood and Blood Forming Organs, Cardiovascular Agents, Enzyme Inhibitors, Fibrin Modulating Agents, Hematologic Agents, Peptides, Protease Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Thrombin Inhibitors | CA1339104 | 29-Jul-1997 | 29-Jul-2014 | Ginkgo biloba = may increase bleed risk. | Prothrombin | Refludan | Berlex Labs | Berlex Labs | heparin-induced thrombocytopenia (HIT) and associated thromboembolic disease | [Leu1, Thr2]-63-desulfohirudin | Each vial of REFLUDAN contains 50 mg lepirudin. Other ingre-dients are 40 mg mannitol and sodium hydroxide for adjust-ment of pH to approximately 7 | Sterile, white, freeze-dried powder | Intravenous infusion | Recommended dose is 0.4 mg/kg body weight (up to 110kg) slowly intravenously (eg, over 15 to 20seconds) as a bolus dose, and can be followed by 0.15 mg/kg body weight (up to 110kg)/hour as a continuous Intravenous infusion for 2 to 10 days or longer if CL. | Hypersensitivity | NA | Link | NA | NA |
| 10002 | Th1001 | Lepirudin | >Th1001_Lepirudin LTYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ | 6979 | C287H440N80O111S6 | 3.7 | -0.777 | 65 | Approximately 1.3 hours | Lepirudin is identical to natural hirudin except for substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. It is produced via yeast cells. | For the treatment of heparin-induced thrombocytopenia. | Lepirudin is used to break up clots and to reduce thrombocytopenia. It binds to thrombin and prevents thrombus or clot formation. It is a highly potent, selective, and essentially irreversible inhibitor of thrombin and clot-bond thrombin. Lepirudin requires no cofactor for its anticoagulant action. Lepirudin is a recombinant form of hirudin, an endogenous anticoagulant found in medicinal leeches. | Lepirudin forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen and initiate the clotting cascade. The inhibition of thrombin prevents the blood clotting cascade. | In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased. | Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. However, conclusive data are not available. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) | Bioavailability is 100% following injection. | 18.7 L [Healthy elderly subjects (n = 10, age 65-80 years)] | 139 ml/min [Healthy 65-80 yrs] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombin Proteins, Antithrombins, Blood and Blood Forming Organs, Cardiovascular Agents, Enzyme Inhibitors, Fibrin Modulating Agents, Hematologic Agents, Peptides, Protease Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Thrombin Inhibitors | US5180668 | 19-Jan-1993 | 6-Mar-2012 | Treprostinil = increases the risk of bleeding when combined with Lepirudin. | NA | NA | Bayer Healthcare | Bayer Healthcare | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10003 | Th1001 | Lepirudin | >Th1001_Lepirudin LTYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ | 6979 | C287H440N80O111S6 | 3.7 | -0.777 | 65 | Approximately 1.3 hours | Lepirudin is identical to natural hirudin except for substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. It is produced via yeast cells. | For the treatment of heparin-induced thrombocytopenia. | Lepirudin is used to break up clots and to reduce thrombocytopenia. It binds to thrombin and prevents thrombus or clot formation. It is a highly potent, selective, and essentially irreversible inhibitor of thrombin and clot-bond thrombin. Lepirudin requires no cofactor for its anticoagulant action. Lepirudin is a recombinant form of hirudin, an endogenous anticoagulant found in medicinal leeches. | Lepirudin forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen and initiate the clotting cascade. The inhibition of thrombin prevents the blood clotting cascade. | In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased. | Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. However, conclusive data are not available. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) | Bioavailability is 100% following injection. | 18 L [Renally impaired patients (n = 16, creatinine clearance below 80 mL/min)] | 61 ml/min [renal impaired] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombin Proteins, Antithrombins, Blood and Blood Forming Organs, Cardiovascular Agents, Enzyme Inhibitors, Fibrin Modulating Agents, Hematologic Agents, Peptides, Protease Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Thrombin Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10004 | Th1001 | Lepirudin | >Th1001_Lepirudin LTYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ | 6979 | C287H440N80O111S6 | 3.7 | -0.777 | 65 | Approximately 1.3 hours | Lepirudin is identical to natural hirudin except for substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. It is produced via yeast cells. | For the treatment of heparin-induced thrombocytopenia. | Lepirudin is used to break up clots and to reduce thrombocytopenia. It binds to thrombin and prevents thrombus or clot formation. It is a highly potent, selective, and essentially irreversible inhibitor of thrombin and clot-bond thrombin. Lepirudin requires no cofactor for its anticoagulant action. Lepirudin is a recombinant form of hirudin, an endogenous anticoagulant found in medicinal leeches. | Lepirudin forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen and initiate the clotting cascade. The inhibition of thrombin prevents the blood clotting cascade. | In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased. | Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. However, conclusive data are not available. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) | Bioavailability is 100% following injection. | 32.1 L [HIT patients (n = 73)] | 114 ml/min [HIT (Heparin-induced thrombocytopenia)] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombin Proteins, Antithrombins, Blood and Blood Forming Organs, Cardiovascular Agents, Enzyme Inhibitors, Fibrin Modulating Agents, Hematologic Agents, Peptides, Protease Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Thrombin Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10022 | Th1003 | Dornase alfa | >Th1003_Dornase_alfa LKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK | 29253.9 | C1321H1999N339O396S9 | 4.58 | -0.083 | 67 | NA | It is a biosynthetic form of human enzyme DNase I, produced in genetically modified CHO cells using recombinant DNA technology. The 260 amino acid synthetic sequence of dornase alfa is identical to the endogenous human enzyme. Dornase alfa cleaves extracellular DNA to 5´-phosphodinucleotide and 5´-phospho-oligonucleotide end products(without affecting intracellular DNA). In individuals with cystic fibrosis, extracellular DNA, an extremely viscous anion, is released by degenerating leukocytes which accumulate during inflammatory responses to infections. Enzymatic breakdown of this extracellular DNA causes reduction in sputum viscosity and viscoelasticity. | Used in the treatment of cystic fibrosis as adjunct therapy. | Cystic fibrosis (CF) is characterized by retention of viscous purulent secretions in the airways. These thick secretions contribute to reduced pulmonary function and to frequent pulmonary infection. Purulent pulmonary secretions of individuals with cystic fibrosis contain very high concentrations of extracellular DNA released by degenerating leukocytes that accumulate in response to these infections. Dornase alfa hydrolyzes the DNA in sputum of CF patients and reduces sputum viscosity and viscoelasticity. The enzyme does not appear to affect sputum in the absence of an inflammatory response to infection, nor does it affect the sputum of healthy individuals. | Dornase alfa is a biosynthetic form of human DNase I. The enzyme is involved in endonucleolytic cleavage of extracellular DNA to 5´-phosphodinucleotide and 5´-phospho-oligonucleotide end products. It has no effect on intracellular DNA. Optimal activity dependent on the presence of divalent cations such as calcium and magnesium. Extracellular DNA is a viscous anionic polymer and its breakdown appears to improve the viscosity and viscoelasticity of purulent sputum of individuals with CF. | Adverse reactions occur at a rate of 1/1000 and are usually mild and transient in nature. Reported adverse effects include decreased lung function, rash, urticaria, chest pain (pleuritic/non-cardiac), dyspepsia, voice alteration (hoarseness), pharyngitis | NA | Systemic absorption is undetectable when administered via inhalation. | NA | NA | Amino Acids, Peptides, and Proteins, Cough and Cold Preparations, Decreased Respiratory Secretion Viscosity, Deoxyribonucleases, Endodeoxyribonucleases, Endonucleases, Enzymes, Enzymes and Coenzymes, Esterases, Expectorants, Hydrolases, Proteins, Recombinant Human Deoxyribonuclease 1 | CA2184581 | 22-Feb-2005 | 28-Feb-2015 | Afrezza (insulin inhalation, rapid acting) | DNA | Pulmozyme | Genentech Inc | Genentech Inc | Pulmozyme is used to improve lung function by thinning pulmonary secretions and reducing the risk of respiratory tract infections in people with cystic fibrosis. | NA | The aqueous formulation contains 1.0 mg/mL dornase alfa, 0.15 mg/mL calcium chloride dihydrate and 8.77 mg/mL sodium chloride. The solution contains no preservative and supports a pH of 6.3. | NA | Administered by inhalation of an aerosol mist prod | NA | allergic | Serious side effects include difficulty breathing; closing of the throat; swelling of the lips, tongue, or face; or hives; increased difficulty breathing; chest pain; or fever. Less serious side effects may be voice alteration; sore throat; rash. | Link | NA | NA |
| 10023 | Th1003 | Dornase alfa | >Th1003_Dornase_alfa LKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK | 29253.9 | C1321H1999N339O396S9 | 4.58 | -0.083 | 67 | NA | It is a biosynthetic form of human enzyme DNase I, produced in genetically modified CHO cells using recombinant DNA technology. The 260 amino acid synthetic sequence of dornase alfa is identical to the endogenous human enzyme. Dornase alfa cleaves extracellular DNA to 5´-phosphodinucleotide and 5´-phospho-oligonucleotide end products(without affecting intracellular DNA). In individuals with cystic fibrosis, extracellular DNA, an extremely viscous anion, is released by degenerating leukocytes which accumulate during inflammatory responses to infections. Enzymatic breakdown of this extracellular DNA causes reduction in sputum viscosity and viscoelasticity. | Used in the treatment of cystic fibrosis as adjunct therapy. | Cystic fibrosis (CF) is characterized by retention of viscous purulent secretions in the airways. These thick secretions contribute to reduced pulmonary function and to frequent pulmonary infection. Purulent pulmonary secretions of individuals with cystic fibrosis contain very high concentrations of extracellular DNA released by degenerating leukocytes that accumulate in response to these infections. Dornase alfa hydrolyzes the DNA in sputum of CF patients and reduces sputum viscosity and viscoelasticity. The enzyme does not appear to affect sputum in the absence of an inflammatory response to infection, nor does it affect the sputum of healthy individuals. | Dornase alfa is a biosynthetic form of human DNase I. The enzyme is involved in endonucleolytic cleavage of extracellular DNA to 5´-phosphodinucleotide and 5´-phospho-oligonucleotide end products. It has no effect on intracellular DNA. Optimal activity dependent on the presence of divalent cations such as calcium and magnesium. Extracellular DNA is a viscous anionic polymer and its breakdown appears to improve the viscosity and viscoelasticity of purulent sputum of individuals with CF. | Adverse reactions occur at a rate of 1/1000 and are usually mild and transient in nature. Reported adverse effects include decreased lung function, rash, urticaria, chest pain (pleuritic/non-cardiac), dyspepsia, voice alteration (hoarseness), pharyngitis, | NA | Systemic absorption is undetectable when administered via inhalation. | NA | NA | Amino Acids, Peptides, and Proteins, Cough and Cold Preparations, Decreased Respiratory Secretion Viscosity, Deoxyribonucleases, Endodeoxyribonucleases, Endonucleases, Enzymes, Enzymes and Coenzymes, Esterases, Expectorants, Hydrolases, Proteins, Recombinant Human Deoxyribonuclease 1 | NA | NA | NA | Exubera (insulin inhalation, rapid acting) | NA | NA | Cardinal Health, Catalent Pharma Solutions, F Hoffmann-La Roche Ltd., Meda AB, Medpointe Pharmaceuticals | Cardinal Health, Catalent Pharma Solutions, F Hoffmann-La Roche Ltd., Meda AB, Medpointe Pharmaceuticals | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10024 | Th1003 | Dornase alfa | >Th1003_Dornase_alfa LKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK | 29253.9 | C1321H1999N339O396S9 | 4.58 | -0.083 | 67 | NA | It is a biosynthetic form of human enzyme DNase I, produced in genetically modified CHO cells using recombinant DNA technology. The 260 amino acid synthetic sequence of dornase alfa is identical to the endogenous human enzyme. Dornase alfa cleaves extracellular DNA to 5´-phosphodinucleotide and 5´-phospho-oligonucleotide end products(without affecting intracellular DNA). In individuals with cystic fibrosis, extracellular DNA, an extremely viscous anion, is released by degenerating leukocytes which accumulate during inflammatory responses to infections. Enzymatic breakdown of this extracellular DNA causes reduction in sputum viscosity and viscoelasticity. | Used in the treatment of cystic fibrosis as adjunct therapy. | Cystic fibrosis (CF) is characterized by retention of viscous purulent secretions in the airways. These thick secretions contribute to reduced pulmonary function and to frequent pulmonary infection. Purulent pulmonary secretions of individuals with cystic fibrosis contain very high concentrations of extracellular DNA released by degenerating leukocytes that accumulate in response to these infections. Dornase alfa hydrolyzes the DNA in sputum of CF patients and reduces sputum viscosity and viscoelasticity. The enzyme does not appear to affect sputum in the absence of an inflammatory response to infection, nor does it affect the sputum of healthy individuals. | Dornase alfa is a biosynthetic form of human DNase I. The enzyme is involved in endonucleolytic cleavage of extracellular DNA to 5´-phosphodinucleotide and 5´-phospho-oligonucleotide end products. It has no effect on intracellular DNA. Optimal activity dependent on the presence of divalent cations such as calcium and magnesium. Extracellular DNA is a viscous anionic polymer and its breakdown appears to improve the viscosity and viscoelasticity of purulent sputum of individuals with CF. | Adverse reactions occur at a rate of 1/1000 and are usually mild and transient in nature. Reported adverse effects include decreased lung function, rash, urticaria, chest pain (pleuritic/non-cardiac), dyspepsia, voice alteration (hoarseness), pharyngitis, | NA | Systemic absorption is undetectable when administered via inhalation. | NA | NA | Amino Acids, Peptides, and Proteins, Cough and Cold Preparations, Decreased Respiratory Secretion Viscosity, Deoxyribonucleases, Endodeoxyribonucleases, Endonucleases, Enzymes, Enzymes and Coenzymes, Esterases, Expectorants, Hydrolases, Proteins, Recombinant Human Deoxyribonuclease 1 | CA2137237 | 26-Oct-2004 | 28-May-2013 | NA | NA | Viscozyme | Roche (Chile) | Roche (Chile) | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10025 | Th1004 | Denileukin diftitox | >Th1004_Denileukin_diftitox MGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAYSPGHKTHAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT | 57647.3 | C2560H4042N678O799S17 | 5.45 | -0.301 | NA | 1.16-1.3 hours | A recombinant (using E. coli expression system) DNA-derived cytotoxic protein containing amino acid sequences for diphtheria toxin fragments A and B (Met 1-Thr 387)-His and sequences for interleukin-2 (Ala 1-Thr 133). | Used in the treatment of cutaneous T-cell lymphoma. | Denileukin diftitox (Ontak) uses the cytocidal action of diphtheria toxin on cells which express the IL-2 receptor. The human IL-2 receptor exists in three forms on basis of affinity, low (CD25), intermediate (CD122/CD132) and high (CD25/CD122/CD132). Malignant cells expressing one or more of the subunits of the IL-2 receptor are found in certain leukemias and lymphomas including cutaneous T-cell lymphoma (CTCL). Ontak interacts with the high affinity IL-2 receptor on the cell surface and inhibits cellular protein synthesis, resulting in cell death within hours. | Denileukin diftitox binds to the high-affinity IL-2 receptor. The IL-2 receptor (Tac) subunit is expressed on activated lymphocytes. The diphtheria toxin associated with Ontak selectively kills the IL-2 bearing cells. | NA | NA | NA | 0.06 to 0.09 L/kg | 0.6 - 2.0 mL/min/kg [Lymphoma] | ADP Ribose Transferases, Amino Acids, Peptides, and Proteins, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Bacterial Toxins, Biological Factors, Cancer immunotherapy, CD25-directed Cytotoxin, Cytokines, Enzymes, Enzymes and Coenzymes, Glycosyltransferases, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interleukins, Lymphokines, Narrow Therapeutic Index Drugs, Pentosyltransferases, Peptides, Proteins, Recombinant Proteins, Toxins, Biological, Transferases | NA | NA | NA | Rilonacept decreases effects of toxoids by pharmacodynamic antagonism | Interleukin-2 receptor subunit alpha,Interleukin-2 receptor subunit beta,Cytokine receptor common subunit gamma | Ontak | Eisai Inc. , Hollister-Stier Laboratories LLC , Ligand Pharmaceuticals Inc. | Eisai Inc. , Hollister-Stier Laboratories LLC , Ligand Pharmaceuticals Inc. | Treating leukemia and lymphomas, including cutaneous (of the skin) T-cell lymphoma. | NA | Ontak contains 300 mcg of recombinant denileukin diftitox in a sterile solution of citric acid (20 mM), EDTA (0.05 mM) and polysorbate 20 ( < 1%) in Water for Injection, USP. The solution has a pH range of 6.9-7.2. | Sterile, white, preservative-free, lyophilized powder. | Intravenous (Intravenous) administration | NA | allergic | Common side effects include:headache, dizziness, or nervousness, numbness or tingling, skin itching or rash, runny or stuffy nose; weight gain or loss; mild diarrhea or constipation, or nausea, vomiting, loss of appetite. | Link | NA | NA |
| 10026 | Th1004 | Denileukin diftitox | >Th1004_Denileukin_diftitox MGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAYSPGHKTHAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT | 57647.3 | C2560H4042N678O799S17 | 5.45 | -0.301 | NA | 1.16-1.3 hours | A recombinant (using E. coli expression system) DNA-derived cytotoxic protein containing amino acid sequences for diphtheria toxin fragments A and B (Met 1-Thr 387)-His and sequences for interleukin-2 (Ala 1-Thr 133). | Used in the treatment of cutaneous T-cell lymphoma. | Denileukin diftitox (Ontak) uses the cytocidal action of diphtheria toxin on cells which express the IL-2 receptor. The human IL-2 receptor exists in three forms on basis of affinity, low (CD25), intermediate (CD122/CD132) and high (CD25/CD122/CD132). Malignant cells expressing one or more of the subunits of the IL-2 receptor are found in certain leukemias and lymphomas including cutaneous T-cell lymphoma (CTCL). Ontak interacts with the high affinity IL-2 receptor on the cell surface and inhibits cellular protein synthesis, resulting in cell death within hours. | Denileukin diftitox binds to the high-affinity IL-2 receptor. The IL-2 receptor (Tac) subunit is expressed on activated lymphocytes. The diphtheria toxin associated with Ontak selectively kills the IL-2 bearing cells. | NA | NA | NA | 0.06 to 0.09 L/kg | 0.6 - 2.0 mL/min/kg [Lymphoma] | ADP Ribose Transferases, Amino Acids, Peptides, and Proteins, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Bacterial Toxins, Biological Factors, Cancer immunotherapy, CD25-directed Cytotoxin, Cytokines, Enzymes, Enzymes and Coenzymes, Glycosyltransferases, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interleukins, Lymphokines, Narrow Therapeutic Index Drugs, Pentosyltransferases, Peptides, Proteins, Recombinant Proteins, Toxins, Biological, Transferases | NA | NA | NA | Trastuzumab may increase the risk of neutropenia and anemia. Monitor closely for signs and symptoms of adverse events. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10027 | Th1004 | Denileukin diftitox | >Th1004_Denileukin_diftitox MGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAYSPGHKTHAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT | 57647.3 | C2560H4042N678O799S17 | 5.45 | -0.301 | NA | 1.16-1.3 hours | A recombinant (using E. coli expression system) DNA-derived cytotoxic protein containing amino acid sequences for diphtheria toxin fragments A and B (Met 1-Thr 387)-His and sequences for interleukin-2 (Ala 1-Thr 133). | Used in the treatment of cutaneous T-cell lymphoma. | Denileukin diftitox (Ontak) uses the cytocidal action of diphtheria toxin on cells which express the IL-2 receptor. The human IL-2 receptor exists in three forms on basis of affinity, low (CD25), intermediate (CD122/CD132) and high (CD25/CD122/CD132). Malignant cells expressing one or more of the subunits of the IL-2 receptor are found in certain leukemias and lymphomas including cutaneous T-cell lymphoma (CTCL). Ontak interacts with the high affinity IL-2 receptor on the cell surface and inhibits cellular protein synthesis, resulting in cell death within hours. | Denileukin diftitox binds to the high-affinity IL-2 receptor. The IL-2 receptor (Tac) subunit is expressed on activated lymphocytes. The diphtheria toxin associated with Ontak selectively kills the IL-2 bearing cells. | NA | NA | NA | 0.06 to 0.09 L/kg | 0.6 - 2.0 mL/min/kg [Lymphoma] | ADP Ribose Transferases, Amino Acids, Peptides, and Proteins, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Bacterial Toxins, Biological Factors, Cancer immunotherapy, CD25-directed Cytotoxin, Cytokines, Enzymes, Enzymes and Coenzymes, Glycosyltransferases, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interleukins, Lymphokines, Narrow Therapeutic Index Drugs, Pentosyltransferases, Peptides, Proteins, Recombinant Proteins, Toxins, Biological, Transferases | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10032 | Th1006 | Bivalirudin | >Th1006_Bivalirudin FPRPGGGGNGDFEEIPEEYL | 2180.285 | C98H138N24O33 | 3.91 | -0.985 | NA | Normal renal function: 0.42 hours (in normal conditions) | Bivalirudin is a synthetic 20 residue peptide which acts as a thrombin inhibitor. Once bound to the active site of the inhibitor, thrombin cannot activate fibrinogen into fibrin which is a crucial step in the formation of thrombus. As it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. It is administered intravenously. | For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. | Bivalirudin directly and reversibly inhibits thrombin by specifically binding to both the catalytic site and the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible as thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. | Inhibits the action of thrombin by binding to both its catalytic site and to its anion-binding exosite. Thrombin, a serine proteinase that plays a central role in the thrombotic process, acts to cleave fibrinogen into fibrin monomers and activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. | Based on a study by Gleason et al., the no observed adverse effect level (NOAEL) for bivalirudin administered to rats via Intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. | 80% proteolytic cleavage | Bivalirudin exhibits linear pharmacokinetics. The mean steady state concentration is 12.3 ± 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr Intravenous infusion given over 4 hours. | 0.2L/kg | 3.4 mL/min/kg [Normal renal function] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombins, Blood and Blood Forming Organs, Enzyme Inhibitors, Hematologic Agents, Peptides, Protease Inhibitors, Serine Protease Inhibitors, Thrombin Inhibitors | US7582727 | 1-Sep-2009 | 27-Jul-2028 | Deferasirox, Anticoagulants increase the risk for gastrointestinal ulceration/irritation and/or GI bleeding. If these two agents must be used, patients need to be closely monitored for signs and symptoms of GI toxicity. | Prothrombin | Angiomax | Sandoz Canada Incorporated, The Medicines Company,Cardinal Health, Sandoz Inc | Sandoz Canada Incorporated, The Medicines Company,Cardinal Health, Sandoz Inc | It is used for thinning the blood in patients with unstable angina who are undergoing percutaneous transluminal coronary angioplasty (PTCA) and in patients undergoing percutaneous coronary intervention (PCI). | D-phenylalanyl-L-prolyl-L-arginyl-L-prolyl-glycylglycyl-glycyl-glycyl-L-asparagyl-glycyl-L-aspartyl-L-phenylalanyl-L-glutamyl-L-glutamyl-L-isoleucyl-L-prolyl-L-glutamyl-L-glutamyl-L-tyrosyl-L-leucine trifluoroacetate (salt) hydrate | Each vial contains 250 mg bivalirudin, 125 mg mannitol, and sodium hydroxide to adjust the pH to 5-6 (equivalent of approximately 12.5 mg sodium). When reconstituted with Sterile Water for Injection, the product yields a clear to opalescent, colorless to | Supplied in single-use vials as a white lyophilized cake | Intravenous infusion | Intravenous (IV) bolus dose of 0.75 mg/kg, followed by an infusion of 1.75 mg/kg/h for the duration of the PCI/PTCA procedure. | Allergic and have major active bleeding | Anxiety; back, stomach, or pelvic pain; headache; nausea; nervousness; pain at the injection site; trouble sleeping; upset stomach; vomiting. And severe side effect may include Severe allergic reactions (rash; hives; itching; difficulty breathing. | Link | NA | NA |
| 10033 | Th1006 | Bivalirudin | >Th1006_Bivalirudin FPRPGGGGNGDFEEIPEEYL | 2180.285 | C98H138N24O33 | 3.91 | -0.985 | NA | Creatinine clearance 10-29mL/min: 0.95 hours | Bivalirudin is a synthetic 20 residue peptide which acts as a thrombin inhibitor. Once bound to the active site of the inhibitor, thrombin cannot activate fibrinogen into fibrin which is a crucial step in the formation of thrombus. As it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. It is administered intravenously. | For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. | Bivalirudin directly and reversibly inhibits thrombin by specifically binding to both the catalytic site and the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible as thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. | Inhibits the action of thrombin by binding to both its catalytic site and to its anion-binding exosite. Thrombin, a serine proteinase that plays a central role in the thrombotic process, acts to cleave fibrinogen into fibrin monomers and activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. | Based on a study by Gleason et al., the no observed adverse effect level (NOAEL) for bivalirudin administered to rats via Intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. | 80% proteolytic cleavage | Bivalirudin exhibits linear pharmacokinetics. The mean steady state concentration is 12.3 ± 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr Intravenous infusion given over 4 hours. | 0.2L/kg | 3.4 mL/min/kg [mild renal function] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombins, Blood and Blood Forming Organs, Enzyme Inhibitors, Hematologic Agents, Peptides, Protease Inhibitors, Serine Protease Inhibitors, Thrombin Inhibitors | US5196404 | 23-Mar-1993 | 15-Dec-2014 | Gemcitabine, Gemcitabine may enhance the adverse/toxic effect of Bleomycin. The risk of pulmonary toxicity may be increased. Use extreme caution if using gemcitabine and bleomycin in combination. Monitor for the development of pulmonary toxicity | NA | Angiox | The Medicines Company UK Ltd | The Medicines Company UK Ltd | Used as an anticoagulant in adult patients undergoing percutaneous coronary intervention (PCI), including patients with ST-segment elevation myocardial infarction (STEMI) undergoing primary PCI. Angiox is also indicated for the treatment of adult patients | NA | Each vial contains 250 mg bivalirudin. | Powder for concentrated solution | Injection | 0.75 mg/kg IV bolus, initially, followed by continuous infusion at rate of 1.75 mg/kg/hr for duration of procedure | Hypersensitivity, active bleeding or increased risk of bleeding because of haemostasis disorder or irreversible coagulation disorder, uncontrolled hypertension, subacute bacterial endocarditis, severe renal impairment and in dialysis dependent pateints, | NA | Link | NA | NA |
| 10034 | Th1006 | Bivalirudin | >Th1006_Bivalirudin FPRPGGGGNGDFEEIPEEYL | 2180.285 | C98H138N24O33 | 3.91 | -0.985 | NA | Dialysis-dependant patients: 3.5 hours | Bivalirudin is a synthetic 20 residue peptide which acts as a thrombin inhibitor. Once bound to the active site of the inhibitor, thrombin cannot activate fibrinogen into fibrin which is a crucial step in the formation of thrombus. As it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. It is administered intravenously. | For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. | Bivalirudin directly and reversibly inhibits thrombin by specifically binding to both the catalytic site and the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible as thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. | Inhibits the action of thrombin by binding to both its catalytic site and to its anion-binding exosite. Thrombin, a serine proteinase that plays a central role in the thrombotic process, acts to cleave fibrinogen into fibrin monomers and activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. | Based on a study by Gleason et al., the no observed adverse effect level (NOAEL) for bivalirudin administered to rats via Intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. | 80% proteolytic cleavage | Bivalirudin exhibits linear pharmacokinetics. The mean steady state concentration is 12.3 ± 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr Intravenous infusion given over 4 hours. | 0.2L/kg | 2.7 mL/min/kg [moderate renal function] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombins, Blood and Blood Forming Organs, Enzyme Inhibitors, Hematologic Agents, Peptides, Protease Inhibitors, Serine Protease Inhibitors, Thrombin Inhibitors | CA2065150 | 14-Dec-1999 | 17-Aug-2010 | Ginkgo biloba, Additive anticoagulant/antiplatelet effects may increase bleed risk. Concomitant therapy should be avoided. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10035 | Th1006 | Bivalirudin | >Th1006_Bivalirudin FPRPGGGGNGDFEEIPEEYL | 2180.285 | C98H138N24O33 | 3.91 | -0.985 | NA | NA | Bivalirudin is a synthetic 20 residue peptide which acts as a thrombin inhibitor. Once bound to the active site of the inhibitor, thrombin cannot activate fibrinogen into fibrin which is a crucial step in the formation of thrombus. As it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. It is administered intravenously. | For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. | Bivalirudin directly and reversibly inhibits thrombin by specifically binding to both the catalytic site and the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible as thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. | Inhibits the action of thrombin by binding to both its catalytic site and to its anion-binding exosite. Thrombin, a serine proteinase that plays a central role in the thrombotic process, acts to cleave fibrinogen into fibrin monomers and activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. | Based on a study by Gleason et al., the no observed adverse effect level (NOAEL) for bivalirudin administered to rats via Intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. | 80% proteolytic cleavage | Bivalirudin exhibits linear pharmacokinetics. The mean steady state concentration is 12.3 ± 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr Intravenous infusion given over 4 hours. | 0.2L/kg | 2.8 mL/min/kg [severe renal function] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombins, Blood and Blood Forming Organs, Enzyme Inhibitors, Hematologic Agents, Peptides, Protease Inhibitors, Serine Protease Inhibitors, Thrombin Inhibitors | NA | NA | NA | Rivaroxaban, Anticoagulants may enhance the anticoagulant effect of rivaroxaban. Avoid concurrent use of rivaroxaban with other anticoagulants whenever possible, other than during transition periods, due to the possible increased for bleeding. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10036 | Th1006 | Bivalirudin | >Th1006_Bivalirudin FPRPGGGGNGDFEEIPEEYL | 2180.285 | C98H138N24O33 | 3.91 | -0.985 | NA | NA | Bivalirudin is a synthetic 20 residue peptide which acts as a thrombin inhibitor. Once bound to the active site of the inhibitor, thrombin cannot activate fibrinogen into fibrin which is a crucial step in the formation of thrombus. As it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. It is administered intravenously. | For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. | Bivalirudin directly and reversibly inhibits thrombin by specifically binding to both the catalytic site and the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible as thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. | Inhibits the action of thrombin by binding to both its catalytic site and to its anion-binding exosite. Thrombin, a serine proteinase that plays a central role in the thrombotic process, acts to cleave fibrinogen into fibrin monomers and activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. | Based on a study by Gleason et al., the no observed adverse effect level (NOAEL) for bivalirudin administered to rats via Intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. | 80% proteolytic cleavage | Bivalirudin exhibits linear pharmacokinetics. The mean steady state concentration is 12.3 ± 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr Intravenous infusion given over 4 hours. | 0.2L/kg | 1 mL/min/kg [Dialysis-dependent patients] | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombins, Blood and Blood Forming Organs, Enzyme Inhibitors, Hematologic Agents, Peptides, Protease Inhibitors, Serine Protease Inhibitors, Thrombin Inhibitors | NA | NA | NA | Treprostinil, The prostacyclin analogue, Treprostinil, increases the risk of bleeding when combined with the anticoagulant, Bivalirudin. Monitor for increased bleeding during concomitant thearpy. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10037 | Th1006 | Bivalirudin | >Th1006_Bivalirudin FPRPGGGGNGDFEEIPEEYL | 2180.285 | C98H138N24O33 | 3.91 | -0.985 | NA | NA | Bivalirudin is a synthetic 20 residue peptide which acts as a thrombin inhibitor. Once bound to the active site of the inhibitor, thrombin cannot activate fibrinogen into fibrin which is a crucial step in the formation of thrombus. As it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. It is administered intravenously. | For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. | Bivalirudin directly and reversibly inhibits thrombin by specifically binding to both the catalytic site and the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible as thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. | Inhibits the action of thrombin by binding to both its catalytic site and to its anion-binding exosite. Thrombin, a serine proteinase that plays a central role in the thrombotic process, acts to cleave fibrinogen into fibrin monomers and activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. | Based on a study by Gleason et al., the no observed adverse effect level (NOAEL) for bivalirudin administered to rats via Intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. | 80% proteolytic cleavage | Bivalirudin exhibits linear pharmacokinetics. The mean steady state concentration is 12.3 ± 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr Intravenous infusion given over 4 hours. | 0.2L/kg | NA | Amino Acids, Peptides, and Proteins, Anticoagulants, Antithrombins, Blood and Blood Forming Organs, Enzyme Inhibitors, Hematologic Agents, Peptides, Protease Inhibitors, Serine Protease Inhibitors, Thrombin Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10049 | Th1008 | Peginterferon alfa-2a | >Th1008_Peginterferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | NA | 5.99 | NA | 61 | Terminal half life is 164 hours (range 84 to 353 hours). | Human interferon 2a, is a covalent conjugate of recombinant interferon alfa-2a with a single branched bis-mono-methoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | To treat hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins which increases presentation of peptides derived from viral antigens. Thus enhancing the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Peginterferon alfa-2a may manifest neuropsychiatric complications include suicide, suicidal ideation, homicidal ideation, depression, relapse of drug addiction, and drug overdose Label. Hypertension, supraventricular arrhythmias, chest pain, and myocardial infarction have been observed in patients using Peginterferon alfa-2a. | NA | NA | NA | 94 milliliters per hour | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cardiotoxic antineoplastic agents, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatotoxic Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Macromolecular Substances, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | CA2203480 | 30-Jun-2009 | 23-Apr-2017 | Interferon increases the effect and toxicity of theophylline called Aminophylline | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Pegasys | Hoffman-La Roche Inc | Hoffman-La Roche Inc | Pegasys is used to treat chronic hepatitis B or C (adults), and to treat chronic hepatitis C (children 5 or more years of age). It is mostly used with ribavirin | NA | Each vial of 180 mcg/mL peginterferon alfa-2a (expressed as the amount of interferon alfa-2a) also contains acetic acid (0.05 mg), benzyl alcohol (10 mg), polysorbate 80 (0.05 mg), sodium acetate trihydrate (2.62 mg), and sodium chloride (8 mg) at pH 6 ± | Sterile, preservative-free, colorless to light yellow injectable solution | Subcutaneous Injection | Pegasys is usually given once a week. | Allergic | Nausea, vomiting, loss of appetite; headache, muscle pain, feeling weak or tired; sleep problems (insomnia); temporary hair loss; or itching, redness, dryness, or swelling where the medicine was injected. | Link | NA | NA |
| 10050 | Th1008 | Peginterferon alfa-2a | >Th1008_Peginterferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | NA | 5.99 | NA | 61 | Terminal half life is 164 hours (range 84 to 353 hours). | Human interferon 2a, is a covalent conjugate of recombinant interferon alfa-2a with a single branched bis-mono-methoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | To treat hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins which increases presentation of peptides derived from viral antigens. Thus enhancing the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Peginterferon alfa-2a may manifest neuropsychiatric complications include suicide, suicidal ideation, homicidal ideation, depression, relapse of drug addiction, and drug overdose Label. Hypertension, supraventricular arrhythmias, chest pain, and myocardial infarction have been observed in patients using Peginterferon alfa-2a. | NA | NA | NA | 94 milliliters per hour | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cardiotoxic antineoplastic agents, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatotoxic Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Macromolecular Substances, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | CA2172664 | 3-Oct-2000 | 26-Mar-2016 | Interferon increases the effect and toxicity of theophylline called Dyphylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Having failure or autoimmune hepatitis | NA | Link | NA | NA |
| 10051 | Th1008 | Peginterferon alfa-2a | >Th1008_Peginterferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | NA | 5.99 | NA | 61 | Terminal half life is 164 hours (range 84 to 353 hours). | Human interferon 2a, is a covalent conjugate of recombinant interferon alfa-2a with a single branched bis-mono-methoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | To treat hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins which increases presentation of peptides derived from viral antigens. Thus enhancing the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Peginterferon alfa-2a may manifest neuropsychiatric complications include suicide, suicidal ideation, homicidal ideation, depression, relapse of drug addiction, and drug overdose Label. Hypertension, supraventricular arrhythmias, chest pain, and myocardial infarction have been observed in patients using Peginterferon alfa-2a. | NA | NA | NA | 94 milliliters per hour | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cardiotoxic antineoplastic agents, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatotoxic Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Macromolecular Substances, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Etravirine (a CYP2C9 substrate, when used concomitantly with peginterferon alfa-2a, may experience a decrease in serum concentration. It is recommended to monitor effectiveness of etravirine therapy. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Haemoglobin blood cell disorder as sickle cell anemia or thalessimia. | NA | Link | NA | NA |
| 10052 | Th1008 | Peginterferon alfa-2a | >Th1008_Peginterferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | NA | 5.99 | NA | 61 | Terminal half life is 164 hours (range 84 to 353 hours). | Human interferon 2a, is a covalent conjugate of recombinant interferon alfa-2a with a single branched bis-mono-methoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | To treat hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins which increases presentation of peptides derived from viral antigens. Thus enhancing the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Peginterferon alfa-2a may manifest neuropsychiatric complications include suicide, suicidal ideation, homicidal ideation, depression, relapse of drug addiction, and drug overdose Label. Hypertension, supraventricular arrhythmias, chest pain, and myocardial infarction have been observed in patients using Peginterferon alfa-2a. | NA | NA | NA | 94 milliliters per hour | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cardiotoxic antineoplastic agents, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatotoxic Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Macromolecular Substances, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Interferon increases the effect and toxicity of theophylline called Oxtriphylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10053 | Th1008 | Peginterferon alfa-2a | >Th1008_Peginterferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | NA | 5.99 | NA | 61 | Terminal half life is 164 hours (range 84 to 353 hours). | Human interferon 2a, is a covalent conjugate of recombinant interferon alfa-2a with a single branched bis-mono-methoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | To treat hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins which increases presentation of peptides derived from viral antigens. Thus enhancing the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Peginterferon alfa-2a may manifest neuropsychiatric complications include suicide, suicidal ideation, homicidal ideation, depression, relapse of drug addiction, and drug overdose Label. Hypertension, supraventricular arrhythmias, chest pain, and myocardial infarction have been observed in patients using Peginterferon alfa-2a. | NA | NA | NA | 94 milliliters per hour | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cardiotoxic antineoplastic agents, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatotoxic Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Macromolecular Substances, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Interferon increases the effect and toxicity of theophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10054 | Th1008 | Peginterferon alfa-2a | >Th1008_Peginterferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | NA | 5.99 | NA | 61 | Terminal half life is 164 hours (range 84 to 353 hours). | Human interferon 2a, is a covalent conjugate of recombinant interferon alfa-2a with a single branched bis-mono-methoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | To treat hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins which increases presentation of peptides derived from viral antigens. Thus enhancing the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Peginterferon alfa-2a may manifest neuropsychiatric complications include suicide, suicidal ideation, homicidal ideation, depression, relapse of drug addiction, and drug overdose Label. Hypertension, supraventricular arrhythmias, chest pain, and myocardial infarction have been observed in patients using Peginterferon alfa-2a. | NA | NA | NA | 94 milliliters per hour | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cardiotoxic antineoplastic agents, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatotoxic Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Macromolecular Substances, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Co-administration of Peginterferon alpha-2a and Telbivudine may increase the risk of serious peripheral neuropathy. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10055 | Th1009 | Alteplase | >Th1009_Alteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Ophthalmologicals, Peptide Hydrolases, Plasminogen Activators, Proteins, Sensory Organs, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator, Tissue Plasminogen Activator, antagonists & inhibitors | NA | NA | NA | Ginkgo biloba.Additive anticoagulant/antiplatelet effects may increase bleeding risk. Concomitant therapy should be avoided. | Plasminogen,Fibrinogen alpha chain,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1 | Activase | Genentech Inc | Genentech Inc | To treat blood clots in the lungs and improve heart function and survival followed by a heart attack. Activase may also be used to improve recovery and reduce disability in certain patients who have suffered from a stroke. | NA | NA | Sterile, white to off-white, lyophilized powder | Intravenous | The recommended dose is not to exceed 100 mg. Patients weighing > 67 kg are recommended a dose of 100 mg as a 15 mg intravenous bolus, followed by 50 mg infused over the next 30 minutes, and then 35 mg infused over the next 60 minutes. | Allergic | Rash; hives; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue. | Link | NA | NA |
| 10056 | Th1009 | Alteplase | >Th1009_Alteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Ophthalmologicals, Peptide Hydrolases, Plasminogen Activators, Proteins, Sensory Organs, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator, Tissue Plasminogen Activator, antagonists & inhibitors | NA | NA | NA | IV nitroglycerin may decrease the effect of alteplase. | NA | Cathflo | Hoffmann La Roche | Hoffmann La Roche | NA | NA | NA | NA | NA | NA | Have active internal bleeding, history of stroke, recent brain or spinal surgery (within 3 months), a growth in the brain, abnormal formation of blood vessels. | Black or bloody stools; bloody vomit; change in color of your fingers or toes; changes in vision; chills; coughing up blood; decreased amount of urine produced; difficulty breathing or sudden shortness of breath; difficulty swallowing. | Link | NA | NA |
| 10057 | Th1009 | Alteplase | >Th1009_Alteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Ophthalmologicals, Peptide Hydrolases, Plasminogen Activators, Proteins, Sensory Organs, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator, Tissue Plasminogen Activator, antagonists & inhibitors | NA | NA | NA | Ticlopidine.Increased bleeding risk. Monitor for signs of bleeding. | NA | Cathflo Activase | Genentech, Inc | Genentech, Inc | Used to treat the symptoms of Acute Myocardial Infarction, Pulmonary Embolism, Acute Ischemic Stroke, and Central Venous Catheter Occlusion | NA | Each vial of Cathflo Activase contains 2.2 mg of Alteplase (which includes a 10% overfill), 77 mg of Larginine, 0.2 mg of polysorbate 80, and phosphoric acid for pH adjustment. Each reconstituted vial will deliver 2 mg of Cathflo Activase, at a pH of approximately 7.3. | sterile, white to pale yellow, lyophilized powder | Injection for intracatheter instillation for restoration of function to central venous access devices following reconstitution with Sterile Water for Injection, USP. | Cathflo® Activase® (Alteplase) is for instillation into the dysfunctional catheter at a concentration of 1 mg/mL. Patients weighing ≥30 kg: 2 mg in 2 mL Patients weighing <30 kg: 110% of the internal lumen volume of the catheter, not to exceed 2 mg in 2 mL | Cathflo Activase should not be administered to patients with known hypersensitivity to Alteplase or any component of the formulation | hives, difficulty breathing, swelling of your face, lips, tongue, or throat, any bleeding that will not stop, sudden headache, weakness, dizziness, bleeding gums, nosebleeds, easy bruising, bleeding from a wound, incision, catheter, or needle injection, bloody or tarry stools, coughing up blood, vomit that looks like coffee grounds, red or pink urine, heavy menstrual periods, abnormal vaginal bleeding, sudden numbness or weakness (especially on one side of the body), slurred speech, problems with vision or balance, chest pain or pressure, pain spreading to the jaw or shoulder, nausea, sweating, general ill feeling, sudden severe back pain, muscle weakness, numbness or loss of feeling in your arms or legs, swelling, rapid weight gain, little or nor urination, severe stomach pain, vomiting, darkening or purple discoloration of your fingers or toes, very slow heartbeats, shortness of breath, lightheadedness, sudden severe back pain, severe headache, blurred vision, pounding in your neck or ears, and anxiety | Link | NA | NA |
| 10058 | Th1009 | Alteplase | >Th1009_Alteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Ophthalmologicals, Peptide Hydrolases, Plasminogen Activators, Proteins, Sensory Organs, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator, Tissue Plasminogen Activator, antagonists & inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | History of bleeding problems, or severe uncontrolled high blood pressure. | Sudden arm or leg pain; sudden dizziness, fainting, severe headache, or vomiting; unusual or easy bleeding or bruising. | NA | NA | NA |
| 10059 | Th1010 | Interferon alfa-n1 | >Th1010_Interferon_alfa-n1 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | 1.2 hours (mammalian reticulocytes, in vitro) | Purified, natural and glycosylated human interferon alpha proteins of 166 residues. | Used to treat venereal or genital warts caused by the Human Papiloma Virus. | Upregulates the expression of MHC I proteins, allowing increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5-oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors namely IFNAR1 and IFNAR2c which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Interferon increases the effect and toxicity of theophylline | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Wellferon | GlaxoSmithKline | GlaxoSmithKline | Used for the treatment of patients with hairy cell leukemia, juvenile laryngeal papillomatosis, condylomata acuminata, chronic hepatitis B and chronic hepatitis C infections. | NA | Each vial of clear, colorless solution contains interferon alpha-n1 (lns) [purified human lymphoblastoid interferon] 3, 5 or 10 mega units. 1 mega unit (Mu)=1´10International Units (IU) of lymphoblastoid interferon. Formulated in 1 mL tris-glycine buffere | Solution | Injection | NA | Hypersensitivity | Most side/adverse effects, except the flu-like syndrome, are dose-related . They are usually mild to moderate at systemic doses less than 10 million Units per day }; hematologic and hepatic toxicities tend to be more frequent with doses above 10 million | Link | NA | NA |
| 10060 | Th1010 | Interferon alfa-n1 | >Th1010_Interferon_alfa-n1 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | 20 hours (yeast, in vivo) | Purified, natural and glycosylated human interferon alpha proteins of 166 residues. | Used to treat venereal or genital warts caused by the Human Papiloma Virus. | Upregulates the expression of MHC I proteins, allowing increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5-oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors namely IFNAR1 and IFNAR2c which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Aminophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Reduced blood pressure occurs frequently with systemic use but is rarely symptomatic ; hypotension may occur during administration or up to two days after therapy, and may require supportive therapy including fluid replacement to maintain intravascular v | Link | NA | NA |
| 10061 | Th1010 | Interferon alfa-n1 | >Th1010_Interferon_alfa-n1 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | 10 hours (Escherichia coli, in vivo) | Purified, natural and glycosylated human interferon alpha proteins of 166 residues. | Used to treat venereal or genital warts caused by the Human Papiloma Virus. | Upregulates the expression of MHC I proteins, allowing increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5-oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors namely IFNAR1 and IFNAR2c which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Dyphylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Development of neutralizing antibodies has been reported. Relationship of the presence of neutralizing antibodies to loss of antitumor effects is controversial; a possible correlation with titer of neutralizing antibodies has been suggested but not confirmed. | NA | NA | NA |
| 10062 | Th1010 | Interferon alfa-n1 | >Th1010_Interferon_alfa-n1 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | NA | Purified, natural and glycosylated human interferon alpha proteins of 166 residues. | Used to treat venereal or genital warts caused by the Human Papiloma Virus. | Upregulates the expression of MHC I proteins, allowing increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5-oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors namely IFNAR1 and IFNAR2c which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Oxtriphylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10063 | Th1010 | Interferon alfa-n1 | >Th1010_Interferon_alfa-n1 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | NA | Purified, natural and glycosylated human interferon alpha proteins of 166 residues. | Used to treat venereal or genital warts caused by the Human Papiloma Virus. | Upregulates the expression of MHC I proteins, allowing increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5-oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors namely IFNAR1 and IFNAR2c which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10067 | Th1012 | Reteplase | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 39589.6 | C1736H2671N499O522S22 | 6.86 | -0.435 | 60 | NA | Human tissue plasminogen activator which is glycosylated and purified (355 residues) from CHO cells. Retavase is considered a third-generation thrombolytic agent, genetically engineered to retain and delete certain portions of human tPA. Retavase is a deletion mutein of human tPA formed by deleting various amino acids present in endogenous human tPA. Retavase contains 355 of the 527 amino acids of native human tPA (amino acids 1-3 and 176-527), and retains the activity-related kringle-2 and serine protease domains of human tPA. Three domains are deleted from retavase – kringle-1, finger, and epidermal growth factor (EGF). | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. | Reteplase cleaves Arg/Val bonds in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that further cause myocardial infarction. | Reteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | CA2107476 | 18-Dec-2007 | 15-Apr-2012 | Additive anticoagulant/antiplatelet effects may increase bleed risk. Concomitant therapy should be avoided with Ginkgo biloba | Plasminogen,Fibrinogen alpha chain,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1 | Retavase | Centocor | Centocor | Improves heart function and reduces long-term effects of a heart attack. | NA | Each single-use vial contains:Reteplase 18.1 mg, Tranexamic Acid 8.32 mg, Dipotassium Hydrogen Phosphate 136.24 mg, Phosphoric Acid 51.27 mg, Sucrose 364.0 mg, Polysorbate 805.20 mg | Sterile, white, lyophilized powder | Intravenous Injection | Retavase is administered as a 10 + 10 unit double-bolus injection. Two 10 unit bolus injections are required for a complete treatment. Each bolus is administered as an Intravenous infusion over 2 minutes. The second bolus is given 30 minutes after initial one. | Allergic, or you have an aneurysm, heart or blood vessel defects, bleeding disorders | Rash; hives; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue. | Link | NA | NA |
| 10068 | Th1012 | Reteplase | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 39589.6 | C1736H2671N499O522S22 | 6.86 | -0.435 | 60 | NA | Human tissue plasminogen activator which is glycosylated and purified (355 residues) from CHO cells. Retavase is considered a third-generation thrombolytic agent, genetically engineered to retain and delete certain portions of human tPA. Retavase is a deletion mutein of human tPA formed by deleting various amino acids present in endogenous human tPA. Retavase contains 355 of the 527 amino acids of native human tPA (amino acids 1-3 and 176-527), and retains the activity-related kringle-2 and serine protease domains of human tPA. Three domains are deleted from retavase – kringle-1, finger, and epidermal growth factor (EGF). | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. | Reteplase cleaves Arg/Val bonds in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that further cause myocardial infarction. | Reteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exe | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | NA | NA | NA | Increased bleeding risk. Monitor for signs of bleeding when given in combination with Ticlopidine | NA | NA | KR Therapeutics Inc. | KR Therapeutics Inc. | NA | NA | NA | NA | NA | NA | Severe uncontrolled high blood pressure | Black, tarry stools; bleeding at the injection site | Link | NA | NA |
| 10069 | Th1012 | Reteplase | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 39589.6 | C1736H2671N499O522S22 | 6.86 | -0.435 | 60 | NA | Human tissue plasminogen activator which is glycosylated and purified (355 residues) from CHO cells. Retavase is considered a third-generation thrombolytic agent, genetically engineered to retain and delete certain portions of human tPA. Retavase is a deletion mutein of human tPA formed by deleting various amino acids present in endogenous human tPA. Retavase contains 355 of the 527 amino acids of native human tPA (amino acids 1-3 and 176-527), and retains the activity-related kringle-2 and serine protease domains of human tPA. Three domains are deleted from retavase – kringle-1, finger, and epidermal growth factor (EGF). | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. | Reteplase cleaves Arg/Val bonds in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that further cause myocardial infarction. | Reteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exe | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | NA | NA | NA | NA | NA | NA | Hospira Inc. | Hospira Inc. | NA | NA | NA | NA | NA | NA | If you have had brain or spinal surgery; or you have suffered recent trauma | Vomiting blood or material that looks like coffee grounds | Link | NA | NA |
| 10070 | Th1012 | Reteplase | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 39589.6 | C1736H2671N499O522S22 | 6.86 | -0.435 | 60 | NA | Human tissue plasminogen activator which is glycosylated and purified (355 residues) from CHO cells. Retavase is considered a third-generation thrombolytic agent, genetically engineered to retain and delete certain portions of human tPA. Retavase is a deletion mutein of human tPA formed by deleting various amino acids present in endogenous human tPA. Retavase contains 355 of the 527 amino acids of native human tPA (amino acids 1-3 and 176-527), and retains the activity-related kringle-2 and serine protease domains of human tPA. Three domains are deleted from retavase – kringle-1, finger, and epidermal growth factor (EGF). | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. | Reteplase cleaves Arg/Val bonds in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that further cause myocardial infarction. | Reteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exe | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | NA | NA | NA | NA | NA | NA | PDL BioPharma Inc. | PDL BioPharma Inc. | NA | NA | NA | NA | NA | NA | A history of stroke, or internal bleeding | Chest pain; severe bleeding; sudden, severe headache; trouble breathing | NA | NA | NA |
| 10110 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Alferon | AIM ImmunoTech Inc | AIM ImmunoTech Inc | Used to treat genital warts (condylomata acuminata) | NA | NA | Solution | Injection | 0.05 mL (250,000 international units) per wart, injected intralesionally twice a week for up to 8 weeks. The maximum recommended dosage per treatment session is 0.5 mL (2.5 million international units). | Allergic to any ingredient in Alferon solution, including egg protein or neomycin | Appetite loss; changes in taste or hearing; chills; diarrhea; fatigue; flu-like symptoms; headache; muscle and joint pain; nausea; pain or other reaction at the site of injection; stomach pain; vomiting. | Link | NA | NA |
| 10111 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Rash; hives; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; black, tarry stools; bloody diarrhea; chest pain; dark urine or changes in amount of urine; depression; difficulty sleeping; dizziness; drowsiness; intolerance to heat or cold; irregular heartbeat; one-sided weakness (arm, leg); persistent sore throat; poor coordination; pounding in the chest; psychotic or manic behavior; seizures; severe stomach/abdominal pain; suicidal thoughts; tingling hands or feet; unusual bleeding/bruising; unusual increase in thirst; vision changes; vomiting blood; yellowing of the skin or eyes. | Link | NA | NA |
| 10112 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10113 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | Alferon LDO | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10114 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | Alferon N Injection | NA | NA | Used to treat genital warts (condylomata acuminata) | NA | NA | NA | NA | 0.05 mL (250,000 international units) per wart, injected intralesionally twice a week for up to 8 weeks. The maximum recommended dosage per treatment session is 0.5 mL (2.5 million international units). | Allergic to to any ingredient in Alferon solution, including egg protein or neomycin | Appetite loss; changes in taste or hearing; chills; diarrhea; fatigue; flu-like symptoms; headache; muscle and joint pain; nausea; pain or other reaction at the site of injection; stomach pain; vomiting. | Link | NA | NA |
| 10115 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Rash; hives; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; black, tarry stools; bloody diarrhea; chest pain; dark urine or changes in amount of urine; depression; difficulty sleeping; dizziness; drowsiness; intolerance to heat or cold; irregular heartbeat; one-sided weakness (arm, leg); persistent sore throat; poor coordination; pounding in the chest; psychotic or manic behavior; seizures; severe stomach/abdominal pain; suicidal thoughts; tingling hands or feet; unusual bleeding/bruising; unusual increase in thirst; vision changes; vomiting blood; yellowing of the skin or eyes. | Link | NA | NA |
| 10116 | Th1015 | Interferon alfa-n3 | >Th1015_Interferon_alfa-n3 CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | NA | NA | 5.99 | NA | 61 | NA | Purified, natural human interferon alpha proteins consisting of 3 forms or polymorphisms including 2a, 2b and 2c. It consists of 166 residues(MW range from 16 kD to 27 kD) out of which some are glycosylated. | For the intralesional treatment of refractory or recurring external condylomata acuminata. | Interferon alfa-n3 upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes and make the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | NA | NA | NA | Alfa Interferons, Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10135 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | CA1341567 | 19-Feb-2008 | 19-Feb-2025 | Aminophylline. Interferon increases the effect and toxicity of theophylline | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | PEG-Intron | Schering Corp | Schering Corp | Used to treat chronic hepatitis C in adults. Peginterferon alfa-2b is often used in combination with another medication called ribavirin (Rebetol, Ribasphere) to treat hepatitis C in adults and children who are at least 3 years old. It may be used in comb | NA | Provided in both vials and the REDIPEN. Each vial contains either 74 mcg, 118.4 mcg, 177.6 mcg, or 222 mcg of PegIntron as a white to off-white tablet-like solid that is whole/in pieces or as a loose powder, and 1.11 mg dibasic sodium phosphate anhydrous, | Powder | Subcutaneous Injection | 1.5 mcg/kg/week. The volume of PegIntron to be injected depends on the strength of PegIntron and patient's body weight | Allergic or in case of having autoimmune hepatitis, liver failure, severe kidney disease, a hemoglobin blood cell disorder | Vision problems; fast heart rate, feeling like you might pass out; unusual weakness; high fever with severe stomach pain and bloody diarrhea; pain or burning when you urinate; severe pain in your upper stomach spreading to your back, nausea and vomiting and new or worsening liver symptoms. | Link | NA | NA |
| 10136 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | CA2329474 | 26-Feb-2002 | 31-Oct-2016 | Dyphylline.Interferon increases the effect and toxicity of theophylline | NA | Sylatron | Merck Sharp & Dohme Corp. | Merck Sharp & Dohme Corp. | SYLATRON™ is an alpha interferon indicated for the adjuvant treatment of melanoma with microscopic or gross nodal involvement within 84 days of definitive surgical resection including complete lymphadenect | NA | NA | sterile, white to off-white lyophilized powder | Subcutaneous Injection | The recommended starting dose is 6 mcg/kg/week subcutaneously for 8 doses, followed by 3 mcg/kg/week subcutaneously for up to 5 years. Premedicate with acetaminophen 500 to 1000 mg orally 30 minutes prior to the first dose of SYLATRON and as needed for subsequent doses. The recommended starting doses of SYLATRON in patients with moderate or severe renal impairment or end-stage renal disease (ESRD) are listed in Table 1 [see Use In Specific Populations]. No dose adjustment is needed for patients with a creatinine clearance (CLcr) > 50 mL/min/1.73m². | SYLATRON is contraindicated in patients with: A history of anaphylaxis to peginterferon alfa-2b or interferon alfa-2b autoimmune hepatitis hepatic decompensation (Child-Pugh score >6 [class B and C]) | Headache, joint or muscle pain; nausea, dry mouth, loss of appetite, weight loss; dizziness, sleep problems (insomnia), feeling mildly anxious, depressed, or irritable; or pain, redness, swelling, or irritation where the medicine was injected. | Link | NA | NA |
| 10137 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Oxtriphylline. Interferon increases the effect and toxicity of theophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10138 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Theophylline. Interferon increases the effect and toxicity of theophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10139 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Aldesleukin | NA | Unitron PEG | Merck Ltd. | Merck Ltd. | It is used to treat chronic hepatitis C (a disease of the liver) for people who cannot tolerate or use the antiviral medication, ribavirin. The most effective treatment of chronic hepatitis C is the combination of an interferon and ribavirin. Unitron Peg | NA | NA | Lyophilized powder | Subcutaneous Injection | Its Subcutaneous injection once a week on the same day of the week for 48 weeks. Dosing is based on body weight. Treatment with this medication should be stopped if no response is noticed after 6 months. | Allergic | Abdominal pain or swelling, anemia (paleness, tiredness, shortness of breath), changes in mood (e.g., irritability, depression, anxiety, aggression), confusion, dizziness, eye pain or swelling of the eye, high blood sugar (increased thirst, hunger, weakness, irritability, trouble concentrating, signs of infection (e.g., chills, fever, cough, sore throat, difficulty or painful urination, difficulty breathing), burning sensation in arms or legs, ulcers in mouth or sore throats. | Link | NA | NA |
| 10140 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Telbivudine | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Person having decompensated liver disease, epilepsy (seizures), autoimmune diseases (including autoimmune hepatitis), severe psychiatric conditions, severely reduced kidney function and thyroid disease, when medication cannot bring thyroid function in | Signs of infection (e.g., chills, fever, cough, sore throat, difficulty or painful urination, difficulty breathing), tingling or burning sensation in arms or legs, ulcers or sores in the mouth or throat, unusual bruising or bleeding (e.g., bleeding gums, | Link | NA | NA |
| 10141 | Th1019 | Peginterferon alfa-2b | >Th1019_Peginterferon_alfa-2b CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 31000 | C130H219N43O42 | 5.99 | NA | 61 | Approximately 40 hours (range 22 to 60 hours) in patients with HCV infection | Peginterferon alfa-2b is a covalent conjugate of recombinant alfa-2b interferon with monomethoxy polyethylene glycol (PEG). The average molecular weight of the PEG portion of the molecule is 12,000 daltons. The average molecular weight of the PEG-Intron molecule is approximately 31,000 daltons. The specific activity of peginterferon alfa-2b is approximately 0.7 x 108 IU/mg protein. Interferon alfa-2b is a water-soluble protein with a molecular weight of 19,271 daltons produced by recombinant DNA techniques. It is obtained from the bacterial fermentation of a strain of Escherichia coli bearing a genetically engineered plasmid containing an interferon gene from human leukocytes. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. | Used for the treatment of chronic hepatitis C in patients not previously treated with interferon alpha who have compensated liver disease and are at least 18 years of age. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds to type I interferon receptors IFNAR1 and IFNAR2c which upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | NA | NA | After a single subcutaneous dose of peginterferon alfa-2b, the mean absorption half-life was 4.6 hours. | NA | Oral cl=22 mL/hr/kg [patients with HCV infection], Renal elimination accounts for 30% of the clearance. | Adjuvants, Immunologic, Alcohols, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Compounds used in a research, industrial, or household setting, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 CYP2C9 Inducers, Cytochrome P-450 CYP2C9 Inducers (weak), Cytochrome P-450 CYP2D6 Inhibitors, Cytochrome P-450 CYP2D6 Inhibitors (weak), Cytochrome P-450 Enzyme Inducers, Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drug Carriers, Ethylene Glycols, Glycols, Hepatitis C, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Macromolecular Substances, Myelosuppressive Agents, Pegylated agents, Peptides, Polymers, Proteins, Treatments for Hepatitis C | NA | NA | NA | Theophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Decreased desire for sexual activities, drowsiness, dry mouth, dry skin, flu-like symptoms (unusual tiredness, fever, chills, muscle aches, joint pain and headaches), flushing of the skin, indigestion, loss of appetite, nausea, pain in bones, joints, or muscle stiffness. | Link | NA | NA |
| 10142 | Th1020 | Asparaginase | >Th1020_Asparaginase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | 8-30 hours | L-asparagine amidohydrolase from E. coli | To treat acute lympocytic leukemia and non-Hodgkins lymphoma | In most patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Elspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Asparaginase converts asparagine to aspartic acid and ammonia. It facilitates production of oxalo-acetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and thus the loss of exogenous sources of asparagine leads to cell death. | NA | NA | NA | Apparent volume of distribution was slightly greater than the plasma volume. Asparaginase levels in cerebrospinal fluid were less than 1% of concurrent plasma levels | NA | Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Enzymes, Enzymes and Coenzymes, Hydrolases, Narrow Therapeutic Index Drugs, Thyroxine-binding globulin inhibitors | NA | NA | NA | Trastuzumab may increase the risk of neutropenia and anemia. Monitor closely for signs and symptoms of adverse events. | L-asparagine | Elspar | Lundbeck Inc. | Lundbeck Inc. | To treat acute lymphocytic leukemia. It is used along with other cancer medicines. Elspar is an antineoplastic agent that works by decreasing the amount of asparagine in the body, which kills certain leukemia cells | NA | Each vial contains 10,000 International Units of asparaginase and 80 mg of mannitol. | Lyophilized plug or powder | Intravenous or intramuSubcutaneousular. Intravenou | The recommended dose of Elspar is 6,000 International Units/m_ intramuscularly (IM) or intravenously (IV) three times a week. | Allergic | Fever, chills (see flu like symptoms), Nausea and vomiting, Allergic reaction, (sudden onset of wheezing, itching, rash, face swelling, agitation, low blood pressure). You will be monitored closely for this reaction, Poor appetite, Stomach cramping | Link | NA | NA |
| 10143 | Th1020 | Asparaginase | >Th1020_Asparaginase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | 8-30 hours | L-asparagine amidohydrolase from E. coli | To treat acute lympocytic leukemia and non-Hodgkins lymphoma | In most patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Elspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Asparaginase converts asparagine to aspartic acid and ammonia. It facilitates production of oxalo-acetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and thus the loss of exogenous sources of asparagine leads to cell death. | NA | NA | NA | Apparent volume of distribution was slightly greater than the plasma volume. Asparaginase levels in cerebrospinal fluid were less than 1% of concurrent plasma levels | NA | Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Enzymes, Enzymes and Coenzymes, Hydrolases, Narrow Therapeutic Index Drugs, Thyroxine-binding globulin inhibitors | NA | NA | NA | NA | NA | Kidrolase | Jazz Pharmaceuticals France Sas | Jazz Pharmaceuticals France Sas | NA | NA | NA | NA | NA | NA | NA | Mouth sores, Pancreatitis (inflammation of the pancreas) in up to 10% of patients. Mainly noted in blood tests that return to normal after therapy is discontinued. Rarely may be severe causing symptoms. Symptoms of acute pancreatitis include: (pain in the upper abdomen that worsens with eating, swollen and tender abdomen, nausea, vomiting, fever, and rapid pulse). | Link | NA | NA |
| 10144 | Th1020 | Asparaginase | >Th1020_Asparaginase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | 8-30 hours | L-asparagine amidohydrolase from E. coli | To treat acute lympocytic leukemia and non-Hodgkins lymphoma | In most patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Elspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Asparaginase converts asparagine to aspartic acid and ammonia. It facilitates production of oxalo-acetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and thus the loss of exogenous sources of asparagine leads to cell death. | NA | NA | NA | Apparent volume of distribution was slightly greater than the plasma volume. Asparaginase levels in cerebrospinal fluid were less than 1% of concurrent plasma levels | NA | Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Enzymes, Enzymes and Coenzymes, Hydrolases, Narrow Therapeutic Index Drugs, Thyroxine-binding globulin inhibitors | NA | NA | NA | NA | NA | Rylaze, Spectrila | Jazz Pharmaceuticals, Inc., Medac Gesellschaft Fuer Klinische Spezialpraeparate Mb H | Jazz Pharmaceuticals, Inc., Medac Gesellschaft Fuer Klinische Spezialpraeparate Mb H | NA | NA | NA | NA | NA | NA | NA | Central neurotoxicity: excessive sleepiness, depression, hallucinations, agitation, disorientation or seizure, stupor, confusion and/or coma. | Link | NA | NA |
| 10201 | Th1026 | Anistreplase | >Th1026_Anistreplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Human tissue plasminogen activator, purified, glycosylated, 527 residues purified from CHO cells. Eminase is a lyophilized (freeze-dried) formulation of anistreplase, the p-anisoyl derivative of the primary Lys-plasminogen-streptokinase activator complex (a complex of Lys-plasminogen and streptokinase). A p-anisoyl group is chemically conjugated to a complex of bacterial-derived streptokinase and human Plasma-derived Lys-plasminogen proteins. | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | The use of anistreplase with other cardioactive drugs has not been studied. In addition to bleeding associated with heparin and vitamin K antagonists, drugs that alter platelet function (such as ASA and dipyridamole) may increase the risk of bleeding | Plasminogen,Fibrinogen alpha chain,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1 | Eminase | Wulfing Pharma GmbH | Wulfing Pharma GmbH | For use in the management of ( acute myocardial infarction) AMI in adults for the lysis of thrombi obstructing coronary arteries, the reduction of infarct size, the improvement of ventricular function following AMI, and the reduction of mortality associat | NA | Each unit-dose vial of sterile lyophilized, white to off-white powder contains: anistreplase 30 units, dimethylsulfoxide <3 mg, sodium hydroxide <0.2 mg and the following buffers or stabilizers: p-amidinophenyl-p'-anisate (acylating agent) 150 µg, mannito | Dry powder | Intravenous infusion | 30 units of anistreplase administered only by i.v. injection over 2 to 5 minutes into an i.v. line or vein. | Allergic, active internal bleeding; history of cerebrovascular accident (CVA); patients receiving other i.v. thrombolytic agents; recent (within 2 months) intracranial or intraspinal surgery or trauma, intracranial neoplasm, arteriovenous malformation, or | NA | Link | NA | NA |
| 10202 | Th1026 | Anistreplase | >Th1026_Anistreplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Human tissue plasminogen activator, purified, glycosylated, 527 residues purified from CHO cells. Eminase is a lyophilized (freeze-dried) formulation of anistreplase, the p-anisoyl derivative of the primary Lys-plasminogen-streptokinase activator complex (a complex of Lys-plasminogen and streptokinase). A p-anisoyl group is chemically conjugated to a complex of bacterial-derived streptokinase and human Plasma-derived Lys-plasminogen proteins. | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10203 | Th1026 | Anistreplase | >Th1026_Anistreplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Human tissue plasminogen activator, purified, glycosylated, 527 residues purified from CHO cells. Eminase is a lyophilized (freeze-dried) formulation of anistreplase, the p-anisoyl derivative of the primary Lys-plasminogen-streptokinase activator complex (a complex of Lys-plasminogen and streptokinase). A p-anisoyl group is chemically conjugated to a complex of bacterial-derived streptokinase and human Plasma-derived Lys-plasminogen proteins. | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10204 | Th1026 | Anistreplase | >Th1026_Anistreplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 59042.3 | C2569H3928N746O781S40 | 7.61 | -0.516 | 60 | NA | Human tissue plasminogen activator, purified, glycosylated, 527 residues purified from CHO cells. Eminase is a lyophilized (freeze-dried) formulation of anistreplase, the p-anisoyl derivative of the primary Lys-plasminogen-streptokinase activator complex (a complex of Lys-plasminogen and streptokinase). A p-anisoyl group is chemically conjugated to a complex of bacterial-derived streptokinase and human Plasma-derived Lys-plasminogen proteins. | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Anistreplase cleaves the Arg/Val bond in plasminogen to form plasmin. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10205 | Th1027 | Insulin Regular | >Th1027_Insulin_Regular GIVEQCCTSICSLYQLENYCN | 5808 | C257H383N65O77S6 | 5.39 | 0.218 | 81 | 2-3.4 hours | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. | Hypoglycemia is caused due to insulin toxicity. | Predominantly cleared by metabolic degradation via a receptor-mediated process. | Generally well absorbed. | 0.15 L/kg | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin, metabolism, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | Liraglutide's coadministration may increase the risk of hypoglycemia. A lower dose of the antidiabetic agent may be needed. | Insulin receptor,Insulin-like growth factor 1 receptor,Retinoblastoma-associated protein,Cathepsin D,Insulin-degrading enzyme,Neuroendocrine convertase 2,Carboxypeptidase E,Neuroendocrine convertase 1,Protein NOV homolog,Low-density lipoprotein receptor-r | Humulin R | Eli Lilly and Company | Eli Lilly and Company | Treating diabetes mellitus. | NA | It contains human insulin (rDNA origin) 100 units/mL, glycerin 16 mg/mL and metacresol 2.5 mg/mL, endogenous zinc (approximately 0.015 mg/100 units) and water for injection. The pH is 7.0 to 7.8. Sodiumhydroxide and/or hydrochloric acid may be added durin | Sterile, clear, aqueous, and colorless solution | Subcutaneous Injection in the abdominal wall, the | Humulin R (insulin (human recombinant)) U-100, when used subcutaneously, is usually given three or more times daily before meals. The average range of total daily insulin requirement for maintenance therapy in insulin-treated patients without severe insulin resistance lies between 0.5 and 1 unit/kg/day. | During episodes of hypoglycemia and in patients hypersensitive to humulin R. | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; wheezing; muscle pain; changes in vision; chills; confusion; dizziness; drowsiness; fainting; fast or irregular heartbeat; headache; loss of apetite. | Link | NA | NA |
| 10206 | Th1027 | Insulin Regular | >Th1027_Insulin_Regular GIVEQCCTSICSLYQLENYCN | 5808 | C257H383N65O77S6 | 5.39 | 0.218 | 81 | 2-3.4 hours | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. | Hypoglycemia is caused due to insulin toxicity. | Predominantly cleared by metabolic degradation via a receptor-mediated process. | Generally well absorbed. | 0.15 L/kg | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin, metabolism, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | NA | NA | ACTRAPID INJECTION 100 IU/ml | NOVO NORDISK PHARMA (SINGAPORE) PTE LTD | NOVO NORDISK PHARMA (SINGAPORE) PTE LTD | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10207 | Th1027 | Insulin Regular | >Th1027_Insulin_Regular GIVEQCCTSICSLYQLENYCN | 5808 | C257H383N65O77S6 | 5.39 | 0.218 | 81 | 2-3.4 hours | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. | Hypoglycemia is caused due to insulin toxicity. | Predominantly cleared by metabolic degradation via a receptor-mediated process. | Generally well absorbed. | 0.15 L/kg | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin, metabolism, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | NA | NA | INSULATARD INJECTION 100 iu/ml | NOVO NORDISK PHARMA (SINGAPORE) PTE LTD | NOVO NORDISK PHARMA (SINGAPORE) PTE LTD | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10208 | Th1027 | Insulin Regular | >Th1027_Insulin_Regular GIVEQCCTSICSLYQLENYCN | 5808 | C257H383N65O77S6 | 5.39 | 0.218 | 81 | 2-3.4 hours | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. | Hypoglycemia is caused due to insulin toxicity. | Predominantly cleared by metabolic degradation via a receptor-mediated process. | Generally well absorbed. | 0.15 L/kg | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin, metabolism, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | NA | NA | Novolin R | Novo Nordisk | Novo Nordisk | Used for the treatment of patients with diabetes mellitus, for the control of hyperglycemia | NA | It contains human insulin (rDNA origin) 100 units/mL, glycerol 16 mg/mL, metacresol 3 mg/mL, zinc chloride approximately 7 mcg/mL and water for injection. The pH is adjusted to 7.4. Hydrochloric acid 2N or sodium hydroxide 2N may be added to adjust pH. No | Sterile, clear, aqueous, and colorless solution | Subcutaneous and Intravenous infusion | The injection of Novolin R (recombinant dna origin) should be followed by a meal within approximately 30 minutes of administration The average range of total daily insulin requirement for maintenance therapy in insulin-treated patients lies between 0.5 and 1.0 IU/kg. | During episodes of hypoglycemia and in patients with hypersensitivity to Novolin R | Hypoglycemia, or low blood sugar, is the most common side effect. Symptoms include headache, hunger, dizziness, sweating, irritability, trouble concentrating, rapid breathing, fast heartbeat, fainting, or seizure (severe hypoglycemia can be fatal). | Link | NA | NA |
| 10209 | Th1027 | Insulin Regular | >Th1027_Insulin_Regular GIVEQCCTSICSLYQLENYCN | 5808 | C257H383N65O77S6 | 5.39 | 0.218 | 81 | 2-3.4 hours | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. | Hypoglycemia is caused due to insulin toxicity. | Predominantly cleared by metabolic degradation via a receptor-mediated process. | Generally well absorbed. | 0.15 L/kg | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin, metabolism, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10210 | Th1028 | Tenecteplase | >Th1028_Tenecteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGNWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAAAAASPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 58951.2 | C2561H3919N747O781S40 | 7.61 | -0.528 | 60 | 1.9 hours (mammalian reticulocytes, in vitro) | Tenecteplase(527 amino acid) is a glycoprotein developed by introducing the following modifications to the complementary DNA for natural human tPA: a substitution of threonine 103 with asparagine, and a substitution of asparagine 117 with glutamine, both within the kringle 1 domain, and a tetra-alanine substitution at amino acids 296-299 in the protease domain. | To treat myocardial infarction and lysis of intracoronary emboli. | Tenecteplase is a fibrin-specific tissue-plasminogen activator. It binds to fibrin rich clots and cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Tenecteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | 99 - 119 mL/min [acute myocardial infarction patients] | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | CA2129660 | 28-Jun-2005 | 28-May-2013 | Aprotonin may antagonize the effect of Tenecteplase. Monitor for decreased effects of Tenecteplase. | Plasminogen,Fibrinogen alpha chain,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Calreticulin,Calnexin,Prolow-density lipoprotein | TNKase | Genentech Inc, Hoffmann La Roche | Genentech Inc, Hoffmann La Roche | To prevent death from a heart attack (acute myocardial infarction). | NA | Each vial of TNKase nominally contains 52.5 mg Tenecteplase, 0.55 g L-arginine, 0.17 g phosphoric acid, and 4.3 mg polysorbate 20, which includes a 5% overfill. Each vial will deliver 50 mg of Tenecteplase. | Sterile, white to off-white, lyophilized powder | Intravenous Injection | The recommended total dose should not exceed 50 mg and is based upon patient weight. For less than 60 kg of body weight recommended dose is 30 mg of TNKase. Similarly 35 mg for 60-70 kg, 40 mg for 70-80 kg, 45 mg for 80-90 kg and 50 mg for more than 90 kg. | Active internal bleeding, History of cerebrovascular accident | Nausea, vomiting; or fever. | Link | NA | NA |
| 10211 | Th1028 | Tenecteplase | >Th1028_Tenecteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGNWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAAAAASPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 58951.2 | C2561H3919N747O781S40 | 7.61 | -0.528 | 60 | 20 hours (yeast, in vivo) | Tenecteplase(527 amino acid) is a glycoprotein developed by introducing the following modifications to the complementary DNA for natural human tPA: a substitution of threonine 103 with asparagine, and a substitution of asparagine 117 with glutamine, both within the kringle 1 domain, and a tetra-alanine substitution at amino acids 296-299 in the protease domain. | To treat myocardial infarction and lysis of intracoronary emboli. | Tenecteplase is a fibrin-specific tissue-plasminogen activator. It binds to fibrin rich clots and cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Tenecteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | 99 - 119 mL/min [acute myocardial infarction patients] | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | CA1341432 | 17-Jun-2003 | 17-Jun-2020 | Drotrecogin alfa increases risk of bleeding. | NA | Metalyse | Boehringer Ingelheim | Boehringer Ingelheim | NA | NA | NA | NA | NA | NA | Intracranial neoplasm, Known bleeding diathesis | Chest pain, slow or uneven heartbeats; pain, swelling, hot or cold feeling, skin changes, or discoloration anywhere on your body; sudden leg or foot pain, foot ulcer, purple toes or fingers; swelling or severe pain or signs of infection in your fingers. | Link | NA | NA |
| 10212 | Th1028 | Tenecteplase | >Th1028_Tenecteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGNWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAAAAASPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 58951.2 | C2561H3919N747O781S40 | 7.61 | -0.528 | 60 | 10 hours (Escherichia coli, in vivo) | Tenecteplase(527 amino acid) is a glycoprotein developed by introducing the following modifications to the complementary DNA for natural human tPA: a substitution of threonine 103 with asparagine, and a substitution of asparagine 117 with glutamine, both within the kringle 1 domain, and a tetra-alanine substitution at amino acids 296-299 in the protease domain. | To treat myocardial infarction and lysis of intracoronary emboli. | Tenecteplase is a fibrin-specific tissue-plasminogen activator. It binds to fibrin rich clots and cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Tenecteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | 99 - 119 mL/min [acute myocardial infarction patients] | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | NA | NA | NA | Additive anticoagulant/antiplatelet effects may increase bleed risk, so Ginkgo biloba's (DB01381) concomitant therapy should be avoided. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Intracranial or intraspinal surgery or trauma within 2 months | Sudden numbness or weakness, problems with speech or balance, vision problems; little or no urinating; unexplained muscle pain. | NA | NA | NA |
| 10213 | Th1028 | Tenecteplase | >Th1028_Tenecteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGNWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAAAAASPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 58951.2 | C2561H3919N747O781S40 | 7.61 | -0.528 | 60 | NA | Tenecteplase(527 amino acid) is a glycoprotein developed by introducing the following modifications to the complementary DNA for natural human tPA: a substitution of threonine 103 with asparagine, and a substitution of asparagine 117 with glutamine, both within the kringle 1 domain, and a tetra-alanine substitution at amino acids 296-299 in the protease domain. | To treat myocardial infarction and lysis of intracoronary emboli. | Tenecteplase is a fibrin-specific tissue-plasminogen activator. It binds to fibrin rich clots and cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Tenecteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | 99 - 119 mL/min [acute myocardial infarction patients] | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | NA | NA | NA | Ginseng increases risk of bleeding. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Arteriovenous malformation or aneurysm | Muscle weakness or loss of function, loss of bowel or bladder control; or severe pain in your upper stomach spreading to your back. | NA | NA | NA |
| 10214 | Th1028 | Tenecteplase | >Th1028_Tenecteplase SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGNWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAAAAASPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | 58951.2 | C2561H3919N747O781S40 | 7.61 | -0.528 | 60 | NA | Tenecteplase(527 amino acid) is a glycoprotein developed by introducing the following modifications to the complementary DNA for natural human tPA: a substitution of threonine 103 with asparagine, and a substitution of asparagine 117 with glutamine, both within the kringle 1 domain, and a tetra-alanine substitution at amino acids 296-299 in the protease domain. | To treat myocardial infarction and lysis of intracoronary emboli. | Tenecteplase is a fibrin-specific tissue-plasminogen activator. It binds to fibrin rich clots and cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Tenecteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. | NA | NA | NA | NA | 99 - 119 mL/min [acute myocardial infarction patients] | Agents causing angioedema, Amino Acids, Peptides, and Proteins, Anticoagulants, Biological Factors, Blood and Blood Forming Organs, Blood Proteins, Cardiovascular Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Fibrin Modulating Agents, Fibrinolytic Agents, Hematologic Agents, Hydrolases, Peptide Hydrolases, Plasminogen Activators, Proteins, Serine Endopeptidases, Serine Proteases, Tissue Plasminogen Activator | NA | NA | NA | Ticlopidine increases bleeding risk. Monitor for signs of bleeding. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Severe uncontrolled hypertension | Tenderness, or weakness especially if you also have fever, unusual tiredness, and dark colored urine. | NA | NA | NA |
| 10226 | Th1030 | Interferon gamma-1b | >Th1030_Interferon_gamma-1b CYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ | 17145.6 | C761H1206N214O225S6 | 9.54 | -0.823 | 61 | NA | Human Interferon gamma-1b (140 residues), produced from E. coli. Production of Actimmune is achieved by fermentation of a genetically engineered Escherichia coli bacterium containing the DNA which encodes for the human protein. Purification of the product is achieved by conventional column chromatography. The sequence displayed is a cDNA sequence which codes for human interferon gamma, as described by Gray et. al. and not specifically interferon gamma 1b. | To treat Chronic granulomatous disease and Osteopetrosis. | IFN gamma stimulates expression of the immunoglobulin heavy chain C gamma 3 and C gamma 2a germline transcripts in B cells. Many components of the antigen presentation pathways are also up-regulated by interferon gamma. It is also a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of type I interferons. Interferon gamma may also help the body regulate the activity of fibroblasts. By directly blocking the multiplication of fibroblasts and inhibiting the production and action of TGF-b, a potent scar-inducing molecule, Interferon gamma-1b may prevent excessive scarring. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon gamma, Interferons, Lymphokines, Macrophage-Activating Factors, Myelosuppressive Agents, Peptides, Proteins | US6936695 | 30-Aug-2005 | 30-Aug-2022 | NA | Interferon gamma receptor 1,Interferon gamma receptor 2 | Actimmune | InterMune Inc, Hznp Usa, Inc., Horizon Therapeutics USA, Inc. | InterMune Inc, Hznp Usa, Inc., Horizon Therapeutics USA, Inc. | Used for reducing the number and severity of infections associated with chronic granulomatous disease. It is also used to delay the progression of severe, life-threatening bone density disease | NA | Each 0.5 mL of ACTIMMUNE contains 100 mcg (2 million IU) of Interferon gamma-1 b formulated in 20 mg mannitol, 0.36 mg sodium succinate, 0.05 mg polysorbate 20 and Sterile Water for Injection. | Sterile, clear, colorless solution | Subcutaneous Injection | Dose for the treatment of patients with Chronic Granulomatous Disease and severe, malignant osteopetrosis is 50 mcg/m2(1 million IU/m2) for patients whose body surface area is greater than 0.5 m2 and 1.5 mcg/kg/dose for patients whose body surface area is equal to or less than 0.5 m2. | Hypersensitivity | Diarrhea; fatigue; flu-like symptoms (eg, low-grade fever, chills, general body discomfort); headache; joint pain; muscle pain; nausea; pain, redness, or swelling at the injection site; tiredness; vomiting; weakness. Severe side efects include Severe dizziness and troubled breathing. | Link | NA | NA |
| 10227 | Th1030 | Interferon gamma-1b | >Th1030_Interferon_gamma-1b CYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ | 17145.6 | C761H1206N214O225S6 | 9.54 | -0.823 | 61 | NA | Human Interferon gamma-1b (140 residues), produced from E. coli. Production of Actimmune is achieved by fermentation of a genetically engineered Escherichia coli bacterium containing the DNA which encodes for the human protein. Purification of the product is achieved by conventional column chromatography. The sequence displayed is a cDNA sequence which codes for human interferon gamma, as described by Gray et. al. and not specifically interferon gamma 1b. | To treat Chronic granulomatous disease and Osteopetrosis. | IFN gamma stimulates expression of the immunoglobulin heavy chain C gamma 3 and C gamma 2a germline transcripts in B cells. Many components of the antigen presentation pathways are also up-regulated by interferon gamma. It is also a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of type I interferons. Interferon gamma may also help the body regulate the activity of fibroblasts. By directly blocking the multiplication of fibroblasts and inhibiting the production and action of TGF-b, a potent scar-inducing molecule, Interferon gamma-1b may prevent excessive scarring. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon gamma, Interferons, Lymphokines, Macrophage-Activating Factors, Myelosuppressive Agents, Peptides, Proteins | US6936694 | 30-Aug-2005 | 30-Aug-2022 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10228 | Th1030 | Interferon gamma-1b | >Th1030_Interferon_gamma-1b CYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ | 17145.6 | C761H1206N214O225S6 | 9.54 | -0.823 | 61 | NA | Human Interferon gamma-1b (140 residues), produced from E. coli. Production of Actimmune is achieved by fermentation of a genetically engineered Escherichia coli bacterium containing the DNA which encodes for the human protein. Purification of the product is achieved by conventional column chromatography. The sequence displayed is a cDNA sequence which codes for human interferon gamma, as described by Gray et. al. and not specifically interferon gamma 1b. | To treat Chronic granulomatous disease and Osteopetrosis. | IFN gamma stimulates expression of the immunoglobulin heavy chain C gamma 3 and C gamma 2a germline transcripts in B cells. Many components of the antigen presentation pathways are also up-regulated by interferon gamma. It is also a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of type I interferons. Interferon gamma may also help the body regulate the activity of fibroblasts. By directly blocking the multiplication of fibroblasts and inhibiting the production and action of TGF-b, a potent scar-inducing molecule, Interferon gamma-1b may prevent excessive scarring. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon gamma, Interferons, Lymphokines, Macrophage-Activating Factors, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10229 | Th1031 | Interferon Alfa-2a, Recombinant | >Th1031_Interferon_Alfa-2a,_Recombinant CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | NA | IM half-life of interferon alfa-2a is 6 hours to 8 hours | Its a type I interferon consisting of 165 amino acid residues with lysine in position 23. This protein is produced by recombinant DNA technology and resembles interferon secreted by leukocytes. It is used extensively as an antiviral or antineoplastic agent. An oral form is being developed by Amarillo Biosciences. | For the treatment of chronic hepatitis C, hairy cell leukemia, AIDS-related Kaposi's sarcoma, and chronic myelogenous leukemia. Also for the treatment of oral warts arising from HIV infection. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a bbetter target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | Interferon alfa-2 may cause serious adverse effects such as anemia; autoimmune diseases, including vasculitis, arthritis, hemolytic anemia, and erythematosus syndrome; cardiotoxicity; hepatotoxicity; hyperthyroidism or hypothyroidism; transient ischemic a | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | 0.223 to 0.748 L/kg [healthy people] | 2.14 - 3.62 mL/min/kg [healthy] | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | CA2172664 | 3-Oct-2000 | 26-Mar-2016 | Interferon increases the effect and toxicity of theophylline | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Roferon A | Hoffmann-La Roche Inc | Hoffmann-La Roche Inc | To treat chronic hepatitis C and hairy cell leukemia in patients 18 years of age or older. In addition, it is indicated for chronic phase, Philadelphia chromosome (Ph) positive chronic myelogenous leukemia (CML) patients who are minimally pretreated (with | NA | 3 million IU (11.1 mcg/0.5 mL) Roferon-A (interferon alfa-2a, recombinant) per syringe  The solution is colorless and each 0.5 mL contains 3 MIU of Interferon alfa-2a, recombinant, 3.605 mg sodium chloride, 0.1 mg polysorbate 80, 5 mg benzyl alcohol as a | Solution | Subcutaneous Injection | Dosage for the treatment of chronic hepatitis C is 3 MIU three times a week (tiw) administered subcutaneously for 12 months (48-52 weeks). As an alternative, patients may be treated with an induction dose of 6 MIU tiw for the first 3 months (12 weeks) followed by 3 MIU tiw for 9 months (36 weeks). | Hypersensitivity to Roferon-A (interferon alfa-2a, recombinant) or any of its components | Injection site reactions (pain/swelling/redness), headache, tiredness, diarrhea, upset stomach, loss of appetite, back pain, dizziness, dry mouth, taste changes, nausea, or vomiting may occur. Tooth and gum problems may sometimes occur during treatment. | Link | NA | NA |
| 10230 | Th1031 | Interferon Alfa-2a, Recombinant | >Th1031_Interferon_Alfa-2a,_Recombinant CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | NA | Half-life for IV infusion is 3.7 hours to 8.5 hours (mean 5.1 hours). | Its a type I interferon consisting of 165 amino acid residues with lysine in position 23. This protein is produced by recombinant DNA technology and resembles interferon secreted by leukocytes. It is used extensively as an antiviral or antineoplastic agent. An oral form is being developed by Amarillo Biosciences. | For the treatment of chronic hepatitis C, hairy cell leukemia, AIDS-related Kaposi's sarcoma, and chronic myelogenous leukemia. Also for the treatment of oral warts arising from HIV infection. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a bbetter target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | Interferon alfa-2 may cause serious adverse effects such as anemia; autoimmune diseases, including vasculitis, arthritis, hemolytic anemia, and erythematosus syndrome; cardiotoxicity; hepatotoxicity; hyperthyroidism or hypothyroidism; transient ischemic a | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | 0.223 to 0.748 L/kg [healthy people] | 2.14 - 3.62 mL/min/kg [healthy] | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Aminophylline interferon increases the effect and toxicity of theophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Autoimmune hepatitis or hepatic decompensation (Child-Pugh class B and C) before or during treatment. | NA | Link | NA | NA |
| 10231 | Th1031 | Interferon Alfa-2a, Recombinant | >Th1031_Interferon_Alfa-2a,_Recombinant CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | NA | NA | Its a type I interferon consisting of 165 amino acid residues with lysine in position 23. This protein is produced by recombinant DNA technology and resembles interferon secreted by leukocytes. It is used extensively as an antiviral or antineoplastic agent. An oral form is being developed by Amarillo Biosciences. | For the treatment of chronic hepatitis C, hairy cell leukemia, AIDS-related Kaposi's sarcoma, and chronic myelogenous leukemia. Also for the treatment of oral warts arising from HIV infection. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a bbetter target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | Interferon alfa-2 may cause serious adverse effects such as anemia; autoimmune diseases, including vasculitis, arthritis, hemolytic anemia, and erythematosus syndrome; cardiotoxicity; hepatotoxicity; hyperthyroidism or hypothyroidism; transient ischemic a | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | 0.223 to 0.748 L/kg [healthy people] | 2.14 - 3.62 mL/min/kg [healthy] | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Dyphylline interferon increases the effect and toxicity of theophylline | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Roferon-A (interferon alfa-2a, recombinant) is contraindicated in neonates and infants because it contains benzyl alcohol. Benzyl alcohol is associated with an increased incidence of neurologic and other complications in neonates and infants, which are sometimes fatal. | NA | Link | NA | NA |
| 10232 | Th1031 | Interferon Alfa-2a, Recombinant | >Th1031_Interferon_Alfa-2a,_Recombinant CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | NA | NA | Its a type I interferon consisting of 165 amino acid residues with lysine in position 23. This protein is produced by recombinant DNA technology and resembles interferon secreted by leukocytes. It is used extensively as an antiviral or antineoplastic agent. An oral form is being developed by Amarillo Biosciences. | For the treatment of chronic hepatitis C, hairy cell leukemia, AIDS-related Kaposi's sarcoma, and chronic myelogenous leukemia. Also for the treatment of oral warts arising from HIV infection. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a bbetter target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | Interferon alfa-2 may cause serious adverse effects such as anemia; autoimmune diseases, including vasculitis, arthritis, hemolytic anemia, and erythematosus syndrome; cardiotoxicity; hepatotoxicity; hyperthyroidism or hypothyroidism; transient ischemic a | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | 0.223 to 0.748 L/kg [healthy people] | 2.14 - 3.62 mL/min/kg [healthy] | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Oxtriphylline, interferon increases the effect and toxicity of theophylline | NA | Veldona | Amarillo Biosciences | Amarillo Biosciences | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10233 | Th1031 | Interferon Alfa-2a, Recombinant | >Th1031_Interferon_Alfa-2a,_Recombinant CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | NA | NA | Its a type I interferon consisting of 165 amino acid residues with lysine in position 23. This protein is produced by recombinant DNA technology and resembles interferon secreted by leukocytes. It is used extensively as an antiviral or antineoplastic agent. An oral form is being developed by Amarillo Biosciences. | For the treatment of chronic hepatitis C, hairy cell leukemia, AIDS-related Kaposi's sarcoma, and chronic myelogenous leukemia. Also for the treatment of oral warts arising from HIV infection. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a bbetter target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2-5 oligoadenylate synthetase (2-5 A synthetase) and protein kinase R. | It binds directly to the type II interferon gamma receptor IFNGR1, leading to a complex of IFNGR1 and IFNGR2. This activates JAK1 and JAK2 kinases which form a STAT1 docking site. This leads to STAT1 phosphorylation, nuclear translocation and initiation of gene transcription of multiple immune-related genes. | Interferon alfa-2 may cause serious adverse effects such as anemia; autoimmune diseases, including vasculitis, arthritis, hemolytic anemia, and erythematosus syndrome; cardiotoxicity; hepatotoxicity; hyperthyroidism or hypothyroidism; transient ischemic a | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | 0.223 to 0.748 L/kg [healthy people] | 2.14 - 3.62 mL/min/kg [healthy] | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Immunotherapy, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferon-alpha, Interferons, Myelosuppressive Agents, Peptides, Proteins | NA | NA | NA | Roferon-A (interferon alfa-2a, recombinant) has been reported to reduce the clearance of theophylline. Synergistic toxicity has been observed when Roferon-A (interferon alfa-2a, recombinant) is administered in combination with zidovudine (AZT) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10234 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | 121 ± 30 mL/kg [adults] | 33 - 37 mL/h x kg [healthy] | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Autoplex T (anti-inhibitor coagulant complex) | Coagulation factor X,Serine protease hepsin,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NovoSeven | Novo Nordisk | Novo Nordisk | For treatment and prevention of bleeding in surgeries and procedures in adults and children with hemophilia A or B with inhibitors, congenital Factor VII (FVII) deficiency, and people with Glanzmann’s thrombasthenia who have a decreased or absent response | NA | Each vial contains approximately 0. 6 mg/mL NovoSeven (coagulation factor viia recombinant) (corresponding to 600 _g/mL). The reconstituted vials have a pH of approximately 5. 5 in sodium chloride (3 mg/mL), calcium chloride dihydrate (1. 5 mg/mL), glycyl | Sterile, white lyophilized powder | Injection | For bleeding episodes, the recommended dose of NovoSeven (coagulation factor viia (recombinant)) for hemophilia A or B patients with inhibitors is 90 _g/kg given every two hours by bolus infusion until hemostasis is achieved, or until thehemostasis has been acheived. | Hypersensitivity | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; bleeding at the injection site; bloody stools; calf or stomach pain, tenderness, or swelling; chest pain; confusion; dizziness; fainting; numbness. | Link | NA | NA |
| 10235 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | 153 ± 29 mL/kg [children] | 1375 ± 396 mL/hr [severe hemophilia A male children] | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Bebulin VH (factor ix complex) | NA | Sevenfact | Laboratoire Français du Fractionnement et des Biotechnologies Société Anonyme (LFB S.A.) | Laboratoire Français du Fractionnement et des Biotechnologies Société Anonyme (LFB S.A.) | treatment and control of bleeding episodes occurring in adults and adolescents (12 years of age and older) with hemophilia A or B with inhibitors. | NA | SEVENFACT is formulated with arginine, isoleucine, citrate, glycine, lysine and polysorbate 80. It does not contain any antimicrobial preservatives nor human or bovine plasma-derived proteins. | sterile, white to off-white lyophilized powder | intravenous | For mild bleeding: 75 mcg/kg repeated every 3 hours until hemostasis is achieved or Initial dose of 225 mcg/kg. If hemostasis is not achieved within 9 hours, additional 75 mcg/kg doses may be administered every 3 hours as needed to achieve hemostasis For severe Bleeding: 225 mcg/kg initially, followed if necessary 6 hours later with 75 mcg/kg every 2 hours until hemostasis is achieved. | SEVENFACT is contraindicated in known allergy to rabbits or rabbit proteins. Exposure to SEVENFACT in these patients can result in severe hypersensitivity reaction. patients with severe hypersensitivity reaction to SEVENFACT or any of its components. Exposure to SEVENFACT in these patients can result in severe hypersensitivity reaction. | headache, dizziness, infusion-site discomfort, infusion-site bleeding, infusion-related reactions, and fever | Link | NA | NA |
| 10236 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | 280 to 290 mL/kg [congenital Factor VII deficiency] | 57.3 ± 9.5 mL/hr/kg [severe hemophilia A male children] | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Febia NF (anti-inhibitor coagulant complex) | NA | Niastase | Novo Nordisk | Novo Nordisk | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10237 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | NA | 2767 ± 385 mL/hr [severe hemophilia A men] | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Feiba VH (anti-inhibitor coagulant complex) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10238 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | NA | 37.6 ± 13.1 mL/hr/kg [severe hemophilia A men] | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Konyne 80 (factor ix complex) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10239 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Profilnine SD (factor ix complex) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10240 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Proplex T (factor ix complex) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10241 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Brilinta (ticagrelor) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10257 | Th1036 | Aldesleukin | >Th1036_Aldesleukin MPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT | 15314.8 | C690H1115N177O202S6 | 7.31 | -0.192 | NA | 0.22-1.42 hours | Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125. | For treatment of adults with metastatic renal cell carcinoma. | Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor. | Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells. | NA | NA | NA | 0.18 l/kg | The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-HIV Agents, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP2E1 Inhibitors, Cytochrome P-450 CYP2E1 Inhibitors (strength unknown), Cytochrome P-450 CYP3A Inhibitors, Cytochrome P-450 CYP3A4 Inhibitors, Cytochrome P-450 CYP3A4 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drugs that are Mainly Renally Excreted, Hypotensive Agents, Immunosuppressive Agents, Immunotherapy, Increased Lymphocyte Activation, Increased Lymphocyte Cell Production, Intercellular Signaling Peptides and Proteins, Interleukins, Lymphocyte Growth Factor, Lymphokines, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Peptides, Proteins | NA | NA | NA | Corticosteroids such as clobetasol propionate may diminish the antineoplastic effect of aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin. | Interleukin-2 receptor subunit beta,Interleukin-2 receptor subunit alpha,Cytokine receptor common subunit gamma | Proleukin | Bayer Healthcare , Chiron Corp. , Novartis AG , Physicians Total Care Inc. , Prometheus Laboratories Inc. | Bayer Healthcare , Chiron Corp. , Novartis AG , Physicians Total Care Inc. , Prometheus Laboratories Inc. | Treating skin cancer and kidney cancer that has spread to other parts of the body. | desalanyl-1, serine-125 human interleukin-2 | Proleukin is supplied in single-use vials intended for intravenous administration. When reconstituted with 1.2 mL Sterile Water for Injection, USP, each mL contains 18 million International Units (1.1 mg) Proleukin, 50 mg mannitol, and 0.18 mg sodium dod | Sterile, white to off-white, lyophilized cake | Intravenous administration | The recommended Proleukin treatment regimen is administered by a 15 minute Intravenous infusion every 8 hours. 600,000 International Units/kg (0.037 mg/kg) dose administered every 8 hours by a 15 minute Intravenous infusion for a maximum of 14 doses. ollowing 9 days of rest, the schedule is repeated for another 14 doses, for a maximum of 28 doses per course, as tolerated. | Proleukin is contraindicated in patients with a known history of hypersensitivity to interleukin-2 or any component of the Proleukin formulation. | Anxiety; dizziness; general body discomfort; increased cough; infection; loss of appetite; pain; runny nose; weakness. | Link | NA | NA |
| 10258 | Th1036 | Aldesleukin | >Th1036_Aldesleukin MPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT | 15314.8 | C690H1115N177O202S6 | 7.31 | -0.192 | NA | 0.22-1.42 hours | Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125. | For treatment of adults with metastatic renal cell carcinoma. | Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor. | Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells. | NA | NA | NA | 0.18 l/kg | The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-HIV Agents, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP2E1 Inhibitors, Cytochrome P-450 CYP2E1 Inhibitors (strength unknown), Cytochrome P-450 CYP3A Inhibitors, Cytochrome P-450 CYP3A4 Inhibitors, Cytochrome P-450 CYP3A4 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drugs that are Mainly Renally Excreted, Hypotensive Agents, Immunosuppressive Agents, Immunotherapy, Increased Lymphocyte Activation, Increased Lymphocyte Cell Production, Intercellular Signaling Peptides and Proteins, Interleukins, Lymphocyte Growth Factor, Lymphokines, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Peptides, Proteins | NA | NA | NA | Corticosteroids such as clocortolone may diminish the antineoplastic effect of aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Proleukin is contraindicated in patients with an abnormal thallium stress test or abnormal pulmonary function tests and those with organ allografts. Retreatment with Proleukin is contraindicated in patients who have experienced the following drug-related | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; black stools; chest pain; chills; confusion; depression; diarrhea; drowsiness; fainting; fever; heart murmurs or gallops; infrequent urination. | Link | NA | NA |
| 10259 | Th1036 | Aldesleukin | >Th1036_Aldesleukin MPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT | 15314.8 | C690H1115N177O202S6 | 7.31 | -0.192 | NA | 0.22-1.42 hours | Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125. | For treatment of adults with metastatic renal cell carcinoma. | Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor. | Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells. | NA | NA | NA | 0.18 l/kg | The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-HIV Agents, Anti-Infective Agents, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Biological Factors, Cancer immunotherapy, Cytochrome P-450 CYP2E1 Inhibitors, Cytochrome P-450 CYP2E1 Inhibitors (strength unknown), Cytochrome P-450 CYP3A Inhibitors, Cytochrome P-450 CYP3A4 Inhibitors, Cytochrome P-450 CYP3A4 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Drugs that are Mainly Renally Excreted, Hypotensive Agents, Immunosuppressive Agents, Immunotherapy, Increased Lymphocyte Activation, Increased Lymphocyte Cell Production, Intercellular Signaling Peptides and Proteins, Interleukins, Lymphocyte Growth Factor, Lymphokines, Myelosuppressive Agents, Narrow Therapeutic Index Drugs, Peptides, Proteins | NA | NA | NA | Corticosteroids such as corticotropin may diminish the antineoplastic effect of Aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10260 | Th1037 | Botulinum Toxin Type B | >Th1037_Botulinum_Toxin_Type_B MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE | 150804 | C690H1115N177O202S6 | NA | NA | NA | NA | Neurotoxin produced by fermentation of clostridium botulinum type B. The protein exists in noncovalent association with hemagglutinin and nonhemagglutinin proteins as a neurotoxin complex. The neurotoxin complex is recovered from the fermentation process. | To treat patients with cervical dystonia to reduce the severity of abnormal head position and neck pain associated with cervical dystonia. | Botulinum Toxin Type B inhibits acetylcholine release at the neuromuscular junction via a three stage process: 1) Heavy Chain mediated neurospecific binding of the toxin, 2) internalization of the toxin by receptor-mediated endocytosis, and 3) ATP and pH dependent translocation of the Light Chain to the neuronal cytosol where it acts as a zinc-dependent endoprotease cleaving polypeptides essential for neurotransmitter release. | Botulinum Toxin Type B binds and cleaves the synaptic Vesicle Associated Membrane Protein (VAMP, also known as synaptobrevin) which is a component of the protein complex responsible for docking and fusion of the synaptic vesicle to the presynaptic membrane, a necessary step to neurotransmitter release. | One unit of Botulinum Toxin Type B corresponds to the calculated median lethal intraperitoneal dose (LD50) in mice. | NA | Botulinum Toxin Type B is not expected to be present in the peripheral blood at measurable levels following IM injection at the recommended doses as pharmacokinetic or ADME studies were not performed | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Amphibian Venoms, Anti-Dyskinesia Agents, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Central Nervous System Agents, Central Nervous System Depressants, Cholinergic Agents, Complex Mixtures, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neurotoxins, Neurotransmitter Agents, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Proteins, Toxins, Biological, Venoms | NA | NA | NA | NA | Vesicle-associated membrane protein 2,Vesicle-associated membrane protein 1,Synaptotagmin-2 | Myobloc | Solstice Neurosciences | Solstice Neurosciences | It is used for reducing the severity of abnormal head position and neck pain associated with a certain neck problem (cervical dystonia) | NA | It is supplied in 3.5-mL glass vials. Each single-use vial of formulated MYOBLOC contains 5,000 Units of botulinum toxin type B per milliliter in 0.05% human serum albumin, 0.01 M sodium succinate, and 0.1 M sodium chloride at approximately pH 5.6. | Clear and colorless to light-yellow Sterile injectable solution | Injection | The recommended initial dose of MYOBLOC (botulinum toxin type b) for patients with a prior history of tolerating botulinum toxin injections is 2,500 to 5,000 Units divided among affected muscles. Patients without a prior history of tolerating botulinum toxin injections should receive lower initial dose. | MYOBLOC is contraindicated in patients with a known hypersensitivity to any botulinum toxin preparation or to any of the components in the formulation and in patients with infection at the proposed injection site | Anxiety; back pain; dizziness; drowsiness; dry eyes; dry mouth; flu-like symptoms; headache; increased cough; indigestion; nausea; neck pain; pain, redness, swelling, or tenderness at the injection site; runny nose; sensitivity to light; sweating; upset stomach. | Link | NA | NA |
| 10261 | Th1037 | Botulinum Toxin Type B | >Th1037_Botulinum_Toxin_Type_B MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE | 150804 | C690H1115N177O202S6 | NA | NA | NA | NA | Neurotoxin produced by fermentation of clostridium botulinum type B. The protein exists in noncovalent association with hemagglutinin and nonhemagglutinin proteins as a neurotoxin complex. The neurotoxin complex is recovered from the fermentation process. | To treat patients with cervical dystonia to reduce the severity of abnormal head position and neck pain associated with cervical dystonia. | Botulinum Toxin Type B inhibits acetylcholine release at the neuromuscular junction via a three stage process: 1) Heavy Chain mediated neurospecific binding of the toxin, 2) internalization of the toxin by receptor-mediated endocytosis, and 3) ATP and pH dependent translocation of the Light Chain to the neuronal cytosol where it acts as a zinc-dependent endoprotease cleaving polypeptides essential for neurotransmitter release. | Botulinum Toxin Type B binds and cleaves the synaptic Vesicle Associated Membrane Protein (VAMP, also known as synaptobrevin) which is a component of the protein complex responsible for docking and fusion of the synaptic vesicle to the presynaptic membrane, a necessary step to neurotransmitter release. | One unit of Botulinum Toxin Type B corresponds to the calculated median lethal intraperitoneal dose (LD50) in mice. | NA | Botulinum Toxin Type B is not expected to be present in the peripheral blood at measurable levels following IM injection at the recommended doses as pharmacokinetic or ADME studies were not performed | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Amphibian Venoms, Anti-Dyskinesia Agents, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Central Nervous System Agents, Central Nervous System Depressants, Cholinergic Agents, Complex Mixtures, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neurotoxins, Neurotransmitter Agents, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Proteins, Toxins, Biological, Venoms | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; bleeding at the injection site; chest pain; difficulty swallowing or breathing; double or blurred vision, or other vision changes; drooping eyelids, hoarseness, change in or loss of voice; loss of bladder control; or trouble speaking, breathing, or swallowing. | Link | NA | NA |
| 10262 | Th1037 | Botulinum Toxin Type B | >Th1037_Botulinum_Toxin_Type_B MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE | 150804 | C690H1115N177O202S6 | NA | NA | NA | NA | Neurotoxin produced by fermentation of clostridium botulinum type B. The protein exists in noncovalent association with hemagglutinin and nonhemagglutinin proteins as a neurotoxin complex. The neurotoxin complex is recovered from the fermentation process. | To treat patients with cervical dystonia to reduce the severity of abnormal head position and neck pain associated with cervical dystonia. | Botulinum Toxin Type B inhibits acetylcholine release at the neuromuscular junction via a three stage process: 1) Heavy Chain mediated neurospecific binding of the toxin, 2) internalization of the toxin by receptor-mediated endocytosis, and 3) ATP and pH dependent translocation of the Light Chain to the neuronal cytosol where it acts as a zinc-dependent endoprotease cleaving polypeptides essential for neurotransmitter release. | Botulinum Toxin Type B binds and cleaves the synaptic Vesicle Associated Membrane Protein (VAMP, also known as synaptobrevin) which is a component of the protein complex responsible for docking and fusion of the synaptic vesicle to the presynaptic membrane, a necessary step to neurotransmitter release. | One unit of Botulinum Toxin Type B corresponds to the calculated median lethal intraperitoneal dose (LD50) in mice. | NA | Botulinum Toxin Type B is not expected to be present in the peripheral blood at measurable levels following IM injection at the recommended doses as pharmacokinetic or ADME studies were not performed | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Amphibian Venoms, Anti-Dyskinesia Agents, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Central Nervous System Agents, Central Nervous System Depressants, Cholinergic Agents, Complex Mixtures, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neurotoxins, Neurotransmitter Agents, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Proteins, Toxins, Biological, Venoms | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Seizures; severe or persistent muscle weakness or dizziness; shortness or breath; speech changes or problems; swelling of the hands or feet; vaginal irritation, odor, or discharge; wheezing. | Link | NA | NA |
| 10263 | Th1037 | Botulinum Toxin Type B | >Th1037_Botulinum_Toxin_Type_B MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE | 150804 | C690H1115N177O202S6 | NA | NA | NA | NA | Neurotoxin produced by fermentation of clostridium botulinum type B. The protein exists in noncovalent association with hemagglutinin and nonhemagglutinin proteins as a neurotoxin complex. The neurotoxin complex is recovered from the fermentation process. | To treat patients with cervical dystonia to reduce the severity of abnormal head position and neck pain associated with cervical dystonia. | Botulinum Toxin Type B inhibits acetylcholine release at the neuromuscular junction via a three stage process: 1) Heavy Chain mediated neurospecific binding of the toxin, 2) internalization of the toxin by receptor-mediated endocytosis, and 3) ATP and pH dependent translocation of the Light Chain to the neuronal cytosol where it acts as a zinc-dependent endoprotease cleaving polypeptides essential for neurotransmitter release. | Botulinum Toxin Type B binds and cleaves the synaptic Vesicle Associated Membrane Protein (VAMP, also known as synaptobrevin) which is a component of the protein complex responsible for docking and fusion of the synaptic vesicle to the presynaptic membrane, a necessary step to neurotransmitter release. | One unit of Botulinum Toxin Type B corresponds to the calculated median lethal intraperitoneal dose (LD50) in mice. | NA | Botulinum Toxin Type B is not expected to be present in the peripheral blood at measurable levels following IM injection at the recommended doses as pharmacokinetic or ADME studies were not performed | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Amphibian Venoms, Anti-Dyskinesia Agents, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Central Nervous System Agents, Central Nervous System Depressants, Cholinergic Agents, Complex Mixtures, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neurotoxins, Neurotransmitter Agents, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Proteins, Toxins, Biological, Venoms | NA | NA | NA | The effect of administering different botulinum neurotoxin serotypes concurrently is unknown. However, in clinical studies, NeuroBloc was administered 16 weeks after the injection of Botulinum Toxin Type A. Co-administration of NeuroBloc and aminoglycos | NA | Neurobloc | Sloan Pharma S.A.R.L | Sloan Pharma S.A.R.L | NeuroBloc is indicated for the treatment of cervical dystonia (torticollis) in adults. It means Neurobloc is used to treat muscle spasms of the neck | NA | Medicines contain active ingredients and may also contain other, additional ingredients that help ensure the stability, safety and effectiveness of the medicine. Some may be used to prolong the life of the medicine. Neurobloc contains botulinum toxin type | Clear and colourless to light yellow solution | IntramuSubcutaneousular Injection | The initial dose is 10,000 U and should be divided between the two to four most affected muscles. Data from clinical studies suggest that efficacy is dose dependent, but these trials, because they were not powered for a comparison, do not show a significant difference between 5000 U and 10,000 U. | Hypersensitivity | Dry mouth, dysphagia, dyspepsia, and injection site pain. | Link | NA | NA |
| 10264 | Th1037 | Botulinum Toxin Type B | >Th1037_Botulinum_Toxin_Type_B MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE | 150804 | C690H1115N177O202S6 | NA | NA | NA | NA | Neurotoxin produced by fermentation of clostridium botulinum type B. The protein exists in noncovalent association with hemagglutinin and nonhemagglutinin proteins as a neurotoxin complex. The neurotoxin complex is recovered from the fermentation process. | To treat patients with cervical dystonia to reduce the severity of abnormal head position and neck pain associated with cervical dystonia. | Botulinum Toxin Type B inhibits acetylcholine release at the neuromuscular junction via a three stage process: 1) Heavy Chain mediated neurospecific binding of the toxin, 2) internalization of the toxin by receptor-mediated endocytosis, and 3) ATP and pH dependent translocation of the Light Chain to the neuronal cytosol where it acts as a zinc-dependent endoprotease cleaving polypeptides essential for neurotransmitter release. | Botulinum Toxin Type B binds and cleaves the synaptic Vesicle Associated Membrane Protein (VAMP, also known as synaptobrevin) which is a component of the protein complex responsible for docking and fusion of the synaptic vesicle to the presynaptic membrane, a necessary step to neurotransmitter release. | One unit of Botulinum Toxin Type B corresponds to the calculated median lethal intraperitoneal dose (LD50) in mice. | NA | Botulinum Toxin Type B is not expected to be present in the peripheral blood at measurable levels following IM injection at the recommended doses as pharmacokinetic or ADME studies were not performed | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Amphibian Venoms, Anti-Dyskinesia Agents, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Central Nervous System Agents, Central Nervous System Depressants, Cholinergic Agents, Complex Mixtures, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neurotoxins, Neurotransmitter Agents, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Proteins, Toxins, Biological, Venoms | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Individuals with known neuromuscular diseases (e.g. amyotrophic lateral sclerosis or peripheral neuropathy) or known neuromuscula r junctional disorders (e.g. myasthenia gravis or Lambert-Eaton syndrome) must not be given NeuroBloc. | NA | Link | NA | NA |
| 10275 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | US5474978 | 12-Dec-1995 | 16-Jun-2014 | The beta-blocker, acebutolol, atenolol, bisoprolol, carvedilol, may decrease symptoms of hypoglycemia. | Insulin receptor,Insulin-like growth factor 1 receptor | Humalog | Eli Lilly | Eli Lilly | Humalog is used to treat type 1 diabetes in adults. It is usually given together with another long-acting insulin. Humalog is also used together with oral medications to treat type 2 diabetes in adults. | NA | Each milliliter of HUMALOG contains insulin lispro 100 units, 16 mg glycerin, 1.88 mg dibasic sodium phosphate, 3.15 mg Metacresol, zinc oxide content adjusted to provide 0.0197 mg zinc ion, trace amounts of phenol, and Water for Injection. Insulin lispro | Sterile, aqueous, clear, and colorless solution | Subcutaneous and Intravenous infusion | The total daily insulin requirement may vary and is usually between 0.5 to 1 unit/kg/day. Insulin requirements may be altered during stress, major illness, or with changes in exercise, meal patterns, or coadministered drugs. Usual maintenance range is 0.5-1 unit/kg/day in divided doses; nonobese may require 0.4-0.6 unit/kg/day; obese may require 0.8-1.2 units/kg/day. | During episodes of hypoglycemia in patients who are hypersensitive to HUMALOG or to any of its excipients. | Low blood sugar--headache, hunger, weakness, sweating, confusion, irritability, dizziness, fast heart rate, or feeling jittery. | Link | NA | NA |
| 10276 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | US5514646 | 7-May-1996 | 7-May-2013 | Concomitant therapy with drugs like Dextropropoxyphene, Pentoxifylline, Pramlintide, Fluoxetine, Fenofibrate and Disopyramide that may increase the blood-glucose-lowering effect of insulin lispro | NA | Admelog | Sanofi Aventis, REMEDYREPACK INC. | Sanofi Aventis, REMEDYREPACK INC. | symptoms of Type 1 or 2 Diabetes Mellitus. | C257H383N65O77S6 | Insulin lispro is produced by recombinant DNA technology utilizing a non-pathogenic laboratory strain of Escherichia coli. Insulin lispro differs from human insulin in that the amino acid proline at position B28 is replaced by lysine and the lysine in position B29 is replaced by proline. | sterile, aqueous, clear, and colorless solution. | Subcutaneous Injection | Dilute ADMELOG to concentrations from 0.1 unit/mL to 1 unit/mL using 0.9% sodium chloride. Administer ADMELOG intravenously ONLY under medical supervision with close monitoring of blood glucose and potassium levels to avoid hypoglycemia and hypokalemia | ADMELOG is contraindicated: during episodes of hypoglycemia. in patients who are hypersensitive to insulin lispro or to any of the excipients. Clinical Pharmacology | hives, difficulty breathing, swelling of your face, lips, tongue, or throat, redness or swelling where an injection was given, itchy skin rash over the entire body, fast heartbeats, lightheadedness, weight gain, swelling in your hands or feet, shortness of breath, headache, hunger, sweating, irritability, dizziness, anxiety, shakiness, leg cramps, constipation, irregular heartbeats, fluttering in your chest, increased thirst or urination, numbness or tingling, muscle weakness, and limp feeling | Link | NA | NA |
| 10277 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | CA2151564 | 11-Feb-2003 | 12-Jun-2015 | Concomitant therapy with ACE inhibitors like Enalapril and Ramipril may increase the blood-glucose-lowering effect of insulin lispro and thus the chance of hypoglycemia should be monitored closely. | NA | Insulin Lispro | A-S Medication Solutions, Eli Lilly and Company, REMEDYREPACK INC., ImClone LLC | A-S Medication Solutions, Eli Lilly and Company, REMEDYREPACK INC., ImClone LLC | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10278 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | CA2151560 | 9-May-2000 | 12-Jun-2015 | Concomitant therapy with diuretics like Hydrochlorothiazide may reduce the blood-glucose-lowering effect of insulin lispro. | NA | Humalog KwikPen | Eli Lilly | Eli Lilly | Insulin lispro is used to treat type 1 diabetes in adults. It is usually given together with another long-acting insulin. Insulin lispro is also used together with oral medication to treat type 2 diabetes in adults. | NA | NA | Solution | Subcutaneous injection | Insulin lispro can be administered intravenously under medical supervision at concentrations from 0.1 unit/mL to 1 unit/mL in infusion systems containing 0.9% sodium chloride. Blood glucose and potassium levels should be closely monitored to avoid hypoglycemia. | During episodes of hypoglycemia in patients who are hypersensitive to HUMALOG or to any of its excipients. | Low blood sugar is the most common side effect. There are many causes of low blood sugar, including taking too much Humalog. Severe life-threatening allergic reactions (whole-body reactions) can happen.Reactions at the injection site (local allergic reaction. | Link | NA | NA |
| 10279 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | Concomitant therapy with angiotensin II receptor blockers like Losartan may increase the blood-glucose-lowering effect of insulin lispro and thus the chance of hypoglycemia should be monitored closely. | NA | Liprelog | Eli Lilly & Co. Ltd. | Eli Lilly & Co. Ltd. | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10280 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | Concomitant therapy with somatostatin analogs like Octreotide may increase the blood-glucose-lowering effect of insulin lispro and thus the chance of hypoglycemia should be monitored closely. | NA | Humalog Pen | Eli Lilly | Eli Lilly | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10281 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | The beta-blocker, esmolol, may decrease symptoms of hypoglycemia. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10282 | Th1040 | Insulin Lispro | >Th1040_Insulin_Lispro GIVEQCCTSICSLYQLENYCN | 5808 | C257H387N65O76S6 | 5.39 | 0.218 | 81 | On subcutaneous administration = 1 hour | Insulin lispro is a recombinant human insulin analogue produced in a specialized laboratory strain of Escherischia coli. Plasmid DNA transfected into the bacteria encodes for an analogue of human insulin that has a lysine at residuce B28 and proline at B29; these residues are reversed in endogenous human insulin. Reversal of these amino acid residues produces a rapid-acting insulin analogue. FDA approved on 1996. | To treat type 1 or 2 diabetes mellitus. To be used in conjunction with an intermediate or long-acting insulin except when used in a continuous insulin infusion pump. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin lispro binds to the insulin receptor(IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Reversal of the proline and lysine residues at positions B28 and B29 of native insulin eliminates hydrophobic interactions and weakens some of the hydrogen bonds that contribute to the stability of the insulin dimers that comprise insulin hexamers. Hexamers of insulin lispro are produced in the presence of zinc and -cresol. These weakly associated hexamers quickly dissociate upon subcutaneous injection and are absorbed as monomers through vascular endothelial cells. These properties give insulin lispro its fast-acting properties. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | Rapidly absorbed following subcutaneous administration. It is also absorbed more quickly than regular human insulin. Peak serum levels occur 30-90 minutes after injection in healthy subjects. Absorption also differs depending on the site of injection. Aft | When administered intravenously as bolus injections of 0.1 and 0.2 U/kg dose in two separate groups of healthy subjects, the mean volume of distribution of insulin lispro appeared to decrease with increase in dose (1.55 and 0.72 L/kg, respectively). | Clearance is dose dependent. When a dose of 0.1 unit/kg and 0.2 unit/kg were administered intravenously, the mean clearance was 21.0 mL/min/kg and 9.6 mL/min/kg respectively. | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Insulin, Insulin Analog, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | Concomitant therapy with sympathomimetic agents like Epinephrine may reduce the blood-glucose-lowering effect of insulin lispro. | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10283 | Th1041 | Insulin Glargine | >Th1041_Insulin_Glargine GIVEQCCTSICSLYQLENYCG | 6063 | C267H404N72O78S6 | 6.88 | 0.098 | 81 | Not reported in humans; 30 hours in mammalian reticulocytes. | Insulin glargine is produced by recombinant DNA technology using a non-pathogenic laboratory strain of Escherichia coli (K12). It is an analogue of human insulin made by replacing the asparagine residue at position A21 of the A-chain with glycine and adding two arginines to the C-terminus (positions B31 and 32) of the B-chain. The resulting protein is soluble at pH 4 and forms microprecipitates at physiological pH 7.4. Small amounts of insulin glargine are slowly released from microprecipitates giving the drug a long duration of action (up to 24 hours) and no pronounced peak concentration. | To treat Type 1 or 2 diabetes mellitus in patients over 17 years old who require a long-acting (basal) insulin for the control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for glycemic control. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin glargine binds to the insulin receptor, a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism. Insulin glargine is completely soluble at pH 4, the pH of administered solution, and has low solubility at physiological pH 7.4. Upon subcuteous injection, the solution is neutralized resulting in the formation of microprecipitates. Small amounts of insulin glargine are released from microprecipitates giving the drug a relatively constant concentration over time profile over 24 hours with no pronounced peak. This release mechanism allows the drug to mimic basal insulin levels within the body. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Partly metabolized to two active metabolites with similar in vitro activity to insulin: A21-Gly-insulin and A21-Gly-des-B30-Thr-insulin. | Due to the modifications in the A and B chain, the isoelectric point shifts towards a neutral pH and insulin glargine is more stable in acidic conditions than regular insulin. As insulin glargine is less soluble at neutral pH, once injected, forms micro-p | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Antimetabolites, Biological Products, Blood Glucose Lowering Agents, Complex Mixtures, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Hypolipidemic Agents, Insulin, Insulin Analog, Insulin, Long-Acting, Lipid Regulating Agents, Pancreatic Hormones, Peptide Hormones, Peptides | US7476652 | 13-Jan-2009 | 23-Jul-2023 | Somatropin may antagonize the hypoglycemic effect of insulin glargine. Monitor for changes in fasting and postprandial blood sugars. | Insulin receptor,Insulin-like growth factor 1 receptor | Lantus | Sanofi-Aventis | Sanofi-Aventis | Its used to improve glycemic control in adults and children with type 1 diabetes mellitus and in adults with type 2 diabetes mellitus. | 21A-Gly-30Ba-L-Arg-30Bb-L-Arg-human insulin | LANTUS consists of insulin glargine dissolved in a clear aqueous fluid. Each milliliter of LANTUS contains 100 Units (3.6378 mg) insulin glargine. The 10 mL vial presentation contains the following inactive ingredients per mL: 30 mcg zinc, 2.7 mg m-cresol | Solution | Subcutaneous Injection | LANTUS may be administered at any time during the day. LANTUS should be administered subcutaneously once a day at the same time every day. The dose of LANTUS must be individualized based on clinical response. | Hypersensitivity | Low blood sugar (headache, hunger, weakness, sweating, confusion, irritability, dizziness, fast heart rate, or feeling jittery). Sign of insulin allergy include itching skin rash over the entire body, wheezing, trouble breathing, fast heart rate, sweating. | Link | NA | NA |
| 10284 | Th1041 | Insulin Glargine | >Th1041_Insulin_Glargine GIVEQCCTSICSLYQLENYCG | 6063 | C267H404N72O78S6 | 6.88 | 0.098 | 81 | Not reported in humans; 30 hours in mammalian reticulocytes. | Insulin glargine is produced by recombinant DNA technology using a non-pathogenic laboratory strain of Escherichia coli (K12). It is an analogue of human insulin made by replacing the asparagine residue at position A21 of the A-chain with glycine and adding two arginines to the C-terminus (positions B31 and 32) of the B-chain. The resulting protein is soluble at pH 4 and forms microprecipitates at physiological pH 7.4. Small amounts of insulin glargine are slowly released from microprecipitates giving the drug a long duration of action (up to 24 hours) and no pronounced peak concentration. | To treat Type 1 or 2 diabetes mellitus in patients over 17 years old who require a long-acting (basal) insulin for the control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for glycemic control. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin glargine binds to the insulin receptor, a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism. Insulin glargine is completely soluble at pH 4, the pH of administered solution, and has low solubility at physiological pH 7.4. Upon subcuteous injection, the solution is neutralized resulting in the formation of microprecipitates. Small amounts of insulin glargine are released from microprecipitates giving the drug a relatively constant concentration over time profile over 24 hours with no pronounced peak. This release mechanism allows the drug to mimic basal insulin levels within the body. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Partly metabolized to two active metabolites with similar in vitro activity to insulin: A21-Gly-insulin and A21-Gly-des-B30-Thr-insulin. | Due to the modifications in the A and B chain, the isoelectric point shifts towards a neutral pH and insulin glargine is more stable in acidic conditions than regular insulin. As insulin glargine is less soluble at neutral pH, once injected, forms micro-p | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Antimetabolites, Biological Products, Blood Glucose Lowering Agents, Complex Mixtures, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Hypolipidemic Agents, Insulin, Insulin Analog, Insulin, Long-Acting, Lipid Regulating Agents, Pancreatic Hormones, Peptide Hormones, Peptides | US6100376 | 8-Aug-2000 | 6-Nov-2009 | The beta-blocker, Timolol, Sotalol, Propranolol, Practolol, Acebutolol, Atenolol, Betaxolol, Bevantolol, Bisoprolol, Carteolol, Carvedilol, Esmolol | NA | Lantus R / Lusduna Nexvue / Optisulin / Semglee | (Mylan Pharmaceuticals Inc) | (Mylan Pharmaceuticals Inc) | to control high blood sugar in adults with diabetes mellitus. | NA | NA | clear aqueous fluid | Injection | NA | LANTUS is contraindicated: during episodes of hypoglycemia in patients with hypersensitivity to LANTUS or one of its excipients | NA | Link | NA | NA |
| 10285 | Th1041 | Insulin Glargine | >Th1041_Insulin_Glargine GIVEQCCTSICSLYQLENYCG | 6063 | C267H404N72O78S6 | 6.88 | 0.098 | 81 | Not reported in humans; 30 hours in mammalian reticulocytes. | Insulin glargine is produced by recombinant DNA technology using a non-pathogenic laboratory strain of Escherichia coli (K12). It is an analogue of human insulin made by replacing the asparagine residue at position A21 of the A-chain with glycine and adding two arginines to the C-terminus (positions B31 and 32) of the B-chain. The resulting protein is soluble at pH 4 and forms microprecipitates at physiological pH 7.4. Small amounts of insulin glargine are slowly released from microprecipitates giving the drug a long duration of action (up to 24 hours) and no pronounced peak concentration. | To treat Type 1 or 2 diabetes mellitus in patients over 17 years old who require a long-acting (basal) insulin for the control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for glycemic control. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin glargine binds to the insulin receptor, a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism. Insulin glargine is completely soluble at pH 4, the pH of administered solution, and has low solubility at physiological pH 7.4. Upon subcuteous injection, the solution is neutralized resulting in the formation of microprecipitates. Small amounts of insulin glargine are released from microprecipitates giving the drug a relatively constant concentration over time profile over 24 hours with no pronounced peak. This release mechanism allows the drug to mimic basal insulin levels within the body. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Partly metabolized to two active metabolites with similar in vitro activity to insulin: A21-Gly-insulin and A21-Gly-des-B30-Thr-insulin. | Due to the modifications in the A and B chain, the isoelectric point shifts towards a neutral pH and insulin glargine is more stable in acidic conditions than regular insulin. As insulin glargine is less soluble at neutral pH, once injected, forms micro-p | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Antimetabolites, Biological Products, Blood Glucose Lowering Agents, Complex Mixtures, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Hypolipidemic Agents, Insulin, Insulin Analog, Insulin, Long-Acting, Lipid Regulating Agents, Pancreatic Hormones, Peptide Hormones, Peptides | CA1339044 | 1-Apr-1997 | 1-Apr-2014 | NA | NA | Abasaglar/Basaglar | Eli Lilly Nederland B.V | Eli Lilly Nederland B.V | to control high blood sugar in adults and children with type 1 diabetes mellitus and adults with type 2 diabetes mellitus. | NA | BASAGLAR is produced by recombinant DNA technology utilizing a non-pathogenic laboratory strain of Escherichia coli (K12) as the production organism. Insulin glargine differs from human insulin in that the amino acid asparagine at position A21 is replaced by glycine and two arginines are added to the C-terminus of the B-chain. | clear, colorless, sterile aqueous solution | subcutaneously into the abdominal area, thigh, or deltoid, and rotate injection sites within the same region from one injection to the next | Inject between 1 and 80 units per injection. | BASAGLAR is contraindicated: During episodes of hypoglycemia. In patients with hypersensitivity to insulin glargine or one of its excipients | low blood sugar (hypoglycemia), allergic reactions, injection site reactions, body fat redistribution, itching, rash, swelling, weight gain, upper respiratory tract infection, runny or stuffy nose, back pain, cough, urinary tract infection, diarrhea, depression, or headache. | Link | NA | NA |
| 10286 | Th1041 | Insulin Glargine | >Th1041_Insulin_Glargine GIVEQCCTSICSLYQLENYCG | 6063 | C267H404N72O78S6 | 6.88 | 0.098 | 81 | Not reported in humans; 30 hours in mammalian reticulocytes. | Insulin glargine is produced by recombinant DNA technology using a non-pathogenic laboratory strain of Escherichia coli (K12). It is an analogue of human insulin made by replacing the asparagine residue at position A21 of the A-chain with glycine and adding two arginines to the C-terminus (positions B31 and 32) of the B-chain. The resulting protein is soluble at pH 4 and forms microprecipitates at physiological pH 7.4. Small amounts of insulin glargine are slowly released from microprecipitates giving the drug a long duration of action (up to 24 hours) and no pronounced peak concentration. | To treat Type 1 or 2 diabetes mellitus in patients over 17 years old who require a long-acting (basal) insulin for the control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for glycemic control. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin glargine binds to the insulin receptor, a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism. Insulin glargine is completely soluble at pH 4, the pH of administered solution, and has low solubility at physiological pH 7.4. Upon subcuteous injection, the solution is neutralized resulting in the formation of microprecipitates. Small amounts of insulin glargine are released from microprecipitates giving the drug a relatively constant concentration over time profile over 24 hours with no pronounced peak. This release mechanism allows the drug to mimic basal insulin levels within the body. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Partly metabolized to two active metabolites with similar in vitro activity to insulin: A21-Gly-insulin and A21-Gly-des-B30-Thr-insulin. | Due to the modifications in the A and B chain, the isoelectric point shifts towards a neutral pH and insulin glargine is more stable in acidic conditions than regular insulin. As insulin glargine is less soluble at neutral pH, once injected, forms micro-p | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Antimetabolites, Biological Products, Blood Glucose Lowering Agents, Complex Mixtures, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Hypolipidemic Agents, Insulin, Insulin Analog, Insulin, Long-Acting, Lipid Regulating Agents, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | NA | NA | Lantus OptiSet | NA | NA | Its used to reduce high blood sugar in adults, adolescents and children of 6 years or above with diabetes mellitus. | NA | NA | Solution | Subcutaneous Injection | Patients need one injection of Lantus every day, at the same time of the day. In children, only evening injection has been studied.OptiSet delivers insulin in increments of 2 units up to a maximum single dose of 40 units. The dosage may vary from person tto person. | Hypersensitivity | Hypoglycemia, skin changes at the injection site, allergic reactions, large-scale skin reactions (rash and itching all over the body), severe swelling of skin or mucous membranes (angio-oedema), shortness of breath, a fall in blood pressure with rapid headache. | Link | NA | NA |
| 10287 | Th1041 | Insulin Glargine | >Th1041_Insulin_Glargine GIVEQCCTSICSLYQLENYCG | 6063 | C267H404N72O78S6 | 6.88 | 0.098 | 81 | Not reported in humans; 30 hours in mammalian reticulocytes. | Insulin glargine is produced by recombinant DNA technology using a non-pathogenic laboratory strain of Escherichia coli (K12). It is an analogue of human insulin made by replacing the asparagine residue at position A21 of the A-chain with glycine and adding two arginines to the C-terminus (positions B31 and 32) of the B-chain. The resulting protein is soluble at pH 4 and forms microprecipitates at physiological pH 7.4. Small amounts of insulin glargine are slowly released from microprecipitates giving the drug a long duration of action (up to 24 hours) and no pronounced peak concentration. | To treat Type 1 or 2 diabetes mellitus in patients over 17 years old who require a long-acting (basal) insulin for the control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for control of hyperglycemia. May be used in pediatric patients with Type 1 diabetes mellitus who require a long-acting (basal) insulin for glycemic control. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin lispro is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin lispro is 10-15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 4-5 hours. Compared to regular human insulin, insulin lispro has a more rapid onset of action and a shorter duration of action. Insulin lispro is also shown to be equipotent to human insulin on a molar basis. | Insulin glargine binds to the insulin receptor, a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism. Insulin glargine is completely soluble at pH 4, the pH of administered solution, and has low solubility at physiological pH 7.4. Upon subcuteous injection, the solution is neutralized resulting in the formation of microprecipitates. Small amounts of insulin glargine are released from microprecipitates giving the drug a relatively constant concentration over time profile over 24 hours with no pronounced peak. This release mechanism allows the drug to mimic basal insulin levels within the body. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweat | Partly metabolized to two active metabolites with similar in vitro activity to insulin: A21-Gly-insulin and A21-Gly-des-B30-Thr-insulin. | Due to the modifications in the A and B chain, the isoelectric point shifts towards a neutral pH and insulin glargine is more stable in acidic conditions than regular insulin. As insulin glargine is less soluble at neutral pH, once injected, forms micro-p | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Antimetabolites, Biological Products, Blood Glucose Lowering Agents, Complex Mixtures, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Hypolipidemic Agents, Insulin, Insulin Analog, Insulin, Long-Acting, Lipid Regulating Agents, Pancreatic Hormones, Peptide Hormones, Peptides | NA | NA | NA | NA | NA | Lantus SoloStar | NA | NA | It works by helping your body to use sugar properly. This lowers the amount of glucose in the blood, which helps to treat diabetes. | NA | NA | Solution | Subcutaneous Injection | NA | Hypersensitivity | Severe allergic reactions (rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue); changes in vision; chills; confusion; dizziness; drowsiness; fainting; fast heartbeat; fast, shallow breathing. | Link | NA | NA |
| 10288 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | NA | Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain,Collagen alpha-2(I) chain | Cordase | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10289 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | Grafco Silver Nitrate (silver nitrate topical) | NA | Santyl | Smith & Nephew, Inc | Smith & Nephew, Inc | Used to remove dead skin from wounds and burned areas. Santyl ointment is an enzymatic debriding ointment which works by breaking down dead skin. | NA | Collagenase Santyl Ointment contains 250 units of collagenase enzyme per gram of white petrolatum USP. The potency assay of collagenase is based on the digestion of undenatured collagen (from bovine Achilles tendon) at pH 7.2 and 37°C for 24 hours. The nu | Sterile enzymatic debriding ointment | Apply on the affected area. | Collagenase Santyl Ointment should be applied once daily (or more frequently if the dressing becomes soiled as from incontinence). | Hypersensitivity | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; signs of infection (eg, fever, chills, or persistent sore throat). | Link | NA | NA |
| 10290 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | SilvrSTAT (silver topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10291 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | Thermazene (silver sulfadiazine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10292 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | silver / zinc oxide topical | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10293 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | SilvaSorb (silver topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10294 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | Mersol (thimerosal topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10295 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | silver sulfadiazine topical | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10296 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | SSD AF (silver sulfadiazine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10297 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | Silvadene Cream 1% (silver sulfadiazine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10298 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | Silvadene (silver sulfadiazine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10299 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | SSD (silver sulfadiazine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10300 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | silver nitrate topical | NA | Qwo | Endo Aesthetics LLC | Endo Aesthetics LLC | used for the treatment of moderate to severe cellulite in the buttocks of adult women. | NA | Each QWO 0.92-mg single-dose vial contains 0.92 mg of collagenase clostridium histolyticumaaes and mannitol (37.7 mg), sucrose (18.9 mg), tromethamine (1.1 mg), and hydrochloric acid as needed to adjust pH. Reconstitution with 4 mL of supplied Diluent for QWO yields a solution containing 0.23 mg/mL collagenase clostridium histolyticum-aaes at a pH of approximately 8.0. Each QWO 1.84-mg single-dose vial contains 1.84 mg of collagenase clostridium histolyticumaaes and mannitol (75.4 mg), sucrose (37.8 mg), tromethamine (2.2 mg), and hydrochloric acid as needed to adjust pH. Reconstitution with 8 mL of supplied Diluent for QWO yields a solution containing 0.23 mg/mL collagenase clostridium histolyticum-aaes at a pH of approximately 8.0. | sterile, preservative-free, lyophilized powder (appearing as a white cake) | injected subcutaneously | A treatment area is defined as a single buttock receiving up to 12 injections, 0.3 mL each (up to a total of 3.6 mL), of QWO. A treatment visit may consist of up to 2 treatment areas. Treatment should be repeated every 21 days for 3 treatment visits. | QWO is contraindicated in: patients with a history of hypersensitivity to collagenase or to any of the excipients. the presence of infection at the injection sites. | hives swollen face trouble breathing chest pain low blood pressure dizziness or fainting | NA | NA | NA |
| 10301 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | thimerosal topical | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10302 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | NA | NA | Xiaflex | Auxilium, Endo Pharmaceuticals Inc., Swedish Orphan Biovitrum Ab | Auxilium, Endo Pharmaceuticals Inc., Swedish Orphan Biovitrum Ab | XIAFLEX is indicated for the treatment of adult patients with Dupuytren's contracture with a palpable cord. XIAFLEX is also indicated for the treatment of adult men with Peyronie's disease with a palpable plaque and curvature deformity of at least 30 degr | NA | XIAFLEX is available in single-use, glass vials containing 0.9 mg of collagenase clostridium histolyticum. Each vial also contains 0.5 mg of hydrochloric acid, 18.5 mg of sucrose, and 1.1 mg of tromethamine. | Sterile lyophilized powder (white cake) and must be reconstituted with the provided diluent prior to use. | Intralesional Injection | The dose of XIAFLEX is 0.58 mg per injection into a palpable cord with a contracture of a metacarpophalangeal (MP) joint or a proximal interphalangeal (PIP) joint | The treatment of Peyronie's plaques that involve the penile urethra due to potential risk to this structure. | Swelling, bruising, or bleeding where the medicine was injected; mild pain or tenderness in the treated hand; swollen glands in your elbow or underarm; itching, redness, or warmth of the skin; cracked skin; or underarm pain. | Link | NA | NA |
| 10303 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Patients with a history of hypersensitivity to XIAFLEX or to collagenase used in any other therapeutic application or application method | NA | Link | NA | NA |
| 10304 | Th1042 | Collagenase | >Th1042_Collagenase MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.58 | -0.714 | 49-54 | NA | This enzyme is derived from fermentation of Clostridium histolyticum | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. | NA | NA | NA | NA | NA | Collagen-specific Enzyme, Collagenases, Dermatologicals, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Metalloendopeptidases, Metalloproteases, Microbial Collagenase, antagonists & inhibitors, Misc. Skin and Mucous Membrane Agents, Musculo-Skeletal System, Peptide Hydrolases, Preparations for Treatment of Wounds and Ulcers | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10305 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | 110 to 127 mL/kg [pediatric patients] | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | CA2175971 | 30-Dec-2003 | 7-May-2016 | amyl nitrite / sodium nitrite / sodium thiosulfate | Uric acid | Elitek | Sanofi-Synthelabo Inc | Sanofi-Synthelabo Inc | Used for preventing high blood levels of uric acid from occurring in patients with certain types of cancer (eg, leukemia, lymphoma, solid malignant tumors) who are receiving cancer chemotherapy treatment. | NA | Elitek is supplied in 3 mL and 10 mL colorless, glass vials containing rasburicase at a concentration of 1.5 mg/mL after reconstitution. Elitek 1.5 mg presentation contains 1.5 mg rasburicase, 10.6 mg mannitol, 15.9 mg L-alanine, between 12.6 and 14.3 mg | Sterile, white to off-white, lyophilized powder | Intravenous administration | The recommended dose of Elitek is 0.2 mg/kg as a 30 minute Intravenous infusion daily for up to 5 days. Dosing beyond 5 days or administration of more than one course is not recommended. | Pateints with history of anaphylaxic or severe hypersensitivity | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; blue or gray skin color; chest pain; chills; coughing up blood; dark urine; fever; irregular heartbeat; numbness or tingling of the skin; persistent sore throat; severe dizziness; shortness of breath, trouble breathing, or wheezing; swelling of the hands or feet; weakness; yellowing of the eyes and skin. | Link | NA | NA |
| 10306 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | 75.8 to 138 mL/kg [adult patients] | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | CA2148537 | 16-Jul-2002 | 3-May-2015 | Citanest Forte (epinephrine / prilocaine) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Individulas deficient in glucose -6-phosphate dehydrogenase. | NA | Link | NA | NA |
| 10307 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | Citanest HCl Plain (prilocaine) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10308 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | Cyanide Antidote Kit (amyl nitrite / sodium nitrite / sodium thiosulfate) | NA | Fasturtec | Sanofi Aventis | Sanofi Aventis | Fasturtec is used to treat and prevent high levels of uric acid in the blood in order to prevent kidney failure. It is used in adults and children with blood cancers who are at risk of a sudden rise in uric acid levels when they start to receive chemother | NA | NA | Powder and solvent that are made upto make solution. | Intravenous administartion | The recommended dose is 0.2 mg per kilogram body weight in both children and adults, given as a daily infusion for up to seven days. The duration of treatment is adjusted depending on the patient’s blood levels of uric acid and the doctor’s judgment. | Hypersensitivity | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; blue or gray skin color; chest pain; chills; coughing up blood; dark urine; fever; irregular heartbeat; numbness or tingling of the skin; persistent sore throat; severe dizziness; shortness of breath, trouble breathing, or wheezing; swelling of the hands or feet; weakness; yellowing of the eyes and skin. | Link | NA | NA |
| 10309 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | Emla (lidocaine / prilocaine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Pateint with a deficiency in glucose-6-phoshphate dehydrogenase or other metabolic disorder known to cause haemolytic anaemia. | NA | Link | NA | NA |
| 10310 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | Emla Anesthetic Disc (lidocaine / prilocaine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10311 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | epinephrine / prilocaine | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10312 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | lidocaine / prilocaine topical | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10313 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | Nithiodote (sodium nitrite / sodium thiosulfate) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10314 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | Oraqix (lidocaine / prilocaine topical) | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10315 | Th1043 | Rasburicase | >Th1043_Rasburicase SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKADNSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVNIVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLTVLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSHVPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEYSLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRSSLKSKL | 34109.5 | C1521H2381N417O461S7 | 7.16 | -0.465 | NA | 18 hours | Rasburicase is a recombinant urate-oxidase enzyme produced by a genetically modified Saccharomyces cerevisiae< strain. The cDNA coding for rasburicase was cloned from a strain of Aspergillus flavus. | For treatment of hyperuricemia, reduces elevated plasma uric acid levels (from chemotherapy). | Drugs used to treat lympohoid leukemia, non-Hodgkin's lymphoma and acute myelogenous leukemia often lead to the accumulation of toxic plasma levels of purine metabolites (i.e. uric acid). The injection of rasburicase reduces levels of uric acid and mitigates the toxic effects of chemotherapy induced tumor lysis. | Rasburicase catalyzes enzymatic oxidation of uric acid into an inactive and soluble metabolite (allantoin). | NA | NA | NA | NA | NA | Antigout Preparations, Detoxifying Agents for Antineoplastic Treatment, Enzymes, Enzymes and Coenzymes, Methemoglobinemia Associated Agents, Musculo-Skeletal System, Oxidoreductases, Recombinant Proteins, Uric Acid-specific Enzyme | NA | NA | NA | sodium nitrite / sodium thiosulfate | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10324 | Th1045 | Imiglucerase | >Th1045_Imiglucerase ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ | 55597.4 | C2532H3854N672O711S16 | 7.41 | -0.168 | NA | 0.06-0.173 hours | Human Beta-glucocerebrosidase or Beta-D-glucosyl-N-acylsphingosine glucohydrolase E.C. 3.2.1.45. 497 residue protein with N-linked carbohydrates, MW=59.3 kD. Alglucerase is prepared by modification of the oligosaccharide chains of human Beta-glucocerebros. | For the treatment of Gaucher's disease (deficiency in glucocerebrosidase). | Gaucher disease is characterized by a functional deficiency in Beta-glucocerebrosidase enzymatic activity and the resultant accumulation of lipid glucocerebroside in tissue macrophages which become engorged and are termed Gaucher cells. Gaucher cells are typically found in liver, spleen and bone marrow. This can lead to an enlarged spleen and liver (hepatosplenomegaly). Secondary hematologic sequelae include severe anemia and thrombocytopenia. Injections of imiglucerase into Gaucher disease patients leads to elevated serum levels of the enzyme and reduction in the accumulation of glucocerebroside leading to reduced anemia and thrombocytopenia, reduced spleen and liver size, and decreased cachexia. | Imiglucerase catalyzes the hydrolysis of the glycolipid, glucocerebroside, to glucose and ceramide as part of the normal degradation pathway for membrane lipids. | NA | NA | NA | 0.09 to 0.15 L/kg | 14.5 ± 4.0 mL/min/kg | Alimentary Tract and Metabolism, Enzyme Replacement Therapy, Enzymes, Enzymes and Coenzymes, Gaucher Disease, Glucosidases, Glycoside Hydrolases, Hydrolases, Hydrolytic Lysosomal Glucocerebroside-specific Enzyme | US5549892 | 27-Aug-1996 | 27-Aug-2013 | Zavesca (miglustat) | Glucocerebroside | Cerezyme | Genzyme | Genzyme | It is used as an enzyme replacement in people with Type I Gaucher disease. | NA | Certezyme is supplied as 200 unit vial and 400 unit vial. The constituent of 200 unit vial are 212 units of Imiglucerase, 170 mg mannitol , 70 mg sodium citrates, 52 mg trisodium citrate, 18 mg Disodium hydrogen citrate and 0.53 mg polysorbate. | Sterile, non-pyrogenic, white to off-white lyophilized product | Intravenous infusion | Dosage should be individualized to each patient. Initial dosages range from 2.5 U/kg of body weight 3 times a week to 60 U/kg once every 2 weeks. | There are no known contraindications to the use of Cerezyme | Stomach pain, nausea, vomiting, diarrhea; fast heartbeats; headache, dizziness; back pain; fever, chills, tired feeling; mild rash; or itching, burning, swelling, or other discomfort around the IV needle. | Link | NA | NA |
| 10325 | Th1045 | Imiglucerase | >Th1045_Imiglucerase ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ | 55597.4 | C2532H3854N672O711S16 | 7.41 | -0.168 | NA | 0.06-0.173 hours | Human Beta-glucocerebrosidase or Beta-D-glucosyl-N-acylsphingosine glucohydrolase E.C. 3.2.1.45. 497 residue protein with N-linked carbohydrates, MW=59.3 kD. Alglucerase is prepared by modification of the oligosaccharide chains of human Beta-glucocerebros. | For the treatment of Gaucher's disease (deficiency in glucocerebrosidase). | Gaucher disease is characterized by a functional deficiency in Beta-glucocerebrosidase enzymatic activity and the resultant accumulation of lipid glucocerebroside in tissue macrophages which become engorged and are termed Gaucher cells. Gaucher cells are typically found in liver, spleen and bone marrow. This can lead to an enlarged spleen and liver (hepatosplenomegaly). Secondary hematologic sequelae include severe anemia and thrombocytopenia. Injections of imiglucerase into Gaucher disease patients leads to elevated serum levels of the enzyme and reduction in the accumulation of glucocerebroside leading to reduced anemia and thrombocytopenia, reduced spleen and liver size, and decreased cachexia. | Imiglucerase catalyzes the hydrolysis of the glycolipid, glucocerebroside, to glucose and ceramide as part of the normal degradation pathway for membrane lipids. | NA | NA | NA | 0.09 to 0.15 L/kg | 14.5 ± 4.0 mL/min/kg | Alimentary Tract and Metabolism, Enzyme Replacement Therapy, Enzymes, Enzymes and Coenzymes, Gaucher Disease, Glucosidases, Glycoside Hydrolases, Hydrolases, Hydrolytic Lysosomal Glucocerebroside-specific Enzyme | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10326 | Th1045 | Imiglucerase | >Th1045_Imiglucerase ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ | 55597.4 | C2532H3854N672O711S16 | 7.41 | -0.168 | NA | 0.06-0.173 hours | Human Beta-glucocerebrosidase or Beta-D-glucosyl-N-acylsphingosine glucohydrolase E.C. 3.2.1.45. 497 residue protein with N-linked carbohydrates, MW=59.3 kD. Alglucerase is prepared by modification of the oligosaccharide chains of human Beta-glucocerebros. | For the treatment of Gaucher's disease (deficiency in glucocerebrosidase). | Gaucher disease is characterized by a functional deficiency in Beta-glucocerebrosidase enzymatic activity and the resultant accumulation of lipid glucocerebroside in tissue macrophages which become engorged and are termed Gaucher cells. Gaucher cells are typically found in liver, spleen and bone marrow. This can lead to an enlarged spleen and liver (hepatosplenomegaly). Secondary hematologic sequelae include severe anemia and thrombocytopenia. Injections of imiglucerase into Gaucher disease patients leads to elevated serum levels of the enzyme and reduction in the accumulation of glucocerebroside leading to reduced anemia and thrombocytopenia, reduced spleen and liver size, and decreased cachexia. | Imiglucerase catalyzes the hydrolysis of the glycolipid, glucocerebroside, to glucose and ceramide as part of the normal degradation pathway for membrane lipids. | NA | NA | NA | 0.09 to 0.15 L/kg | 14.5 ± 4.0 mL/min/kg | Alimentary Tract and Metabolism, Enzyme Replacement Therapy, Enzymes, Enzymes and Coenzymes, Gaucher Disease, Glucosidases, Glycoside Hydrolases, Hydrolases, Hydrolytic Lysosomal Glucocerebroside-specific Enzyme | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10331 | Th1047 | Alpha-1-proteinase inhibitor | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | 44324.5 | C2001H3130N514O601S10 | 5.37 | -0.302 | 59 | NA | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. | For treatment of panacinar emphysema. | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. | NA | NA | NA | 5632 ± 2006 mL [ARALAST NP] | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors | NA | NA | NA | NA | Neutrophil elastase | Aralast | Baxter | Baxter | Its used to treat lung problems (emphysema) caused by a certain inherited disease (alpha-1-proteinase inhibitor deficiency). In people with this condition, lung damage is caused by elastase, a natural substance that the body needs to kill bacteria in the | NA | ARALAST NP is available as a lyophilized powder in single dose vials containing 0.5 gram or 1 gram of functional Alpha 1 -Protenase inhibitor | Lyophilized powder | Intravenous infusion | Recommended dose is 60 mg/kg of body weight, administered once in a week. | ARALAST NP is contraindicated in immunoglobulin A deficient patients with antibodies against IgA, due to the risk of severe hypersensitivity. | Fever, chills, body aches, flu symptoms, sores in your mouth and throat; pain or burning when you urinate; wheezing, chest pain or tightness, trouble breathing; or vision changes. | Link | NA | NA |
| 10332 | Th1047 | Alpha-1-proteinase inhibitor | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | 44324.5 | C2001H3130N514O601S10 | 5.37 | -0.302 | 59 | NA | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. | For treatment of panacinar emphysema. | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. | NA | NA | NA | 5618 ± 1618 mL [Aralast] | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors | NA | NA | NA | NA | NA | Glassia | Takeda, Baxalta US Inc. | Takeda, Baxalta US Inc. | treat the symptoms of Alpha-1 Antitrypsin Deficiency. | NA | GLASSIA is prepared from human plasma obtained from US-licensed plasma collection centers by a modified version of the cold ethanol fractionation process and the Alpha1 -PI is then purified using chromatographic methods. | sterile, ready to use, liquid preparation of purified human alpha1 -proteinase inhibitor | intravenous | Administer 60 mg/kg body weight of GLASSIA once weekly by intravenous infusion. | GLASSIA is contraindicated in: immunoglobulin A (IgA) deficient patients with antibodies against IgA. individuals with a history of anaphylaxis or other severe systemic reaction to Alpha11-PI products. | hives, difficulty breathing, swelling of your face, lips, tongue, or throat, hives, wheezing, lightheadedness, fever, chills, body aches, flu symptoms, sores in your mouth and throat, pain or burning when you urinate, chest pain or tightness, and vision changes | Link | NA | NA |
| 10333 | Th1047 | Alpha-1-proteinase inhibitor | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | 44324.5 | C2001H3130N514O601S10 | 5.37 | -0.302 | 59 | NA | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. | For treatment of panacinar emphysema. | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. | NA | NA | NA | NA | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors | NA | NA | NA | NA | NA | Respreeza | Csl Behring | Csl Behring | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10334 | Th1047 | Alpha-1-proteinase inhibitor | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | 44324.5 | C2001H3130N514O601S10 | 5.37 | -0.302 | 59 | NA | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. | For treatment of panacinar emphysema. | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. | NA | NA | NA | NA | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors | NA | NA | NA | NA | NA | Prolastin | Talecris Biotherapeutics C formerly Bayer | Talecris Biotherapeutics C formerly Bayer | It is used to treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema. | NA | The specific activity of Prolastin is _ 0.35 mg functional alpha1-PI/mg protein and when reconstituted as directed, the concentration of alpha1-PI is _ 20 mg/mL. When reconstituted, Prolastin (alpha) has a pH of 6.6_7.4, a sodium content of 100_210 mEq/L, | Lyophilized powder | Intravenous infusion | Prolastin (alpha) may be given at a rate of 0.08 mL/kg/min or greater and must be administered intravenously. The recommended dosage of 60 mg/kg takes approximately 30 minutes to infuse. | Individuals with selective IgA deficiencies who have known antibody against IgA (anti-IgA antibody) should not receive Alpha1-Proteinase Inhibitor (Human), Prolastin (alpha) , since these patients may experience severe reactions, including anaphylaxis, to IgA which may be present. | Fever, chills, body aches, flu symptoms, sores in your mouth and throat; pain or burning when you urinate; wheezing, chest pain or tightness, trouble breathing; or vision changes. | Link | NA | NA |
| 10335 | Th1047 | Alpha-1-proteinase inhibitor | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | 44324.5 | C2001H3130N514O601S10 | 5.37 | -0.302 | 59 | NA | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. | For treatment of panacinar emphysema. | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. | NA | NA | NA | NA | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors | NA | NA | NA | NA | NA | Zemaira | Csl Behring | Csl Behring | to treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema. | NA | Zemaira is manufactured from large pools of human plasma by cold ethanol fractionation according to a modified Cohn process followed by additional purification steps. The manufacturing process includes two virus clearance steps: heat treatment at 60°C for 10 hours in an aqueous solution with stabilizers; and nanofiltration. These virus clearance steps have been validated in a series of in vitro experiments for their capacity to inactivate/ remove both enveloped and non-enveloped viruses. | sterile, white, lyophilized preparation of purified Alpha1-Proteinase Inhibitor | intravenous | The recommended dose of ZEMAIRA is 60 mg/kg body weight administered once weekly. | ZEMAIRA is contraindicated in patients with a history of anaphylaxis or severe systemic reactions to ZEMAIRA or A1-PI protein. ZEMAIRA is contraindicated in immunoglobulin A (IgA)-deficient patients with antibodies against IgA, due to the risk of severe hypersensitivity | Nausea, bloating; headache, dizziness, drowsiness; feeling tired; back pain, joint or muscle pain; swelling in your hands or feet; flushing (warmth, redness, or tingly feeling); cold symptoms such as stuffy nose, sneezing, sore throat, cough; or mild itching. | Link | NA | NA |
| 10336 | Th1047 | Alpha-1-proteinase inhibitor | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK | 44324.5 | C2001H3130N514O601S10 | 5.37 | -0.302 | 59 | NA | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. | For treatment of panacinar emphysema. | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. | NA | NA | NA | NA | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10337 | Th1048 | Pegaspargase | >Th1048_Pegaspargase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | IM: ~6 days | Pegylated L-asparagine amidohydrolase from E. coli. Pegylation substantially (by a factor of 4) extends the protein half life. | For treatment of acute lymphoblastic leukemia. | In a significant number of patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Oncaspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Pegaspargase, more effective than asparaginase, converts asparagine to aspartic acid and ammonia. It facilitates production of oxaloacetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and so the loss of exogenous sources of asparagine leads to cell death. | Adverse effects that occur more than 10% of the time include hepatotoxicity as it is known to increase serum transaminases (ALT, AST). Also known to induce hypersensitivity reactions including anaphylaxis, erythema and bronchospasm. | NA | Onset of Asparagine depletion by IM is within 4 days Time to peak: IM: 3 to 4 days | IV: Adults (asparaginase naive): 2.4 L/m2 Distributes into CSF (reportedly reducing CSF asparagine concentrations to a similar extent as asparaginase | NA | Alcohols, Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Compounds used in a research, industrial, or household setting, Delayed-Action Preparations, Enzymes, Enzymes and Coenzymes, Ethylene Glycols, Glycols, Hydrolases, Immunosuppressive Agents, Macromolecular Substances, Pegylated agents, Polymers, Thyroxine-binding globulin inhibitors | NA | NA | NA | Trastuzumab may increase the risk of neutropenia and anemia. Monitor closely for signs and symptoms of adverse events. | L-asparagine | Oncaspar | Enzon Inc, Servier Pharmaceuticals LLC, Sigma Tau Pharmaceuticals, Inc., Les Laboratoires Servier, Baxalta US Inc. | Enzon Inc, Servier Pharmaceuticals LLC, Sigma Tau Pharmaceuticals, Inc., Les Laboratoires Servier, Baxalta US Inc. | Oncaspar is indicated as a component of a multi-agent chemotherapeutic regimen for the first line treatment of patients with Acute Lymphoblastic Leukemia (ALL). | NA | Oncaspar is supplied as a clear, colorless, preservative-free, isotonic sterile solution in phosphate-buffered saline, pH 7.3. Each milliliter contains 750 ± 150 International Units of pegaspargase, dibasic sodium phosphate, USP (5.58 mg), monobasic sodiu | Solution | Intravenous or intramuSubcutaneousular administrat | The recommended dose of Oncaspar is 2,500 International Units/m_ intramuscularly or intravenously. Oncaspar should be administered no more frequently than every 14 days. When Oncaspar is administered intramuscularly, the volume at a single injection site should be limited to 2ml. | History of serious allergic reactions to Oncaspar. History of serious thrombosis with prior L-asparaginase therapy. History of pancreatitis with prior L-asparaginase therapy. History of serious hemorrhagic events with prior L-asparaginase therapy. | Hypersensitivity reactions, coagulopathy, hyperglycemia, elevated serum transaminase concentrations, hyperbilirubinemia, pancreatitis, CNS thrombosis.No apparent difference in adverse effects following IV versus IM administration. | Link | NA | NA |
| 10338 | Th1048 | Pegaspargase | >Th1048_Pegaspargase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | 3 days (range: 1.4 to 5 days) in patients with previous hypersensitivity to native L-asparaginase | Pegylated L-asparagine amidohydrolase from E. coli. Pegylation substantially (by a factor of 4) extends the protein half life. | For treatment of acute lymphoblastic leukemia | In a significant number of patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Oncaspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Pegaspargase, more effective than asparaginase, converts asparagine to aspartic acid and ammonia. It facilitates production of oxaloacetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and so the loss of exogenous sources of asparagine leads to cell death. | Adverse effects that occur more than 10% of the time include hepatotoxicity as it is known to increase serum transaminases (ALT, AST). Also known to induce hypersensitivity reactions including anaphylaxis, erythema and bronchospasm. | NA | Onset of Asparagine depletion by IM is within 4 days Time to peak: IM: 3 to 4 days | IV: Adults (asparaginase naive): 2.4 L/m2 Distributes into CSF (reportedly reducing CSF asparagine concentrations to a similar extent as asparaginase | NA | Alcohols, Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Compounds used in a research, industrial, or household setting, Delayed-Action Preparations, Enzymes, Enzymes and Coenzymes, Ethylene Glycols, Glycols, Hydrolases, Immunosuppressive Agents, Macromolecular Substances, Pegylated agents, Polymers, Thyroxine-binding globulin inhibitors | NA | NA | NA | NA | NA | Lyophilized Pegaspargase | Baxalta US Inc., Servier Pharmaceuticals | Baxalta US Inc., Servier Pharmaceuticals | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10339 | Th1048 | Pegaspargase | >Th1048_Pegaspargase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | Adults (asparaginase naive): 7 days | Pegylated L-asparagine amidohydrolase from E. coli. Pegylation substantially (by a factor of 4) extends the protein half life. | For treatment of acute lymphoblastic leukemia | In a significant number of patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Oncaspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Pegaspargase, more effective than asparaginase, converts asparagine to aspartic acid and ammonia. It facilitates production of oxaloacetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and so the loss of exogenous sources of asparagine leads to cell death. | Adverse effects that occur more than 10% of the time include hepatotoxicity as it is known to increase serum transaminases (ALT, AST). Also known to induce hypersensitivity reactions including anaphylaxis, erythema and bronchospasm. | NA | Onset of Asparagine depletion by IM is within 4 days Time to peak: IM: 3 to 4 days | IV: Adults (asparaginase naive): 2.4 L/m2 Distributes into CSF (reportedly reducing CSF asparagine concentrations to a similar extent as asparaginase | NA | Alcohols, Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Compounds used in a research, industrial, or household setting, Delayed-Action Preparations, Enzymes, Enzymes and Coenzymes, Ethylene Glycols, Glycols, Hydrolases, Immunosuppressive Agents, Macromolecular Substances, Pegylated agents, Polymers, Thyroxine-binding globulin inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10340 | Th1048 | Pegaspargase | >Th1048_Pegaspargase MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | 31731.9 | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | NA | Pegylated L-asparagine amidohydrolase from E. coli. Pegylation substantially (by a factor of 4) extends the protein half life. | For treatment of acute lymphoblastic leukemia | In a significant number of patients with acute leukemia, the malignant cells are dependent on an exogenous source of asparagine for survival. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase. Oncaspar exploits a metabolic defect in asparagine synthesis of some malignant cells. | Pegaspargase, more effective than asparaginase, converts asparagine to aspartic acid and ammonia. It facilitates production of oxaloacetate which is needed for general cellular metabolism. Some malignant cells lose the ability to produce asparagine and so the loss of exogenous sources of asparagine leads to cell death. | Adverse effects that occur more than 10% of the time include hepatotoxicity as it is known to increase serum transaminases (ALT, AST). Also known to induce hypersensitivity reactions including anaphylaxis, erythema and bronchospasm. | NA | Onset of Asparagine depletion by IM is within 4 days Time to peak: IM: 3 to 4 days | IV: Adults (asparaginase naive): 2.4 L/m2 Distributes into CSF (reportedly reducing CSF asparagine concentrations to a similar extent as asparaginase | NA | Alcohols, Amidohydrolases, Antineoplastic Agents, Antineoplastic and Immunomodulating Agents, Asparaginase, Asparagine-specific Enzyme, Compounds used in a research, industrial, or household setting, Delayed-Action Preparations, Enzymes, Enzymes and Coenzymes, Ethylene Glycols, Glycols, Hydrolases, Immunosuppressive Agents, Macromolecular Substances, Pegylated agents, Polymers, Thyroxine-binding globulin inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10341 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | CA1341604 | 4-May-2010 | 4-May-2027 | NA | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Avonex | Biogen Inc | Biogen Inc | Avonex is used to treat relapsing multiple sclerosis (MS). This medication will not cure MS, it will only decrease the frequency of relapse symptoms. | NA | AVONEX is avalible as powder vial, Single used prefillled syringe, single used prefilled autoinjector. Each vial of reconstituted AVONEX contains 30 micrograms of interferon beta-1a; 15 mg Albumin (Human), USP; 5.8 mg Sodium Chloride, USP; 5.7 mg Dibasic | Lyophilized powder vial, Sterile liquid as single used prefilled syringe and also available as single use prefilled autoinjector. | IntramuSubcutaneousular Injection | The recommended dose is 30 micrograms once a week. To reduce the incidence and severity of flu-like symptoms that may occur when initiating AVONEX therapy at a dose of 30 micrograms, AVONEX may be started at a dose of 7.5 micrograms and the dose may beincreased by 7.5 micrograms each week for the next three weeks until the recommended dose of 30 micrograms is achieved. | Hypersensitivity | Stomach pain; headache, drowsiness; or minor irritation where the injection was given. | Link | NA | NA |
| 10342 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10343 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10344 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | Betaferon | Bayer | Bayer | Betaferon is indicated for the treatment of patients with a single demyelinating event with an active inflammatory process, if it is severe enough to warrant treatment with intravenous corticosteroids, if alternative diagnoses have been excluded, and if t | NA | NA | Powder and solvent that are made upto make solution. | Subcutaneous Injection | NA | People with severe depression or thoughts of suicide. People with severe liver disease. Pregnancy. Breastfeeding. | Flu-like symptoms such as fever,chills, painful joints, malaise, sweating, headache or muscular pain. These symptoms may be reduced by taking paracetamol or steroidal anti-inflammatory medicines such as ibuprofen. | Link | NA | NA |
| 10345 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | In injection site reactions, symptoms can include redness, swelling, discolouration, inflammation and pain. These may be reduced by the use of an auto-injector device. | Link | NA | NA |
| 10346 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10347 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | Betaseron | Merck | Merck | Betaseron is used to treat relapsing multiple sclerosis (MS). Betaseron will not cure MS, it will only decrease the frequency of relapse symptoms. | NA | Lyophilized Betaseron is a sterile, white to off-white powder, for subcutaneous injection after reconstitution with the diluent supplied (Sodium Chloride, 0.54% Solution). Albumin (Human) USP and Mannitol, USP (15 mg each/vial) are added as stabilizers. | Sterile, white to off-white powder | Subcutaneous Injection | The recommended starting dose is 0.0625 mg (0.25 mL) subcutaneously every other day, with dose increases over a six week period to the recommended dose of 0.25 mg (1 mL) every other day | Betaseron is contraindicated in patients with a history of hypersensitivity to natural or recombinant interferon beta, Albumin (Human). | Depressed mood, anxiety, trouble sleeping, restlessness, or thoughts of suicide or hurting yourself; bruising, swelling, oozing, or skin changes where the injection was given; weight changes, pounding heartbeats, feeling too hot or cold; fever, chills, bo | Link | NA | NA |
| 10348 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Weakness; headache; muscle pain or weakness; sleep problems (insomnia); stomach pain; swelling in your hands or feet; skin rash; or irregular menstrual periods. | Link | NA | NA |
| 10349 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10350 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | Blastoferon | Sidus | Sidus | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10351 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | Extavia | Novartis | Novartis | Extavia is used to treat relapsing multiple sclerosis (MS). This medication will not cure MS, it will only decrease the frequency of relapse symptoms. | NA | Each vial contains 0.3 mg of interferon beta-1b. The unit measurement is derived by comparing the antiviral activity of the product to the World Health Organization (WHO) reference standard of recombinant human interferon beta. Mannitol, USP and Albumin ( | Sterile, white to off-white powder | Subcutaneous Injection | The recommended starting dose is 0.0625 mg (0.25 mL) subcutaneously every other day, with dose increases over a six week period to the recommended dose of 0.25 mg (1 mL) every other day. | Extavia is contraindicated in patients with a history of hypersensitivity to natural or recombinant interferon beta, Albumin (Human). | Depressed mood, anxiety, trouble sleeping, restlessness, or thoughts of suicide or hurting yourself; bruising, swelling, oozing, or skin changes where the injection was given; weight changes, pounding heartbeats, feeling too hot or cold; fever, chills, weating, muscle aches and tiredness. | Link | NA | NA |
| 10352 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Weakness; headache; muscle pain or weakness; sleep problems (insomnia); stomach pain; swelling in your hands or feet; skin rash; or irregular menstrual periods. | Link | NA | NA |
| 10353 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10354 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10355 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | Rebif | Merck, EMD Serono, Inc. | Merck, EMD Serono, Inc. | Rebif is used to treat relapsing multiple sclerosis (MS). This medication will not cure MS, it will only decrease the frequency of relapse symptoms. | NA | Each 0.5 mL (0.5 cc) of REBIF contains either 22 mcg or 44 mcg of interferon beta-1a, 2 mg or 4 mg albumin (human), 27.3 mg mannitol, 0.4 mg sodium acetate, and water for injection. Each 0.2 mL (0.2 cc) of REBIF contains 8.8 mcg of interferon beta-1a, 0.8 | Sterile solution in a prefilled syringe or REBIF Rebidose autoinjector | Subcutaneous Injection | The recommended dose of REBIF is either 22 mcg or 44 mcg injected subcutaneously three times per week. REBIF should be administered, if possible, at the same time (preferably in the late afternoon or evening) on the same three days (e.g., Monday, Wednesday, and Friday) at least 48 hours apart each week. | REBIF is contraindicated in patients with a history of hypersensitivity to natural or recombinant interferon beta, human albumin | Depressed mood, anxiety, trouble sleeping, restlessness, or thoughts of suicide or hurting yourself; bruising, swelling, oozing, or skin changes where the injection was given; weight changes, pounding heartbeats, feeling too hot or cold; fever, chills. | Link | NA | NA |
| 10356 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Weakness; headache; muscle pain or weakness; sleep problems (insomnia); stomach pain; swelling in your hands or feet; skin rash; or irregular menstrual periods. | Link | NA | NA |
| 10357 | Th1049 | Interferon beta-1a | >Th1049_Interferon_beta-1a MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20027 | C908H1408N246O252S7 | 8.93 | -0.427 | NA | 10 hours | Human interferon beta (166 residues, glycosylated, MW=22.5kD) is produced by mammalian cells (Chinese Hamster Ovary cells) into which the human interferon beta gene has been introduced. The amino acid sequence of Avonex is identical to that of natural human interferon beta. | For treatment of relapsing/remitting multiple sclerosis, also for condyloma acuminatum | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin and neopterin. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | NA | 33-55 L/hour [Healthy SC injection of 60 mcg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10358 | Th1050 | Pegademase bovine | >Th1050_Pegademase_bovine MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAEQCL | 40788.2 | C1821H2834N484O552S14 | 5.33 | -0.428 | NA | 72-144 hours | Bovine adenosine deaminase derived from bovine intestine that has been extensively pegylated for extended serum half life. | For treatment of adenosine deaminase deficiency | Used to replace deficient or inactive adenosine deaminase which leads to severe combined immunodeficiency disease (SCID). The enzyme is responsible for converting adenosine to inosine. In the absence of adenosine deaminase, the purine substrates adenosine 2-deoxyadenosine and their metabolites are actually toxic to lymphocytes thereby leading to diminished immune function. | Pegademase converts adenosine (toxic) to inosine (less toxic) by deamination. It also converts 2'-deoxyadenosine to 2'-deoxyinosine via deamination. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Aminohydrolases, Antineoplastic and Immunomodulating Agents, Bovine Intestinal Adenosine Deaminase, Enzymes, Enzymes and Coenzymes, Hydrolases, Nucleoside Deaminases, Pegylated agents, Severe Combined Immunodeficiency | NA | NA | NA | Krystexxa (pegloticase) | Adenosine,Growth factor receptor-bound protein 2 | Adagen | Enzon Inc. | Enzon Inc. | It is used for Treating severe combined immunodeficiency disease (SCID) in certain patients with adenosine deaminase (ADA) deficiency. | (monomethoxypolyethylene glycol succinimidyl) 11-17_ adenosine deaminase | Each ml of ADAGEN injection contains, 250 units of Pegademase bovine, 20 mg of Monobasic sodium phoshphate, USP, 5.58 mg of Dibasic sodium phoshphate, USP, 8.50 mg of Sodiium chloride, USP and q.s. to 0 ml of water for injection. | Isotonic, pyrogen free, Sterile solution, pH 7.2-7.4 | Intramusular Injection | The dosage of ADAGEN (pegademase bovine) Injection should be individualized. The recommended dosing schedule is 10 U/kg for the first dose, 15 U/kg for the second dose, and 20 U/kg for the third dose. The usual maintenance dose is 20 U/kg per week. Further increases of 5 U/kg/week may be necessary, but a maximum single dose of 30 U/kg should not be exceeded. | Allergic | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; dark urine; severe or persistent tiredness or weakness; unusual bruising or bleeding | Link | NA | NA |
| 10359 | Th1050 | Pegademase bovine | >Th1050_Pegademase_bovine MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAEQCL | 40788.2 | C1821H2834N484O552S14 | 5.33 | -0.428 | NA | 72-144 hours | Bovine adenosine deaminase derived from bovine intestine that has been extensively pegylated for extended serum half life. | For treatment of adenosine deaminase deficiency | Used to replace deficient or inactive adenosine deaminase which leads to severe combined immunodeficiency disease (SCID). The enzyme is responsible for converting adenosine to inosine. In the absence of adenosine deaminase, the purine substrates adenosine 2-deoxyadenosine and their metabolites are actually toxic to lymphocytes thereby leading to diminished immune function. | Pegademase converts adenosine (toxic) to inosine (less toxic) by deamination. It also converts 2'-deoxyadenosine to 2'-deoxyinosine via deamination. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Aminohydrolases, Antineoplastic and Immunomodulating Agents, Bovine Intestinal Adenosine Deaminase, Enzymes, Enzymes and Coenzymes, Hydrolases, Nucleoside Deaminases, Pegylated agents, Severe Combined Immunodeficiency | NA | NA | NA | Pegloticase | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Headache; pain or redness at the injection site. | Link | NA | NA |
| 10360 | Th1050 | Pegademase bovine | >Th1050_Pegademase_bovine MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAEQCL | 40788.2 | C1821H2834N484O552S14 | 5.33 | -0.428 | NA | 72-144 hours | Bovine adenosine deaminase derived from bovine intestine that has been extensively pegylated for extended serum half life. | For treatment of adenosine deaminase deficiency | Used to replace deficient or inactive adenosine deaminase which leads to severe combined immunodeficiency disease (SCID). The enzyme is responsible for converting adenosine to inosine. In the absence of adenosine deaminase, the purine substrates adenosine 2-deoxyadenosine and their metabolites are actually toxic to lymphocytes thereby leading to diminished immune function. | Pegademase converts adenosine (toxic) to inosine (less toxic) by deamination. It also converts 2'-deoxyadenosine to 2'-deoxyinosine via deamination. | NA | NA | NA | NA | NA | Adjuvants, Immunologic, Aminohydrolases, Antineoplastic and Immunomodulating Agents, Bovine Intestinal Adenosine Deaminase, Enzymes, Enzymes and Coenzymes, Hydrolases, Nucleoside Deaminases, Pegylated agents, Severe Combined Immunodeficiency | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 10376 | Th1057 | Interferon beta-1b | >Th1057_Interferon_beta-1b SYNLLGFLQRSSNFQSQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20011 | C908H1408N246O253S6 | 9.02 | -0.447 | NA | 10-20 minutes | Human interferon beta (165 residues), cysteine 17 is substituted with serine. Produced in E. coli, no carbohydrates, MW=18.5kD. | Interferon beta-1b is a drug used for the treatment of relapsing/remitting multiple sclerosis. It has been shown to slow the advance of the disease as well as to decrease the frequency of attacks. | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | 0.25 to 2,88 L/kg | 9.4 - 28.9 mL/min/kg [patients with diseases other than MS receiving single intravenous doses up to 2.0 mg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Myelosuppressive Agents, Peptides, Proteins, Recombinant Human Interferon beta | CA1340861 | 28-Dec-1999 | 28-Dec-2016 | NA | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Betaseron | Bayer | Bayer | Betaseron is used to treat relapsing multiple sclerosis (MS). Betaseron will not cure MS, it will only decrease the frequency of relapse symptoms. | NA | Each vial contains 0.3 mg of interferon beta-lb. The unit measurement is derived by comparing the antiviral activity of the product to the World Health Organization (WHO) reference standard of recombinant human interferon beta. Mannitol, USP and Albumin (Human), USP (15 mg each/vial) are added as stabilizers. | Sterile, white to off-white powder | Subcutaneous Injection | The recommended starting dose is 0.0625 mg (0.25 mL) subcutaneously every other day, with dose increases over a six week period to the recommended dose of 0.25 mg (1 mL) every other day. | Betaseron is contraindicated in patients with a history of hypersensitivity to natural or recombinant interferon beta, Albumin (Human), | serious side effects: depressed mood, anxiety, trouble sleeping, restlessness, or thoughts of suicide or hurting yourself; bruising, swelling, oozing, or skin changes where the injection was given; weight changes, pounding heartbeats, feeling too hot or cold; fever, chills, body aches, flu symptoms; or nausea, stomach pain, low fever, loss of appetite, dark urine, clay-colored stools, jaundice (yellowing of the skin or eyes). | Link | NA | NA |
| 10377 | Th1057 | Interferon beta-1b | >Th1057_Interferon_beta-1b SYNLLGFLQRSSNFQSQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20011 | C908H1408N246O253S7 | 9.02 | -0.447 | NA | 10-20 minutes | Human interferon beta (165 residues), cysteine 17 is substituted with serine. Produced in E. coli, no carbohydrates, MW=18.5kD. | Interferon beta-1b is a drug used for the treatment of relapsing/remitting multiple sclerosis. It has been shown to slow the advance of the disease as well as to decrease the frequency of attacks. | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | 0.25 to 2,88 L/kg | 9.4 - 28.9 mL/min/kg [patients with diseases other than MS receiving single intravenous doses up to 2.0 mg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Myelosuppressive Agents, Peptides, Proteins, Recombinant Human Interferon beta | CA1339707 | 10-Mar-1998 | 10-Mar-2015 | NA | NA | Betaferon | Bayer | Bayer | Betaferon is indicated for the treatment of patients with a single demyelinating event with an active inflammatory process, if it is severe enough to warrant treatment with intravenous corticosteroids, if alternative diagnoses have been excluded, and if they are determined to be at high risk of developing clinically definite multiple sclerosis; patients with relapsing-remitting multiple sclerosis and two or more relapses within the last two years; patients with secondary progressive multiple sclerosis with active disease, evidenced by relapses. | NA | NA | Powder and solvent that are made upto make solution. | Subcutaneous Injection | NA | People with severe depression or thoughts of suicide; People with severe liver disease; Pregnancy; Breastfeeding. | The most frequently observed side-effects are: Flu-like symptoms- such as fever,chills, painful joints, malaise, sweating, headache or muscular pain. These symptoms may be reduced by taking paracetamol or steroidal anti-inflammatory medicines such as ibuprofen. Injection site reactions. - Symptoms can include redness, swelling, discolouration, inflammation and pain. These may be reduced by the use of an auto-injector device. | Link | NA | NA |
| 10378 | Th1057 | Interferon beta-1b | >Th1057_Interferon_beta-1b SYNLLGFLQRSSNFQSQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN | 20011 | C908H1408N246O253S8 | 9.02 | -0.447 | NA | 10-20 minutes | Human interferon beta (165 residues), cysteine 17 is substituted with serine. Produced in E. coli, no carbohydrates, MW=18.5kD. | Interferon beta-1b is a drug used for the treatment of relapsing/remitting multiple sclerosis. It has been shown to slow the advance of the disease as well as to decrease the frequency of attacks. | Interferon beta upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Type I interferons also induce the synthesis of several key antiviral mediators including 2'-5' oligoadenylate synthetase (2'-5' A synthetase), beta-2 microglobulin, neopterin and protein kinase R. | Interferon beta binds to type I interferon receptors (IFNAR1 and IFNAR2c) which activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon beta binds more stably to type I interferon receptors than interferon alpha. | NA | NA | NA | 0.25 to 2,88 L/kg | 9.4 - 28.9 mL/min/kg [patients with diseases other than MS receiving single intravenous doses up to 2.0 mg] | Adjuvants, Immunologic, Amino Acids, Peptides, and Proteins, Antineoplastic and Immunomodulating Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunologic Factors, Immunomodulatory Agents, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-beta, Interferons, Myelosuppressive Agents, Peptides, Proteins, Recombinant Human Interferon beta | NA | NA | NA | NA | NA | Extavia | Novartis | Novartis | Extavia is used to treat relapsing multiple sclerosis (MS). This medication will not cure MS, it will only decrease the frequency of relapse symptoms. | NA | Each vial contains 0.3 mg of interferon beta-1b. The unit measurement is derived by comparing the antiviral activity of the product to the World Health Organization (WHO) reference standard of recombinant human interferon beta. Mannitol, USP and Albumin (Human), USP (15 mg each/vial) are added as stabilizers. | Sterile, white to off-white powder | Subcutaneous Injection | The recommended starting dose is 0.0625 mg (0.25 mL) subcutaneously every other day, with dose increases over a six week period to the recommended dose of 0.25 mg (1 mL) every other day. | Extavia is contraindicated in patients with a history of hypersensitivity to natural or recombinant interferon beta, Albumin (Human), | serious side effects: depressed mood, anxiety, trouble sleeping, restlessness, or thoughts of suicide or hurting yourself; bruising, swelling, oozing, or skin changes where the injection was given; weight changes, pounding heartbeats, feeling too hot or cold; fever, chills, body aches, flu symptoms; or nausea, stomach pain, low fever, loss of appetite, dark urine, clay-colored stools, jaundice (yellowing of the skin or eyes). | Link | NA | NA |
| 10379 | Th1058 | Interferon alfacon-1 | >Th1058_Interferon_alfacon-1 MCDLPQTHSLGNRRALILLAQMRRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSAAWDESLLEKFYTELYQQLNDLEACVIQEVGVEETPLMNVDSILAVKKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSTNLQERLRRKE | 19343 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | 1.3 hours in golden Syrian hamsters and 3.4 hours in rhesus monkeys. | Recombinant type-I Interferon alpha 2b (human leukocyte clone hif-sn 206 protein moiety reduced), composed of 165 amino acid residues with R at position 23. It resembles leukocyte secreted interferon. Widely used as an antiviral or antineoplastic agent. | For the treatment of hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | There is limited experience with overdosage. Postmarketing surveillance includes reports of patients receiving a single dose as great as 10 times the recommended dose. In general, the primary effects of an overdose are consistent with the effects seen with therapeutic doses of interferon alfa-2b. Hepatic enzyme abnormalities, renal failure, hemorrhage, and myocardial infarction have been reported with single administration overdoses and/or with longer durations of treatment than prescribed. Toxic effects after ingestion of interferon alfa-2b are not expected because interferons are poorly absorbed orally. | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | NA | NA | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | CA1341567 | 19-Feb-2008 | 19-Feb-2025 | Zidovudine, The interferon increases the effect and toxicity of zidovudine | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | INFERGEN | Kadmon Pharmaceuticals, LLC., Valeant Pharmaceuticals, Inc., Three Rivers Pharmaceuticals Llc | Kadmon Pharmaceuticals, LLC., Valeant Pharmaceuticals, Inc., Three Rivers Pharmaceuticals Llc | INFERGEN (interferon alfacon-1) is indicated for treatment of chronic hepatitis C in patients 18 years of age or older with compensated liver disease. | NA | single-use vials containing 9 mcg and 15 mcg interferon alfacon-1 at a fill volume of 0.3 mL and 0.5 mL, respectively. INFERGEN vials contain 0.03 mg/mL interferon alfacon-1, sodium chloride (5.9 mg/mL), and sodium phosphate (3.8 mg/mL) in Water for Injection, USP. | INFERGEN is a Sterile, clear, colorless, preservative-free liquid | Subcutaneous Injection | The recommended dose of INFERGEN monotherapy for the initial treatment of chronic HCV infection is 9 mcg administered three times a week as a single subcutaneous injection for 24 weeks. | contraindicated in patients with hepatic decompensation; autoimmune hepatitis; known hypersensitivity reactions such as urticaria, angioedema, bronchoconstriction, anaphylaxis to interferon alphas or to any component of the product. | INFERGEN alone or in combination with ribavirin causes a broad range of serious adverse reactions; | Link | NA | NA |
| 10380 | Th1058 | Interferon alfacon-1 | >Th1058_Interferon_alfacon-1 MCDLPQTHSLGNRRALILLAQMRRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSAAWDESLLEKFYTELYQQLNDLEACVIQEVGVEETPLMNVDSILAVKKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSTNLQERLRRKE | 19343 | C860H1353N227O255S9 | 5.99 | -0.336 | 61 | 1.3 hours in golden Syrian hamsters and 3.4 hours in rhesus monkeys. | Recombinant type-I Interferon alpha 2b (human leukocyte clone hif-sn 206 protein moiety reduced), composed of 165 amino acid residues with R at position 23. It resembles leukocyte secreted interferon. Widely used as an antiviral or antineoplastic agent. | For the treatment of hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which upon dimerization activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | There is limited experience with overdosage. Postmarketing surveillance includes reports of patients receiving a single dose as great as 10 times the recommended dose. In general, the primary effects of an overdose are consistent with the effects seen with therapeutic doses of interferon alfa-2b. Hepatic enzyme abnormalities, renal failure, hemorrhage, and myocardial infarction have been reported with single administration overdoses and/or with longer durations of treatment than prescribed. Toxic effects after ingestion of interferon alfa-2b are not expected because interferons are poorly absorbed orally. | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | NA | NA | Adjuvants, Immunologic, Alfa Interferons, Amino Acids, Peptides, and Proteins, Anti-Infective Agents, Antineoplastic and Immunomodulating Agents, Antiviral Agents, Biological Factors, Cytochrome P-450 CYP1A2 Inhibitors, Cytochrome P-450 CYP1A2 Inhibitors (strength unknown), Cytochrome P-450 Enzyme Inhibitors, Cytokines, Immunosuppressive Agents, Intercellular Signaling Peptides and Proteins, Interferon alpha, Interferon Type I, Interferons, Myelosuppressive Agents, Peptides, Proteins | CA2201749 | 15-Jun-1999 | 10-Oct-2015 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10381 | Th1059 | Hyaluronidase | >Th1059_Hyaluronidase MWTGLGPAVTLALVLVVAWATELKPTAPPIFTGRPFVVAWDVPTQDCGPR | 53870.9 | C2455H3775N617O704S21 | 5.73 | -0.117 | NA | 0.03 hours | Highly purified sheep hyaluronidase for administration by injection into the vitreous of the eye. | For increase of absorption and distribution of other injected drugs and for rehydration. | Hyaluronidase hydrolyzes hyaluronic acid and increase diffusion of injected drugs, thus facilitating their absorption. Hyaluronidase is used for enhancing absorption and distribution of other injected drugs. | Hyaluronidase is a spreading or diffusing substance. It increase the permeability of connective tissue through the hydrolysis of hyaluronic acid. Hyaluronidase hydrolyzes hyaluronic acid by splitting the glucosaminidic bond between C1 of the glucosamine moiety and C4 of glucuronic acid. This temporarily decreases the viscosity of the cellular cement and increases diffusion of injected fluids or of localized transudates or exudates, thus facilitating their absorption. | NA | NA | NA | NA | NA | Blood and Blood Forming Organs, Carbon-Oxygen Lyases, Enzymes, Enzymes and Coenzymes, Glycoside Hydrolases, Hyaluronoglucosaminidase, antagonists & inhibitors, Hydrolases, Lyases, Polysaccharide-Lyases | NA | NA | NA | NA | Hyaluronic acid, Transforming growth factor beta-1 | HYLENEX | Baxter Healthcare Corporation | Baxter Healthcare Corporation | HYLENEX recombinant is indicated as an adjuvant in subcutaneous fluid administration for achieving hydration, to increase the dispersion and absorption of other injected drug and an adjunct in subcutaneous urography for improving resorption of radioopque agents | NA | Each mL contains 150 USP units of recombinant human hyaluronidase with 8.5 mg sodium chloride, 1.4 mg dibasic sodium phosphate, 1.0 mg albumin human, 0.9 mg edentate disodium, 0.3 mg calcium chloride, and sodium hydroxide added for pH adjustment. | HYLENEX recombinant (hyaluronidase human injection) is supplied as a Sterile, clear, colorless, nonpreserved, ready for use solution. | human Injection Subcutaneous use | Most typically 150 U hyaluronidaseare used to the injection (hyaluronidase human injection) for the subcutaneous fluid administration, will facilitate absorption of 1,000 mL or more of solution. | HYLENEX is contraindicated in patients with known hypersensitivity to hyaluronidase or any of the excipients | adverse experiences have been mild local injection site reactions such as erythema and pain. Edema has been reported most frequently. | Link | NA | NA |
| 10382 | Th1060 | Insulin, porcine | >Th1060_Insulin,_porcine GIVEQCCTSICSLYQLENYCN | 5795.6 | C257H387N65O76S6 | 5.39 | 0.218 | NA | 0.03 hours | Insulin isolated from pig pancreas. Composed of alpha and beta chains, processed from pro-insulin. Forms a hexameric structure. | For the treatment of type I and II diabetes mellitus. | Insulin is used in the treatment of type I and type II diabetes. The primary activity of insulin is the regulation of glucose metabolism. In muscle and other tissues (except the brain), insulin causes rapid transport of glucose and amino acids intracellularly. It also promotes anabolism, and inhibits protein catabolism. In the liver, insulin promotes the uptake and storage of glucose in the form of glycogen, inhibits gluconeogenesis, and promotes the conversion of excess glucose into fat. | Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism. | NA | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | NA | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Insulin, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides, Proteins | NA | NA | NA | NA | Interferon alpha/beta receptor 2,Interferon alpha/beta receptor 1 | vetsulin | Intervet Inc (Merck Animal Health) | Intervet Inc (Merck Animal Health) | vetsulin (porcine insulin zinc suspension) is indicated for the reduction of hyperglycemia and hyperglycemia-associated clinical signs in dogs and cats with diabetes mellitus | NA | purified porcine insulin 40 IU (35% amorphous and 65% crystalline), Zinc (as chloride) 0.08 mg, Sodium acetate trihydrate 1.36 mg, Sodium chloride 7.0 mg, Methylparaben (preservative) 1.0 mg, pH is adjusted with hydrochloric acid and/or sodium hydroxide. | Vetsulin is supplied as a sterile injectable suspension in multidose vials containing 10 mL of 40 IU/mL porcine insulin zinc suspension. Vials are supplied in cartons of one, 10 mL vial. | Subcutaneous Injection | In dogs: The initial recommended vetsulin dose is 0.5 IU insulin/kg body weight. Initially, this dose should be given once daily concurrently with, or right after a meal; In Cats:The initial recommended dose in cats is 1 to 2 IU per injection. The injections should be given twice daily at approximately 12 hour intervals. | Dogs and cats known to have a systemic allergy to pork or pork products should not be treated with vetsulin. vetsulin is contraindicated during periods of hypoglycemia. | In dogs: Clinical signs of hypoglycemia were generally mild in nature (described as weakness, lethargy, stumbling, falling down, and/or depression, hematuria, vomiting, diarrhea, pancreatitis, non-specific hepatopathy/pancreatitis, development of cataracts, and urinary tract infections. In Cats: omiting, lethargy, diarrhea, decreased appetite/anorexia, pancreatitis, dermal events, respiratory disease, urinary tract disorder, renal disease, dehydration, weight loss, polydipsia, polyuria, behavioral change, and ocular discharge/conjunctivitis. | Link | NA | NA |
| 10383 | Th1060 | Insulin, porcine | >Th1060_Insulin,_porcine GIVEQCCTSICSLYQLENYCN | 5795.6 | C257H387N65O76S6 | 5.39 | 0.218 | NA | 0.03 hours | Insulin isolated from pig pancreas. Composed of alpha and beta chains, processed from pro-insulin. Forms a hexameric structure. | For the treatment of type I and II diabetes mellitus. | Insulin is used in the treatment of type I and type II diabetes. The primary activity of insulin is the regulation of glucose metabolism. In muscle and other tissues (except the brain), insulin causes rapid transport of glucose and amino acids intracellularly. It also promotes anabolism, and inhibits protein catabolism. In the liver, insulin promotes the uptake and storage of glucose in the form of glycogen, inhibits gluconeogenesis, and promotes the conversion of excess glucose into fat. | Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism. | NA | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | NA | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Insulin, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides, Proteins | NA | NA | NA | NA | Insulin-like growth factor 1 receptor, Insulin receptor | Hypurin | Wockhardt Uk Ltd | Wockhardt Uk Ltd | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10384 | Th1060 | Insulin, porcine | >Th1060_Insulin,_porcine GIVEQCCTSICSLYQLENYCN | 5795.6 | C257H387N65O76S6 | 5.39 | 0.218 | NA | 0.03 hours | Insulin isolated from pig pancreas. Composed of alpha and beta chains, processed from pro-insulin. Forms a hexameric structure. | For the treatment of type I and II diabetes mellitus. | Insulin is used in the treatment of type I and type II diabetes. The primary activity of insulin is the regulation of glucose metabolism. In muscle and other tissues (except the brain), insulin causes rapid transport of glucose and amino acids intracellularly. It also promotes anabolism, and inhibits protein catabolism. In the liver, insulin promotes the uptake and storage of glucose in the form of glycogen, inhibits gluconeogenesis, and promotes the conversion of excess glucose into fat. | Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism. | NA | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | NA | NA | NA | Alimentary Tract and Metabolism, Amino Acids, Peptides, and Proteins, Blood Glucose Lowering Agents, Cytochrome P-450 CYP1A2 Inducers, Cytochrome P-450 CYP1A2 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Drugs Used in Diabetes, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Insulin, Insulin, Short-Acting, Insulins and Analogues for Injection, Fast-Acting, Pancreatic Hormones, Peptide Hormones, Peptides, Proteins | NA | NA | NA | NA | Hyaluronan,Transforming growth factor beta-1 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10415 | Th1069 | Pegvisomant | >Th1069_Pegvisomant FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | 22129 | C990H1532N262O300S7 | 5.27 | -0.411 | 76 | 6 days | Pegvisomant is a highly selective growth hormone (GH) receptor antagonist. It is used to treat acromegaly. Unlike dopamine or somatostatin analogs (which inhibit growth hormone secretion), this drug actually blocks the hepatic (GH-mediated) production of insulin like growth factor (IGF-1), which is the main mediator of growth hormone activity. | Pegvisomant is a growth hormone receptor antagonist used for the treatment of acromegaly. | Somavert is used for the treatment of acromegaly, which arises from excessive IGF-1 levels. Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH, and thus interferes with GH signal transduction. Inhibition of GH action results in decreased serum concentrations of insulin-like growth factor-I (IGF-I), and IGF binding protein-3 (IGFBP-3). This reduces the symptoms of acromegaly. | Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH. This leads to the normalization of serum IGF-1 levels. | NA | NA | NA | 7 L | 36 ± 28 mL/h [SC doses ranging from 10 to 20 mg/day] | Acromegaly, Amino Acids, Peptides, and Proteins, Anterior Pituitary Lobe Hormones and Analogues, Cholinesterase Inhibitors, Cytochrome P-450 CYP3A Inducers, Cytochrome P-450 CYP3A4 Inducers, Cytochrome P-450 CYP3A4 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Growth Hormone Receptor Antagonist, Growth Hormone Receptor Antagonists, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Pegylated agents, Peptide Hormones, Peptides, Pituitary and Hypothalamic Hormones and Analogues, Pituitary Hormones, Pituitary Hormones, Anterior, Somatotropin Antagonists, Systemic Hormonal Preparations, Excl. Sex Hormones and Insulins | US5849535 | 15-Dec-1998 | 25-Mar-2017 | Dihydrocodeine opioids may diminish the therapeutic effect of pegvisomant. It is recommended to monitor therapy | Growth hormone receptor | SOMAVERT | Pfizer | Pfizer | SOMAVERT is indicated for the treatment of acromegaly in patients who have had an inadequate response to surgery or radiation therapy, or for whom these therapies are not appropriate. The goal of treatment is to normalize serum insulin-like growth factor-I (IGF-I) levels. | NA | SOMAVERT is available in single-dose sterile vials containing 10, 15, or 20 mg of pegvisomant protein (approximately 10, 15, and 20 U activity, respectively). Each vial also contains 1.36 mg of glycine, 36.0 mg of mannitol, 1.04 mg of sodium phosphate dibasic anhydrous, and 0.36 mg of sodium phosphate monobasic monohydrate | SOMAVERT for injection is supplied as a Sterile, white lyophilized powder | Subcutaneous Injection | The recommended loading dose of SOMAVERT is 40 mg given subcutaneously, under healthcare provider supervision. Increase the dosage by 5 mg increments every 4-6 weeks if IGF-I concentrations are elevated.Decrease the dosage by 5 mg decrements every 4-6 weeks if IGF-I concentrations are below the normal range. | None. | Hypoglycemia associated with GH lowering in patients with Diabetes Mellitus, Liver test elevations, Cross-reactivity with GH assay, Lipohypertrophy, Systemic hypersensitivity, pain, nausea ,diarrhea, dizziness, Sinusitis | Link | NA | NA |
| 10416 | Th1069 | Pegvisomant | >Th1069_Pegvisomant FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | 22129 | C990H1532N262O300S7 | 5.27 | -0.411 | 76 | 6 days | Pegvisomant is a highly selective growth hormone (GH) receptor antagonist. It is used to treat acromegaly. Unlike dopamine or somatostatin analogs (which inhibit growth hormone secretion), this drug actually blocks the hepatic (GH-mediated) production of insulin like growth factor (IGF-1), which is the main mediator of growth hormone activity. | Pegvisomant is a growth hormone receptor antagonist used for the treatment of acromegaly. | Somavert is used for the treatment of acromegaly, which arises from excessive IGF-1 levels. Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH, and thus interferes with GH signal transduction. Inhibition of GH action results in decreased serum concentrations of insulin-like growth factor-I (IGF-I), and IGF binding protein-3 (IGFBP-3). This reduces the symptoms of acromegaly. | Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH. This leads to the normalization of serum IGF-1 levels. | NA | NA | NA | 7 L | 36 ± 28 mL/h [SC doses ranging from 10 to 20 mg/day] | Acromegaly, Amino Acids, Peptides, and Proteins, Anterior Pituitary Lobe Hormones and Analogues, Cholinesterase Inhibitors, Cytochrome P-450 CYP3A Inducers, Cytochrome P-450 CYP3A4 Inducers, Cytochrome P-450 CYP3A4 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Growth Hormone Receptor Antagonist, Growth Hormone Receptor Antagonists, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Pegylated agents, Peptide Hormones, Peptides, Pituitary and Hypothalamic Hormones and Analogues, Pituitary Hormones, Pituitary Hormones, Anterior, Somatotropin Antagonists, Systemic Hormonal Preparations, Excl. Sex Hormones and Insulins | US5350836 | 27-Sep-1994 | 27-Sep-2011 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10417 | Th1069 | Pegvisomant | >Th1069_Pegvisomant FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | 22129 | C990H1532N262O300S7 | 5.27 | -0.411 | 76 | 6 days | Pegvisomant is a highly selective growth hormone (GH) receptor antagonist. It is used to treat acromegaly. Unlike dopamine or somatostatin analogs (which inhibit growth hormone secretion), this drug actually blocks the hepatic (GH-mediated) production of insulin like growth factor (IGF-1), which is the main mediator of growth hormone activity. | Pegvisomant is a growth hormone receptor antagonist used for the treatment of acromegaly. | Somavert is used for the treatment of acromegaly, which arises from excessive IGF-1 levels. Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH, and thus interferes with GH signal transduction. Inhibition of GH action results in decreased serum concentrations of insulin-like growth factor-I (IGF-I), and IGF binding protein-3 (IGFBP-3). This reduces the symptoms of acromegaly. | Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH. This leads to the normalization of serum IGF-1 levels. | NA | NA | NA | 7 L | 36 ± 28 mL/h [SC doses ranging from 10 to 20 mg/day] | Acromegaly, Amino Acids, Peptides, and Proteins, Anterior Pituitary Lobe Hormones and Analogues, Cholinesterase Inhibitors, Cytochrome P-450 CYP3A Inducers, Cytochrome P-450 CYP3A4 Inducers, Cytochrome P-450 CYP3A4 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Growth Hormone Receptor Antagonist, Growth Hormone Receptor Antagonists, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Pegylated agents, Peptide Hormones, Peptides, Pituitary and Hypothalamic Hormones and Analogues, Pituitary Hormones, Pituitary Hormones, Anterior, Somatotropin Antagonists, Systemic Hormonal Preparations, Excl. Sex Hormones and Insulins | CA2230492 | 26-May-2009 | 20-Sep-2016 | NA | B-lymphocyte antigen CD20,Low affinity immunoglobulin gamma Fc region receptor III-B,Complement C1r subcomponent,Complement C1q subcomponent subunit A,Complement C1q subcomponent subunit B,Complement C1q subcomponent subunit C,Low affinity immunoglobulin gamma Fc region receptor III-A,High affinity immunoglobulin gamma Fc receptor I,Low affinity immunoglobulin gamma Fc region receptor II-a,Low affinity immunoglobulin gamma Fc region receptor II-b,Low affinity immunoglobulin gamma Fc region receptor II-c | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10418 | Th1069 | Pegvisomant | >Th1069_Pegvisomant FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | 22129 | C990H1532N262O300S7 | 5.27 | -0.411 | 76 | 6 days | Pegvisomant is a highly selective growth hormone (GH) receptor antagonist. It is used to treat acromegaly. Unlike dopamine or somatostatin analogs (which inhibit growth hormone secretion), this drug actually blocks the hepatic (GH-mediated) production of insulin like growth factor (IGF-1), which is the main mediator of growth hormone activity. | Pegvisomant is a growth hormone receptor antagonist used for the treatment of acromegaly. | Somavert is used for the treatment of acromegaly, which arises from excessive IGF-1 levels. Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH, and thus interferes with GH signal transduction. Inhibition of GH action results in decreased serum concentrations of insulin-like growth factor-I (IGF-I), and IGF binding protein-3 (IGFBP-3). This reduces the symptoms of acromegaly. | Somavert selectively binds to growth hormone (GH) receptors on cell surfaces, where it blocks the binding of endogenous GH. This leads to the normalization of serum IGF-1 levels. | NA | NA | NA | 7 L | 36 ± 28 mL/h [SC doses ranging from 10 to 20 mg/day] | Acromegaly, Amino Acids, Peptides, and Proteins, Anterior Pituitary Lobe Hormones and Analogues, Cholinesterase Inhibitors, Cytochrome P-450 CYP3A Inducers, Cytochrome P-450 CYP3A4 Inducers, Cytochrome P-450 CYP3A4 Inducers (strength unknown), Cytochrome P-450 Enzyme Inducers, Growth Hormone Receptor Antagonist, Growth Hormone Receptor Antagonists, Hormones, Hormones, Hormone Substitutes, and Hormone Antagonists, Hypoglycemia-Associated Agents, Pegylated agents, Peptide Hormones, Peptides, Pituitary and Hypothalamic Hormones and Analogues, Pituitary Hormones, Pituitary Hormones, Anterior, Somatotropin Antagonists, Systemic Hormonal Preparations, Excl. Sex Hormones and Insulins | CA2102129 | 1-Apr-2003 | 1-May-2012 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10419 | Th1070 | Botulinum Toxin Type A | >Th1070_Botulinum_Toxin_Type_A MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL | 900000 | C6760H10447N1743O2010S32 | 5.6 | -0.368 | 85.5-86.5 | 230 to 260 min in a pharmacokinetic study of rats and mice | Purified botulinum toxin from Clostridium botulinum, purified from culture via dialysis and acid precipitation. | For the treatment of cervical dystonia in adults to decrease the severity of abnormal head position and neck pain associated with cervical dystonia. Also for the treatment of severe primary axillary hyperhidrosis that is inadequately managed with topical agents and for the treatment of strabismus and blepharospasm associated with dystonia, including benign essential blepharospasm or VII nerve disorders in patients 12 years of age and above. Also used cosmetically to temporarily improve the appearance of moderate-to-severe frown lines between the eyebrows (glabellar lines) as well as for the treatment of excessive underarm sweating. | A 150 kDa neurotoxic protein produced from fermentation of Hall strain Clostridium botulinum type A grown in a medium containing casein hydrolysate, glucose and yeast extract. It is purified from the culture solution by dialysis and a series of acid precipitations to a complex consisting of the neurotoxin, and several accessory proteins. Botulinum Toxin Type A is not expected to be present in the peripheral blood at measurable levels following IM or intradermal injection at the recommended doses. The recommended quantities of neurotoxin administered at each treatment session are not expected to result in systemic, overt distant clinical effects, i.e. muscle weakness, in patients without other neuromuscular dysfunction. However, sub-clinical systemic effects have been shown by single-fiber electromyography after IM doses of botulinum toxins appropriate to produce clinically observable local muscle weakness. | Botulinum Toxin Type A blocks neuromuscular transmission by binding to acceptor sites on motor or sympathetic nerve terminals, entering the nerve terminals, and inhibiting the release of acetylcholine. This inhibition occurs as the neurotoxin cleaves SNAP-25, a protein integral to the successful docking and release of acetylcholine from vesicles situated within nerve endings. | Based on toxicological studies, it has been estimated that the human LD50 by injection is approximately 2800 Units, equivalent to 28 individual vials of BOTOX (Botulinum Toxin Type A) Purified Neurotoxin Complex (100 Units) for a 70 kg adult. When injected intramuscularly, Botulinum Toxin Type A has been shown to be teratogenic or to have embryocidal effects in some animal species. | NA | The chemical complexity of Botulinum Toxin Type A combined with its extreme potency limits the opportunity to study its pharmacokinetic profile in humans. Therefore, no human pharmacokinetic studies have been performed. Botulinum Toxin Type A is injected directly into the target organ, a skeletal muscle. Thus, bioavailability of the intravenous or oral route is not of clinical relevance. | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Botulinum Toxins, Type A, Central Nervous System Depressants, Cholinergic Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neuromuscular Agents, Neuromuscular Blocking Agents, Neurotoxins, Neurotransmitter Agents, Noxae, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Peripheral Nervous System Agents, Proteins, Toxic Actions, Toxins, Biological | CA2280565 | 15-Nov-2005 | 20-Aug-2019 | NA | Synaptosomal-associated protein 25,Rho-related GTP-binding protein RhoB | BOTOX | Allergan | Allergan | Prescribed in cases such as Bladder Dysfunction, Chronic Migraine, Upper Limb Spasticity, Cervical Dystonia, Primary Axillary Hyperhidrosis, Blepharospasm and Strabismus | NA | Each vial of BOTOX contains either 50 Units of Clostridium botulinum type A neurotoxin complex, 0.25 mg of Albumin Human, and 0.45 mg of sodium chloride; 100 Units of Clostridium botulinum type A neurotoxin complex, 0.5 mg of Albumin Human, and 0.9 mg of sodium chloride; or 200 Units of Clostridium botulinum type A neurotoxin complex, 1 mg of Albumin Human, and 1.8 mg of sodium chloride in a sterile, vacuum-dried form without a preservative. | BOTOX (onabotulinum toxin A) For Injection is a sterile, vacuum-dried purified botulinum toxin type A, produced from fermentation of Hall strainClostridium botulinum type A | IntramuSubcutaneousular, intradetrusor and intrade | Do not exceed a total dose of 360 Units administered in a 3 month interval. | Known Hypersensitivity to Botulinum Toxin, Infection at the Injection Site, Urinary Tract Infection or Urinary Retention. | Spread of Toxin Effects, Hypersensitivity, Dysphagia and Breathing Difficulties in Treatment of Cervical Dystonia, Bronchitis and Upper Respiratory Tract Infections in Patients Treated for Spasticity, Urinary Retention in Patients Treated for Bladder Dysfunction. | Link | NA | NA |
| 10420 | Th1070 | Botulinum Toxin Type A | >Th1070_Botulinum_Toxin_Type_A MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL | 900000 | C6760H10447N1743O2010S32 | 5.6 | -0.368 | 85.5-86.6 | 230 to 260 min in a pharmacokinetic study of rats and mice | Purified botulinum toxin from Clostridium botulinum, purified from culture via dialysis and acid precipitation. | For the treatment of cervical dystonia in adults to decrease the severity of abnormal head position and neck pain associated with cervical dystonia. Also for the treatment of severe primary axillary hyperhidrosis that is inadequately managed with topical agents and for the treatment of strabismus and blepharospasm associated with dystonia, including benign essential blepharospasm or VII nerve disorders in patients 12 years of age and above. Also used cosmetically to temporarily improve the appearance of moderate-to-severe frown lines between the eyebrows (glabellar lines) as well as for the treatment of excessive underarm sweating. | A 150 kDa neurotoxic protein produced from fermentation of Hall strain Clostridium botulinum type A grown in a medium containing casein hydrolysate, glucose and yeast extract. It is purified from the culture solution by dialysis and a series of acid precipitations to a complex consisting of the neurotoxin, and several accessory proteins. Botulinum Toxin Type A is not expected to be present in the peripheral blood at measurable levels following IM or intradermal injection at the recommended doses. The recommended quantities of neurotoxin administered at each treatment session are not expected to result in systemic, overt distant clinical effects, i.e. muscle weakness, in patients without other neuromuscular dysfunction. However, sub-clinical systemic effects have been shown by single-fiber electromyography after IM doses of botulinum toxins appropriate to produce clinically observable local muscle weakness. | Botulinum Toxin Type A blocks neuromuscular transmission by binding to acceptor sites on motor or sympathetic nerve terminals, entering the nerve terminals, and inhibiting the release of acetylcholine. This inhibition occurs as the neurotoxin cleaves SNAP-25, a protein integral to the successful docking and release of acetylcholine from vesicles situated within nerve endings. | Based on toxicological studies, it has been estimated that the human LD50 by injection is approximately 2800 Units, equivalent to 28 individual vials of BOTOX (Botulinum Toxin Type A) Purified Neurotoxin Complex (100 Units) for a 70 kg adult. When injected intramuscularly, Botulinum Toxin Type A has been shown to be teratogenic or to have embryocidal effects in some animal species. | NA | The chemical complexity of Botulinum Toxin Type A combined with its extreme potency limits the opportunity to study its pharmacokinetic profile in humans. Therefore, no human pharmacokinetic studies have been performed. Botulinum Toxin Type A is injected directly into the target organ, a skeletal muscle. Thus, bioavailability of the intravenous or oral route is not of clinical relevance. | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Botulinum Toxins, Type A, Central Nervous System Depressants, Cholinergic Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neuromuscular Agents, Neuromuscular Blocking Agents, Neurotoxins, Neurotransmitter Agents, Noxae, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Peripheral Nervous System Agents, Proteins, Toxic Actions, Toxins, Biological | CA2310845 | 15-May-2001 | 7-Jun-2014 | NA | Growth hormone receptor | Dysport | Ipsen Pharmaceuticals | Ipsen Pharmaceuticals | Dysport is indicated for the treatment of Cervical Dystonia and Glabellar Lines | NA | Each vial contains 500 or 300 Units of lyophilized abobotulinumtoxinA, 125 micrograms human serum albumin and 2.5 mg lactose. Dysport may contain trace amounts of cow's milk proteins | Dysport is supplied in a single-use, sterile vial for reconstitution | IntramuSubcutaneousular Injection | In Cervical Dystonia: Initial dose of DYSPORT  is 500 Units given intramuscularly. Re-treatment every 12 to 16 weeks or longer, as necessary, based on return of clinical symptoms with doses administered between 250 and 1000 Units to optimize clinical benefit. In Glabellar Lines: A total dose of 50 Units of DYSPORT , divided in five equal aliquots of 10 Units each, should be administered to affected muscles to achieve clinical effect. | DYSPORT is contraindicated in patients with known hypersensitivity to any botulinum toxin preparation or to any of the components in the formulation. | In Cervical Dystonia: Most commonly observed adverse reactions (> 5% of patients) are: muscular weakness, dysphagia, dry mouth, injection site discomfort, fatigue, headache, neck pain, musculoskeletal pain, dysphonia, injection site pain, and eye disorders. In Glabellar Lines: The most frequently reported adverse events (≥2%) are nasopharyngitis, headache, injection site pain, injection site reaction, upper respiratory tract infection, eyelid edema, eyelid ptosis, sinusitis and nausea. | Link | NA | NA |
| 10421 | Th1070 | Botulinum Toxin Type A | >Th1070_Botulinum_Toxin_Type_A MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL | 900000 | C6760H10447N1743O2010S32 | 5.6 | -0.368 | 85.5-86.7 | 230 to 260 min in a pharmacokinetic study of rats and mice | Purified botulinum toxin from Clostridium botulinum, purified from culture via dialysis and acid precipitation. | For the treatment of cervical dystonia in adults to decrease the severity of abnormal head position and neck pain associated with cervical dystonia. Also for the treatment of severe primary axillary hyperhidrosis that is inadequately managed with topical agents and for the treatment of strabismus and blepharospasm associated with dystonia, including benign essential blepharospasm or VII nerve disorders in patients 12 years of age and above. Also used cosmetically to temporarily improve the appearance of moderate-to-severe frown lines between the eyebrows (glabellar lines) as well as for the treatment of excessive underarm sweating. | A 150 kDa neurotoxic protein produced from fermentation of Hall strain Clostridium botulinum type A grown in a medium containing casein hydrolysate, glucose and yeast extract. It is purified from the culture solution by dialysis and a series of acid precipitations to a complex consisting of the neurotoxin, and several accessory proteins. Botulinum Toxin Type A is not expected to be present in the peripheral blood at measurable levels following IM or intradermal injection at the recommended doses. The recommended quantities of neurotoxin administered at each treatment session are not expected to result in systemic, overt distant clinical effects, i.e. muscle weakness, in patients without other neuromuscular dysfunction. However, sub-clinical systemic effects have been shown by single-fiber electromyography after IM doses of botulinum toxins appropriate to produce clinically observable local muscle weakness. | Botulinum Toxin Type A blocks neuromuscular transmission by binding to acceptor sites on motor or sympathetic nerve terminals, entering the nerve terminals, and inhibiting the release of acetylcholine. This inhibition occurs as the neurotoxin cleaves SNAP-25, a protein integral to the successful docking and release of acetylcholine from vesicles situated within nerve endings. | Based on toxicological studies, it has been estimated that the human LD50 by injection is approximately 2800 Units, equivalent to 28 individual vials of BOTOX (Botulinum Toxin Type A) Purified Neurotoxin Complex (100 Units) for a 70 kg adult. When injected intramuscularly, Botulinum Toxin Type A has been shown to be teratogenic or to have embryocidal effects in some animal species. | NA | The chemical complexity of Botulinum Toxin Type A combined with its extreme potency limits the opportunity to study its pharmacokinetic profile in humans. Therefore, no human pharmacokinetic studies have been performed. Botulinum Toxin Type A is injected directly into the target organ, a skeletal muscle. Thus, bioavailability of the intravenous or oral route is not of clinical relevance. | NA | NA | Acetylcholine Release Inhibitors, Agents that produce neuromuscular block (indirect), Amino Acids, Peptides, and Proteins, Bacterial Proteins, Bacterial Toxins, Biological Factors, Botulinum Toxins, Botulinum Toxins, Type A, Central Nervous System Depressants, Cholinergic Agents, Endopeptidases, Enzymes, Enzymes and Coenzymes, Ganglion Blockers, Hydrolases, Membrane Transport Modulators, Metalloendopeptidases, Metalloproteases, Muscle Relaxants, Muscle Relaxants, Peripherally Acting Agents, Musculo-Skeletal System, Neuromuscular Agents, Neuromuscular Blocking Agents, Neurotoxins, Neurotransmitter Agents, Noxae, Other Miscellaneous Therapeutic Agents, Peptide Hydrolases, Peripheral Nervous System Agents, Proteins, Toxic Actions, Toxins, Biological | NA | NA | NA | NA | NA | Xeomin | MERZ AESTHETICS | MERZ AESTHETICS | Xeomin is indicated in Cervical Dystonia, Blepharospasm, Glabellar Lines | NA | One vial of XEOMIN contains 50 or 100 Units of incobotulinumtoxinA, 1 mg of human albumin, and 4.7 mg sucrose. | XEOMIN is a sterile white to off-white lyophilized powder after reconstitution with preservative-free 0.9% Saline for Injection. | IntramuSubcutaneousular Injection | In Cervical Dystonia: Initial dose of Xeomin is 120 Units given intramuscularly. In Blepharospasm: The total initial dose of XEOMIN in both eyes should not exceed 70 Units (35 Units/eye).In Glabellar Lines: The total recommended XEOMIN dose is 20 Units per treatment session divided into five equal intramuscular injections of 4 Units each. | Known hypersensitivity to the active substance botulinum neurotoxin type A or to any of the excipients and Infection at the proposed injection sites | In Cervical Dystonia: The most commonly observed adverse reactions (≥5% of patients and > placebo) are dysphagia, neck pain, muscle weakness, injection site pain, and musculoskeletal pain. In Blepharospasm: The most commonly observed adverse reactions (≥5% of patients and > placebo) are eyelid ptosis, dry eye, dry mouth, diarrhea, headache, visual impairment, dyspnea, nasopharyngitis, and respiratory tract infection. In Glabellar Lines:The most commonly observed adverse reaction (>1% of patients and > placebo) is headache. | Link | NA | NA |
| 10422 | Th1071 | Pancrelipase | >Th1071_Pancrelipase QYSPNTQQGRTSIVHLFEWRWVDI | 131000 | C5850H8902N1606O1739S49 | 6.44 | NA | 48-50 | Pancrelipase is not significantly absorbed from the gastrointestinal tract and acts locally, so limination half-life is not relevant | Pancrelipase is an enzyme mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. It contains 3 enzymes: amylase, lipase, and a protease (chymotrypsin). Pancrelipase is marketed under several brand names such as Ultresa and Viokace. | For treatment of exocrine pancreatic insufficiency in cystic fibrosis (Ultresa), chronic pancreatitis (Viokace in combination with a proton pump inhibitor), and pancreatectomy (Viokace in combination with a proton pump inhibitor) | Used in the treatment of cystic fibrosis or pancreatic dysfunction, pancrelipase helps improve fat digestion in the small intestine. Specifically, the lipase, protease and amylase components break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. Pancreatic enzymes are used to correct maldigestion, malabsorption and pain associated with pancreatic insufficiency. The major maldigestion/malabsorption problems arise from incomplete fat digestion. Exogenous pancrelipase reduces the amount of nitrogen and fat excreted in the stool. | The lipase, protease and amylase components of pancrelipase break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. | Overdose symptoms may include diarrhea or stomach upset. The most common adverse reactions seen are ear, neck, and abdominal pain; headache, nasal congestion, and beta-hemolytic streptococcal infection. | Pancrelipase acts locally, so there is minimal metabolism. | Pancrelipase is not significantly absorbed from the gastrointestinal tract. | NA | Pancrelipase is not significantly absorbed, so there is minimal clearance from the body. | Alimentary Tract and Metabolism, Carboxylic Ester Hydrolases, Complex Mixtures, Digestives, Incl. Enzymes, Enzyme Preparations, Enzymes, Enzymes and Coenzymes, Esterases, Gastrointestinal Agents, Hydrolases, Lipase, Pancreatic Extracts, Tissue Extracts | NA | NA | NA | If pancrelipase and iron salts are used in combination then monitor therapy. Pancrelipase may decrease the absorption of iron salts except for ferumoxytol, iron dextran complex, and iron sucrose | NA | Pancrecarb | Digestive care US, Inc. | Digestive care US, Inc. | PANCRECARB (pancrelipase) Delayed-Release Capsules, Buffered andEnteric-Coated Microspheres are indicated for patients with exocrinepancreatic enzyme insufficiency such as: cystic fibrosis, chronic pancreatitisdue to alcohol use or other causes, post-pancreatectomy and post-gastrointestinal bypass surgery | NA | it is formulated as Delayed-Release Capsules, Buffered and Enteric-Coated Microspheres.It contains Lipase :4000 to 8000 U.S.P. units, Amylase: 25000 to 40000 U.S.P. units, Protease: 25000 to 45000 U.S.P. units.nactive ingredients include sodium carbonate, sodium bicarbonate, cellulose acetate phthalate, diethyl phthalate, gelatin, sodium carboxymethyl starch, polyvinylpyrrolidone, talc, ursodiol, and other trace ingredients. | Delayed-Release Capsules, Buffered and Enteric-Coated Microspheres. | Oral route | Dosage should be individualized and adjusted according to fat intake, severity of steatorrhea and the severity of the exocrine pancreatic insufficiency. Begin therapy with one or two capsules with meals or snacks and adjust dosage according to symptoms. | PANCRECARB (pancrelipase) Delayed-Release Capsules, Buffered andEnteric-Coated Microspheres are contraindicated in patients known to be hypersensitive to pork protein or any other ingredient of this product. | The most frequently reported adverse reactions to pancrelipase-containing products are gastrointestinal in nature, which may include nausea, vomiting, bloating, cramping, constipation or diarrhea. Less frequently, allergic-type reactions have also been observed. Extremely high doses of exogenouspancreatic enzymes have been reported to be associated with hyperuricosuria and hyperuricemia. High strength pancrelipase preparation (i.e., those labeled as containing more than 20,000 lipase units per capsule) has been associated with colonic strictures. | Link | NA | NA |
| 10423 | Th1071 | Pancrelipase | >Th1071_Pancrelipase QYSPNTQQGRTSIVHLFEWRWVDI | 131000 | C5850H8902N1606O1739S49 | 7.44 | NA | 48-50 | Pancrelipase is not significantly absorbed from the gastrointestinal tract and acts locally, so limination half-life is not relevant | Pancrelipase is an enzyme mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. It contains 3 enzymes: amylase, lipase, and a protease (chymotrypsin). Pancrelipase is marketed under several brand names such as Ultresa and Viokace. | For treatment of exocrine pancreatic insufficiency in cystic fibrosis (Ultresa), chronic pancreatitis (Viokace in combination with a proton pump inhibitor), and pancreatectomy (Viokace in combination with a proton pump inhibitor) | Used in the treatment of cystic fibrosis or pancreatic dysfunction, pancrelipase helps improve fat digestion in the small intestine. Specifically, the lipase, protease and amylase components break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. Pancreatic enzymes are used to correct maldigestion, malabsorption and pain associated with pancreatic insufficiency. The major maldigestion/malabsorption problems arise from incomplete fat digestion. Exogenous pancrelipase reduces the amount of nitrogen and fat excreted in the stool. | The lipase, protease and amylase components of pancrelipase break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. | Overdose symptoms may include diarrhea or stomach upset. The most common adverse reactions seen are ear, neck, and abdominal pain; headache, nasal congestion, and beta-hemolytic streptococcal infection. | Pancrelipase acts locally, so there is minimal metabolism. | Pancrelipase is not significantly absorbed from the gastrointestinal tract. | NA | Pancrelipase is not significantly absorbed, so there is minimal clearance from the body. | Alimentary Tract and Metabolism, Carboxylic Ester Hydrolases, Complex Mixtures, Digestives, Incl. Enzymes, Enzyme Preparations, Enzymes, Enzymes and Coenzymes, Esterases, Gastrointestinal Agents, Hydrolases, Lipase, Pancreatic Extracts, Tissue Extracts | NA | NA | NA | NA | NA | Viokace | Aptalis Pharma US, Inc. | Aptalis Pharma US, Inc. | VIOKACE (pancrelipase) tablets, in combination with a proton pump inhibitor, is indicated in adults for the treatment of exocrine paencratic insufficiencydue to chronic pancreatitis or pancreatectomy. | NA | 10,440 USP units of lipase; 39,150 USP units of protease; 39,150 USP units of amylase tablets are tan, round biconvex and have VIO9111 engraved on one side and 9111 on the other side.Inactive ingredients in VIOKACE include: colloidal silicon dioxide, crosscarmellose sodium, lactose monohydrate, microcrystalline cellulose, stearic acid and talc. | Pancrelipase is a beige-white amorphous powder. It is miscible in water and practically insoluble in alcohol and converted to tablet form | Oral route | Enzyme dosing should begin with 500 lipase units/kg of body weight per meal to a maximum of 2,500 lipase units/kg of body weight per meal (or less than or equal to 10,000 lipase units/kg of body weight per day), or less than 4,000 lipase units/g fat ingested per day. | None | The most serious adverse reactions reported with different pancreatic enzyme products of the same active ingredient (pancrelipase) that are described elsewhere in the label include fibrosing colonopathy, hyperuricemia and allergic reactions. | Link | NA | NA |
| 10424 | Th1071 | Pancrelipase | >Th1071_Pancrelipase QYSPNTQQGRTSIVHLFEWRWVDI | 131000 | C5850H8902N1606O1739S49 | 8.44 | NA | 48-50 | Pancrelipase is not significantly absorbed from the gastrointestinal tract and acts locally, so limination half-life is not relevant | Pancrelipase is an enzyme mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. It contains 3 enzymes: amylase, lipase, and a protease (chymotrypsin). Pancrelipase is marketed under several brand names such as Ultresa and Viokace. | For treatment of exocrine pancreatic insufficiency in cystic fibrosis (Ultresa), chronic pancreatitis (Viokace in combination with a proton pump inhibitor), and pancreatectomy (Viokace in combination with a proton pump inhibitor) | Used in the treatment of cystic fibrosis or pancreatic dysfunction, pancrelipase helps improve fat digestion in the small intestine. Specifically, the lipase, protease and amylase components break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. Pancreatic enzymes are used to correct maldigestion, malabsorption and pain associated with pancreatic insufficiency. The major maldigestion/malabsorption problems arise from incomplete fat digestion. Exogenous pancrelipase reduces the amount of nitrogen and fat excreted in the stool. | The lipase, protease and amylase components of pancrelipase break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. | Overdose symptoms may include diarrhea or stomach upset. The most common adverse reactions seen are ear, neck, and abdominal pain; headache, nasal congestion, and beta-hemolytic streptococcal infection. | Pancrelipase acts locally, so there is minimal metabolism. | Pancrelipase is not significantly absorbed from the gastrointestinal tract. | NA | Pancrelipase is not significantly absorbed, so there is minimal clearance from the body. | Alimentary Tract and Metabolism, Carboxylic Ester Hydrolases, Complex Mixtures, Digestives, Incl. Enzymes, Enzyme Preparations, Enzymes, Enzymes and Coenzymes, Esterases, Gastrointestinal Agents, Hydrolases, Lipase, Pancreatic Extracts, Tissue Extracts | NA | NA | NA | NA | Synaptosomal-associated protein 25,Rho-related GTP-binding protein RhoB | ULTRESA | Aptalis Pharma US, Inc. | Aptalis Pharma US, Inc. | ULTRESA (pancrelipase) is indicated for the treatment of exocrinepancreatic insufficiency due to cystic fibrosis or other conditions. | NA | Each delayed-release capsule for oral administration contains enteric-coatedbeads (1.7 mm in diameter and 1.9 mm thick for 4,000 USP lipase units, approximately 2.0 mm in diameter and 2.0 – 2.4 mm thick for 13,800, 20,700, and 23,000 USP lipase units). it also contains colloidal silicon dioxide, croscarmellose sodium, hydrogenated castor oil, hypromellose phthalate, magnesium stearate, microcrystalline cellulose, talc, and triethyl citrate. | Pancrelipase is a beige-white amorphous powder. It is miscible in water and practically insoluble or insoluble in alcohol and ether and converted to Delayed-Release Capsules | Oral route | Enzyme dosing should begin with 500 lipase units/kg of body weight per meal for those older than age 4 years to a maximum of 2,500 lipase units/kg of body weight per meal (or less than or equal to 10,000 lipase units/kg of body weight per day), or less than 4,000 lipase units/g fat ingested per day. | None | The most serious adverse reactions reported with different pancreatic enzyme products of the same active ingredient (pancrelipase) that are described elsewhere in the label include fibrosing colonopathy,hyperuricemia and allergic reactions. | Link | NA | NA |
| 10425 | Th1071 | Pancrelipase | >Th1071_Pancrelipase QYSPNTQQGRTSIVHLFEWRWVDI | 131000 | C5850H8902N1606O1739S49 | 9.44 | NA | 48-50 | Pancrelipase is not significantly absorbed from the gastrointestinal tract and acts locally, so limination half-life is not relevant | Pancrelipase is an enzyme mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. It contains 3 enzymes: amylase, lipase, and a protease (chymotrypsin). Pancrelipase is marketed under several brand names such as Ultresa and Viokace. | For treatment of exocrine pancreatic insufficiency in cystic fibrosis (Ultresa), chronic pancreatitis (Viokace in combination with a proton pump inhibitor), and pancreatectomy (Viokace in combination with a proton pump inhibitor) | Used in the treatment of cystic fibrosis or pancreatic dysfunction, pancrelipase helps improve fat digestion in the small intestine. Specifically, the lipase, protease and amylase components break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. Pancreatic enzymes are used to correct maldigestion, malabsorption and pain associated with pancreatic insufficiency. The major maldigestion/malabsorption problems arise from incomplete fat digestion. Exogenous pancrelipase reduces the amount of nitrogen and fat excreted in the stool. | The lipase, protease and amylase components of pancrelipase break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. | Overdose symptoms may include diarrhea or stomach upset. The most common adverse reactions seen are ear, neck, and abdominal pain; headache, nasal congestion, and beta-hemolytic streptococcal infection. | Pancrelipase acts locally, so there is minimal metabolism. | Pancrelipase is not significantly absorbed from the gastrointestinal tract. | NA | Pancrelipase is not significantly absorbed, so there is minimal clearance from the body. | Alimentary Tract and Metabolism, Carboxylic Ester Hydrolases, Complex Mixtures, Digestives, Incl. Enzymes, Enzyme Preparations, Enzymes, Enzymes and Coenzymes, Esterases, Gastrointestinal Agents, Hydrolases, Lipase, Pancreatic Extracts, Tissue Extracts | NA | NA | NA | NA | NA | PERTZYE | Digestive care US, Inc. | Digestive care US, Inc. | PERTZYE (pancrelipase) is indicated for the treatment of exocrinepancreatic insufficiency due to cystic fibrosis or other conditions. | NA | Each PERTZYE delayed-release capsule for oral administration contains bicarbonatebuffered enteric-coated microspheres ranging in size from 0.8 – 2.2 mm in diameter.8,000 USP units of lipase; 28,750 USP units of protease; 30,250 USP units of amylase. it also contains odium bicarbonate, sodium carbonate, cellulose acetate phthalate, sodium starch glycolate, diethyl phthalate, ursodiol, polyvinylpyrrolidone, and talc and are contained in hard gelatin capsules. | Pancrelipase is a beige-white amorphous powder. It is miscible in water and practically insoluble or insoluble in alcohol and ether PERTZYE delayed-release capsule | Oral route | Enzyme dosing should begin with 500 lipase units/kg of body weight per meal for those older than age 4 years to a maximum of 2,500 lipase units/kg of body weight per meal (or less than or equal to 10,000 lipase units/kg of body weight per day), or less than 4,000 lipase units/g fat ingested per day. | None | The most serious adverse reactions reported with different pancreatic enzyme products of the same active ingredient (pancrelipase) that are described elsewhere in the label include fibrosing colonopathy,hyperuricemia and allergic reactions | Link | NA | NA |
| 10426 | Th1071 | Pancrelipase | >Th1071_Pancrelipase QYSPNTQQGRTSIVHLFEWRWVDI | 131000 | C5850H8902N1606O1739S49 | 10.44 | NA | 48-50 | Pancrelipase is not significantly absorbed from the gastrointestinal tract and acts locally, so limination half-life is not relevant | Pancrelipase is an enzyme mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. It contains 3 enzymes: amylase, lipase, and a protease (chymotrypsin). Pancrelipase is marketed under several brand names such as Ultresa and Viokace. | For treatment of exocrine pancreatic insufficiency in cystic fibrosis (Ultresa), chronic pancreatitis (Viokace in combination with a proton pump inhibitor), and pancreatectomy (Viokace in combination with a proton pump inhibitor) | Used in the treatment of cystic fibrosis or pancreatic dysfunction, pancrelipase helps improve fat digestion in the small intestine. Specifically, the lipase, protease and amylase components break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. Pancreatic enzymes are used to correct maldigestion, malabsorption and pain associated with pancreatic insufficiency. The major maldigestion/malabsorption problems arise from incomplete fat digestion. Exogenous pancrelipase reduces the amount of nitrogen and fat excreted in the stool. | The lipase, protease and amylase components of pancrelipase break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. | Overdose symptoms may include diarrhea or stomach upset. The most common adverse reactions seen are ear, neck, and abdominal pain; headache, nasal congestion, and beta-hemolytic streptococcal infection. | Pancrelipase acts locally, so there is minimal metabolism. | Pancrelipase is not significantly absorbed from the gastrointestinal tract. | NA | Pancrelipase is not significantly absorbed, so there is minimal clearance from the body. | Alimentary Tract and Metabolism, Carboxylic Ester Hydrolases, Complex Mixtures, Digestives, Incl. Enzymes, Enzyme Preparations, Enzymes, Enzymes and Coenzymes, Esterases, Gastrointestinal Agents, Hydrolases, Lipase, Pancreatic Extracts, Tissue Extracts | NA | NA | NA | NA | NA | ULTRASE | Axcan Pharma | Axcan Pharma | ULTRASE (pancrelipase) Capsules are indicated for patients with partial or complete exocrine pancreatic insufficiency caused by cystic fibrosis, Chronic pancreatitis due to alcohol, Obstruction, Other pancreatic disease, Poor mixing | NA | Each ULTRASE (pancrelipase) Capsule contains 4500 USP units of lipase; 25000 USP units of protease; 20000 USP units of amylase. It contains povidone, talc, sugar, methacrylic acid copolymer (Type C), triethyl citrate, simethicone emulsion. | Capsules Enteric-Coated Microspheres | Oral route | Initial dosing of pancreatic enzyme supplements should begin with 500 lipase U/kg/meal using enteric-coated microsphere products. | Pancrelipase capsules are contraindicated in patients known to be hypersensitive to pork protein. Pancrelipase capsules are contraindicated in patients with acute pancreatitis or with acute exacerbations of chronicpancreatic diseases. |  Extremely high doses of exogenouspancreatic enzymes have been associated with hyperuricosuria andhyperuricemia, | Link | NA | NA |
| 10427 | Th1071 | Pancrelipase | >Th1071_Pancrelipase QYSPNTQQGRTSIVHLFEWRWVDI | 131000 | C5850H8902N1606O1739S49 | 11.44 | NA | 48-50 | Pancrelipase is not significantly absorbed from the gastrointestinal tract and acts locally, so limination half-life is not relevant | Pancrelipase is an enzyme mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. It contains 3 enzymes: amylase, lipase, and a protease (chymotrypsin). Pancrelipase is marketed under several brand names such as Ultresa and Viokace. | For treatment of exocrine pancreatic insufficiency in cystic fibrosis (Ultresa), chronic pancreatitis (Viokace in combination with a proton pump inhibitor), and pancreatectomy (Viokace in combination with a proton pump inhibitor) | Used in the treatment of cystic fibrosis or pancreatic dysfunction, pancrelipase helps improve fat digestion in the small intestine. Specifically, the lipase, protease and amylase components break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. Pancreatic enzymes are used to correct maldigestion, malabsorption and pain associated with pancreatic insufficiency. The major maldigestion/malabsorption problems arise from incomplete fat digestion. Exogenous pancrelipase reduces the amount of nitrogen and fat excreted in the stool. | The lipase, protease and amylase components of pancrelipase break down fat, protein, and starches, respectively, in the small intestine. Lipase hydrolyzes fats into glycerol and fatty acids. Protease converts proteins into proteoses and derived substances, while amylase converts starches into dextrins and sugars. | Overdose symptoms may include diarrhea or stomach upset. The most common adverse reactions seen are ear, neck, and abdominal pain; headache, nasal congestion, and beta-hemolytic streptococcal infection. | Pancrelipase acts locally, so there is minimal metabolism. | Pancrelipase is not significantly absorbed from the gastrointestinal tract. | NA | Pancrelipase is not significantly absorbed, so there is minimal clearance from the body. | Alimentary Tract and Metabolism, Carboxylic Ester Hydrolases, Complex Mixtures, Digestives, Incl. Enzymes, Enzyme Preparations, Enzymes, Enzymes and Coenzymes, Esterases, Gastrointestinal Agents, Hydrolases, Lipase, Pancreatic Extracts, Tissue Extracts | NA | NA | NA | NA | Dietary fat,Dietary protein,Dietary starch | ZENPEP | Aptalis Pharma US, Inc. | Aptalis Pharma US, Inc. | ZENPEP (pancrelipase) is indicated for the treatment of exocrinepancreatic insufficiency due to cystic fibrosis or other conditions. | NA | Each capsule for oral administration contains enteric-coated beads (1.8-1.9mm for 3,000 and 5,000 USP units of lipase, 2.2-2.5mm for 10,000, 15,000, 20,000, 25,000, and 40,000 USP units of lipase). ZENPEP include colloidal silicon dioxide, croscarmellose sodium, hydrogenated castor oil, hypromellose phthalate, magnesium stearate, microcrystalline cellulose, talc, and triethyl citrate and are contained in hypromellose capsules. The imprinting red ink on the 3,000 capsules strength contains, antifoam DC 1510, industrial methylated spirit, iron oxide red C.I. 77491-E172, n-butyl alcohol, shellac and soya lecithin. | Delayed-Release Capsules | Oral route | Enzyme dosing should begin with 500 lipase units/kg of body weight per meal for those older than age 4 years to a maximum of 2,500 lipase units/kg of body weight per meal (or less than or equal to 10,000 lipase units/kg of body weight per day), or less than 4,000 lipase units/g fat ingested per day. | None | The most serious adverse reactions reported with different pancreatic enzyme products of the same active ingredient (pancrelipase) that are described elsewhere in the label include fibrosing colonopathy,hyperuricemia and allergic reactions | Link | NA | NA |
| 10428 | Th1072 | Streptokinase | >Th1072_Streptokinase MKNYLSFGMFALLFALTFGTVNSVQAIAGPEWLLDRPSVNNSQLVVSVAGTVEGTNQDISLKFFEIDLTSRPAHGGKTEQGLSPKSKPFATDSGAMSHKLEKADLLKAIQEQLIANVHSNDDYFEVIDFASDATITDRNGKVYFADKDGSVTLPTQPVQEFLLSGHVRVRPYKEKPIQNQAKSVDVEYTVQFTPLNPDDDFRPGLKDTKLLKTLAIGDTITSQELLAQAQSILNKNHPGYTIYERDSSIVTHDNDIFRTILPMDQEFTYRVKNREQAYRINKKSGLNEEINNTDLISEKYYVLKKGEKPYDPFDRSHLKLFTIKYVDVDTNELLKSEQLLTASERNLDFRDLYDPRDKAKLLYNNLDAFGIMDYTLTGKVEDNHDDTNRIITVYMGKRPEGENASYHLAYDKDRYTEEEREVYSYLRYTGTPIPDNPNDK | 47286.7 | C2100H3278N566O669S4 | 5.12 | -0.728 | NA | NA | Streptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci. | For the treatment of acute evolving transmural myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis or emolism and occlusion of arteriovenous cannulae | Streptokinase creates an active complex which promotes the cleavage of the Arg/Val bond in plasminogen to form the proteolytic enzyme plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Plasminogen is an inactive molecule that becomes activated to plasmin when the Arg/Val bond is cleaved. Plasmin breaks down fibrin clots created by the blood clotting cascade. Streptokinase forms a highly specific 1:1 enzymatic complex with plasminogen which converts inactive plasminogen molecules into active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema,Amino Acids, Peptides, and Proteins,Anticoagulants,Biological Factors,Blood and Blood Forming Organs,Blood Proteins,Cardiovascular Agents,Endopeptidases,Enzymes,Enzymes and Coenzymes,Fibrin Modulating Agents,Fibrinolytic Agents,Hematologic Agents,Hydrolases,Hypotensive Agents,Peptide Hydrolases,Plasminogen Activators,Proteins,Serine Endopeptidases,Serine Proteases,Streptokinase, antagonists & inhibitors | NA | NA | NA | Ticlopidine Increases bleeding risk. Monitor for signs of bleeding | Plasminogen,Proteinase-activated receptor 1 | Streptase | CSL Behring | CSL Behring | Indicated in Acute Evolving Transmural Myocardial Infarction, Pulmonary Embolism, Deep Vein Thrombosis, Arterial Thrombosis or Embolism, Occlusion of Arteriovenous Cannulae | NA | 25 mg cross-linked gelatin polypeptides, 25 mg sodium L-glutamate, sodium hydroxide to adjust pH, and 100 mg Albumin (Human) per vial or infusion bottle as stabilizers. The preparation contains no preservatives | It is Sterile, purified preparation formulated as lypholized powder | Intravenous and intracoronary administration. | In Acute Evolving Transmural Myocardial Infarction,dose for IV-In 1,500,000 IU and IC-In 140,000 IU. For Pulmonary Embolism, Deep Vein Thrombosis, Arterial Thrombosis or Embolism, IV-In: 250,000 IU/30 min | No Information Provided. | Severe internal bleeding involving gastrointestinal  (including hepaticbleeding), genitourinary, retroperitoneal, or intracerebral sites has occurred and has resulted in fatalities. Minor breathing difficulty to bronchospasm, periorbital swelling or angioneurotic edema have been observed rarely. Other milder allergic effects such as urticaria, itching, flushing, nausea, headache and musculoskeletal pain have also been observed, as have delayed hypersensitivity reactions such as vasculitis and interstitial nephritis, Respiratory depression, etc. | Link | NA | NA |
| 10429 | Th1072 | Streptokinase | >Th1072_Streptokinase MKNYLSFGMFALLFALTFGTVNSVQAIAGPEWLLDRPSVNNSQLVVSVAGTVEGTNQDISLKFFEIDLTSRPAHGGKTEQGLSPKSKPFATDSGAMSHKLEKADLLKAIQEQLIANVHSNDDYFEVIDFASDATITDRNGKVYFADKDGSVTLPTQPVQEFLLSGHVRVRPYKEKPIQNQAKSVDVEYTVQFTPLNPDDDFRPGLKDTKLLKTLAIGDTITSQELLAQAQSILNKNHPGYTIYERDSSIVTHDNDIFRTILPMDQEFTYRVKNREQAYRINKKSGLNEEINNTDLISEKYYVLKKGEKPYDPFDRSHLKLFTIKYVDVDTNELLKSEQLLTASERNLDFRDLYDPRDKAKLLYNNLDAFGIMDYTLTGKVEDNHDDTNRIITVYMGKRPEGENASYHLAYDKDRYTEEEREVYSYLRYTGTPIPDNPNDK | 47286.7 | C2100H3278N566O669S4 | 5.12 | -0.728 | NA | NA | Streptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci. | For the treatment of acute evolving transmural myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis or emolism and occlusion of arteriovenous cannulae | Streptokinase creates an active complex which promotes the cleavage of the Arg/Val bond in plasminogen to form the proteolytic enzyme plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Plasminogen is an inactive molecule that becomes activated to plasmin when the Arg/Val bond is cleaved. Plasmin breaks down fibrin clots created by the blood clotting cascade. Streptokinase forms a highly specific 1:1 enzymatic complex with plasminogen which converts inactive plasminogen molecules into active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema,Amino Acids, Peptides, and Proteins,Anticoagulants,Biological Factors,Blood and Blood Forming Organs,Blood Proteins,Cardiovascular Agents,Endopeptidases,Enzymes,Enzymes and Coenzymes,Fibrin Modulating Agents,Fibrinolytic Agents,Hematologic Agents,Hydrolases,Hypotensive Agents,Peptide Hydrolases,Plasminogen Activators,Proteins,Serine Endopeptidases,Serine Proteases,Streptokinase, antagonists & inhibitors | NA | NA | NA | NA | Plasminogen,Proteinase-activated receptor 1 | Kabikinase | Pharmacia & Upjohn Inc | Pharmacia & Upjohn Inc | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10430 | Th1072 | Streptokinase | >Th1072_Streptokinase MKNYLSFGMFALLFALTFGTVNSVQAIAGPEWLLDRPSVNNSQLVVSVAGTVEGTNQDISLKFFEIDLTSRPAHGGKTEQGLSPKSKPFATDSGAMSHKLEKADLLKAIQEQLIANVHSNDDYFEVIDFASDATITDRNGKVYFADKDGSVTLPTQPVQEFLLSGHVRVRPYKEKPIQNQAKSVDVEYTVQFTPLNPDDDFRPGLKDTKLLKTLAIGDTITSQELLAQAQSILNKNHPGYTIYERDSSIVTHDNDIFRTILPMDQEFTYRVKNREQAYRINKKSGLNEEINNTDLISEKYYVLKKGEKPYDPFDRSHLKLFTIKYVDVDTNELLKSEQLLTASERNLDFRDLYDPRDKAKLLYNNLDAFGIMDYTLTGKVEDNHDDTNRIITVYMGKRPEGENASYHLAYDKDRYTEEEREVYSYLRYTGTPIPDNPNDK | 47286.7 | C2100H3278N566O669S4 | 5.12 | -0.728 | NA | NA | Streptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci. | For the treatment of acute evolving transmural myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis or emolism and occlusion of arteriovenous cannulae | Streptokinase creates an active complex which promotes the cleavage of the Arg/Val bond in plasminogen to form the proteolytic enzyme plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction. | Plasminogen is an inactive molecule that becomes activated to plasmin when the Arg/Val bond is cleaved. Plasmin breaks down fibrin clots created by the blood clotting cascade. Streptokinase forms a highly specific 1:1 enzymatic complex with plasminogen which converts inactive plasminogen molecules into active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. This in turn leads to the degradation of blood clots. | NA | NA | NA | NA | NA | Agents causing angioedema,Amino Acids, Peptides, and Proteins,Anticoagulants,Biological Factors,Blood and Blood Forming Organs,Blood Proteins,Cardiovascular Agents,Endopeptidases,Enzymes,Enzymes and Coenzymes,Fibrin Modulating Agents,Fibrinolytic Agents,Hematologic Agents,Hydrolases,Hypotensive Agents,Peptide Hydrolases,Plasminogen Activators,Proteins,Serine Endopeptidases,Serine Proteases,Streptokinase, antagonists & inhibitors | NA | NA | NA | NA | Plasminogen,Proteinase-activated receptor 1 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10434 | Th1074 | Alglucerase | >Th1074_Alglucerase ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ | 55597.4 | C2532H3854N672O711S16 | 7.41 | -0.168 | NA | 3.6-10.4 min | Human Beta-glucocerebrosidase or Beta-D-glucosyl-N-acylsphingosine glucohydrolase E.C. 3.2.1.45. 497 residue protein with N-linked carbohydrates. Alglucerase is prepared by modification of the oligosaccharide chains of human Beta-glucocerebrosidase. The modification alters the sugar residues at the non-reducing ends of the oligosaccharide chains of the glycoprotein so that they are predominantly terminated with mannose residues | For the treatment of Gaucher's disease (deficiency in glucocerebrosidase) | Gaucher disease is characterized by a functional deficiency in Beta-glucocerebrosidase enzymatic activity and the resultant accumulation of lipid glucocerebroside in tissue macrophages which become engorged and are termed Gaucher cells. Gaucher cells are typically found in liver, spleen and bone marrow. This can lead to an enlarged spleen and liver (hepatosplenomegaly). Secondary hematologic sequelae include severe anemia and thrombocytopenia. Injections of alglucerase into Gaucher disease patients leads to elevated serum levels of the enzyme and reduction in the accumulation of glucocerebroside | Alglucerase catalyzes the hydrolysis of the glycolipid, glucocerebroside, to glucose and ceramide as part of the normal degradation pathway for membrane lipids. | NA | NA | NA | 49.4 to 282.1 mL/kg | NA | Alimentary Tract and Metabolism,Enzyme Replacement Therapy,Enzymes,Enzymes and Coenzymes,Gaucher Disease,Glucosidases,Glycoside Hydrolases,Hydrolases,Hydrolytic Lysosomal Glucocerebroside-specific Enzyme,Recombinant Proteins | NA | NA | NA | NA | Glucocerebroside | Ceredase | Genzyme Corporation | Genzyme Corporation | Ceredase (alglucerase injection) is indicated for use as long-term enzyme replacement therapy for children, adolescents and adult patients with a confirmed diagnosis of Type I Gaucher disease who exhibit signs and symptoms that are severe enough to result in moderate-to-severe anemia, thrombocytopenia with bleeding tendency, bone disease, significant hepatomegaly or splenomegaly. | NA | Ceredase citrate is supplied as buffered solution (53 mM citrate, 143 mM sodium) containing 1% albumin human USP. The enzyme is supplied in one concentration, 400 units per bottle (80 units/mL) with a fill volume of 5 mL per bottle. An enzyme unit (U) is defined as the amount of enzyme required to hydrolyze in one minute one micromole of the synthetic substrate, p-nitrophenyl-β-D-glucopyranoside. | Ceredase (alglucerase injection) is supplied as a clear sterile non-pyrogenic solution of alglucerase in a citrate buffered solution | Intravenous infusion | Ceredase (alglucerase injection) is administered by Intravenous infusion over 1-2 hours. Dosage should be individualized for each patient. Initial dosage may be as little as 2.5 units/kg of body weight 3 times a week up to as much as 60 units/kg administered as frequently as once a week or as infrequently as every 4 weeks. 60 units/kg every 2 weeks is the dose for which the most data are available. Disease severity may dictate that drug be initiated with relatively high doses or relatively frequent administration. After patient response is well-established, a reduction in dosage may be attempted for maintenance therapy. Progressive reductions can be made at intervals of 3-6 months while carefully monitoring response parameters. | There are no known contraindications to the use of Ceredase (alglucerase injection). | Events were related to the route of administration including discomfort,pruritus, burning and swelling or sterile abscess at the site of venipuncture. The remaining experiences consisted of slight fever, chills, abdominaldiscomfort, nausea or vomiting. Additional adverse symptoms which have been reported include: fatigue, vasomotor irritability or hot flash, weakness, headache, light headedness, dysosmia, oral ulcerations, backache and transient peripheral edema, and diarrhea. Menstrual abnormalities and false positive pregnancy tests | Link | NA | NA |
| 10435 | Th1074 | Alglucerase | >Th1074_Alglucerase ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ | 55597.4 | C2532H3854N672O711S16 | 7.41 | -0.168 | NA | 3.6-10.4 min | Human Beta-glucocerebrosidase or Beta-D-glucosyl-N-acylsphingosine glucohydrolase E.C. 3.2.1.45. 497 residue protein with N-linked carbohydrates. Alglucerase is prepared by modification of the oligosaccharide chains of human Beta-glucocerebrosidase. The modification alters the sugar residues at the non-reducing ends of the oligosaccharide chains of the glycoprotein so that they are predominantly terminated with mannose residues | For the treatment of Gaucher's disease (deficiency in glucocerebrosidase) | Gaucher disease is characterized by a functional deficiency in Beta-glucocerebrosidase enzymatic activity and the resultant accumulation of lipid glucocerebroside in tissue macrophages which become engorged and are termed Gaucher cells. Gaucher cells are typically found in liver, spleen and bone marrow. This can lead to an enlarged spleen and liver (hepatosplenomegaly). Secondary hematologic sequelae include severe anemia and thrombocytopenia. Injections of alglucerase into Gaucher disease patients leads to elevated serum levels of the enzyme and reduction in the accumulation of glucocerebroside | Alglucerase catalyzes the hydrolysis of the glycolipid, glucocerebroside, to glucose and ceramide as part of the normal degradation pathway for membrane lipids. | NA | NA | NA | 49.4 to 282.1 mL/kg | NA | Alimentary Tract and Metabolism,Enzyme Replacement Therapy,Enzymes,Enzymes and Coenzymes,Gaucher Disease,Glucosidases,Glycoside Hydrolases,Hydrolases,Hydrolytic Lysosomal Glucocerebroside-specific Enzyme,Recombinant Proteins | NA | NA | NA | NA | Glucocerebroside | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10438 | Th1076 | Laronidase | >Th1076_Laronidase APHLVQVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP | 69899.4 | C3160H4848N898O881S12 | 9.09 | -0.3 | NA | 1.5-3.6 hrs | Human recombinant alpha-L-iduronidase, produced by recombinant DNAtechnology in a Chinese hamster ovary cell line. Laronidase is a glycoprotein with a predicted amino acid sequence of the recombinant form, as well as the nucleotide sequence that encodes it, are identical to a polymorphic form of human a-L-iduronidase. It contains 6 N-linked oligosaccharide modification sites. | For the treatment of mucopolysaccharidosis | Laronidase is used to treat mucopolysaccharide storage disorders (Hurlers syndrome) caused by deficiencies of alpha-L-iduronidase. Reduced or absent a-L-iduronidase activity results in the accumulation of the GAG substrates, dermatan sulfate and heparan sulfate, throughout the body and leads to widespread cellular, tissue, and organ dysfunction. | Laronidase catalyses the hydrolysis of terminal alpha-L-iduronic acid residues of dermatan sulfate and heparin sulfate. | NA | NA | NA | NA | NA | Alimentary Tract and Metabolism,Enzymes,Enzymes and Coenzymes,Hydrolytic Lysosomal Glycosaminoglycan-specific Enzyme | NA | NA | NA | NA | Iduronic acid | ALDURAZYME | Genzyme Corporation | Genzyme Corporation | ALDURAZYME is a hydrolytic lysosomal glycosaminoglycan (GAG)-specific enzyme indicated for patients with Hurler and Hurler-Scheie forms of Mucopolysaccharidosis I (MPS I) and for patients with the Scheie form who have moderate to severe symptoms. The risks and benefits of treating mildly affected patients with the Scheie form have not been established. ALDURAZYME has been shown to improve pulmonary function and walking capacity. ALDURAZYME has not been evaluated for effects on the central nervous system manifestations of the disorder | NA | The solution in each vial contains a nominal laronidase concentration of 0.58 mg/mL and a pH of approximately 5.5. The extractable volume of 5.0 mL from each vial provides 2.9 mg laronidase, 43.9 mg sodium chloride, 63.5 mg sodium phosphate monobasic monohydrate, 10.7 mg sodium phosphate dibasic heptahydrate, and 0.05 mg polysorbate 80. ALDURAZYME does not contain preservatives; vials are for single use only. | ALDURAZYME, for IV infusion, is supplied as a sterile, nonpyrogenic, colorless to pale yellow, clear to slightly opalescent solution that must be diluted prior to administration in 0.9% Sodium Chloride Injection | Intravenous (Intravenous) infusion | 0.58 mg/kg of body weight administered once weekly | None | The most commonly reported infusion reactions occurring in at least 10% of patients 6 months of age and older were pyrexia, chills, blood pressure increased, tachycardia, and oxygen saturation decreased (6). The most frequently occurring adverse reactions occurring in at least 10% of patients 6 years and older are rash, upper respiratory tract infection, injection site reaction, hyperreflexia, paresthesia, flushing, and poor venous access. | Link | NA | NA |
| 10439 | Th1076 | Laronidase | >Th1076_Laronidase APHLVQVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP | 69899.4 | C3160H4848N898O881S12 | 9.09 | -0.3 | NA | 1.5-3.6 hrs | Human recombinant alpha-L-iduronidase, produced by recombinant DNAtechnology in a Chinese hamster ovary cell line. Laronidase is a glycoprotein with a predicted amino acid sequence of the recombinant form, as well as the nucleotide sequence that encodes it, are identical to a polymorphic form of human a-L-iduronidase. It contains 6 N-linked oligosaccharide modification sites. | For the treatment of mucopolysaccharidosis | Laronidase is used to treat mucopolysaccharide storage disorders (Hurlers syndrome) caused by deficiencies of alpha-L-iduronidase. Reduced or absent a-L-iduronidase activity results in the accumulation of the GAG substrates, dermatan sulfate and heparan sulfate, throughout the body and leads to widespread cellular, tissue, and organ dysfunction. | Laronidase catalyses the hydrolysis of terminal alpha-L-iduronic acid residues of dermatan sulfate and heparin sulfate. | NA | NA | NA | NA | NA | Alimentary Tract and Metabolism,Enzymes,Enzymes and Coenzymes,Hydrolytic Lysosomal Glycosaminoglycan-specific Enzyme | NA | NA | NA | NA | Iduronic acid | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10471 | Th1085 | Agalsidase beta | >Th1085_Agalsidase_beta LDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL | 45351.6 | C2029H3080N544O587S27 | 5.17 | -0.307 | NA | 67 ± 12 min for a 1 mg/kg dose (mean infusion length = 115 minutes.) | Recombinant human alpha-galactosidase-A produced in CHO cells. The mature protein comprises 2 subunits of 398 residues. | For treatment of Fabry's disease (alpha-galactosidase A deficiency) | Used in the treatment of Fabry disease, an X-linked genetic disorder of glycosphingolipid metabolism. The disease is characterized by a deficiency of the lysosomal enzyme alpha-galactosidase A, which leads to progressive accumulation of glycosphingolipids, predominantly GL-3, in many body tissues. Clinical manifestations of Fabry disease include renal failure, cardiomyopathy, and cerebrovascular accidents. Fabrazyme is intended to provide an exogenous source of alpha-galactosidase A and to limit the accumulation of these glycolipids in the tissues. Studies show unconclusive evidence for the clinical efficacy of either agalasidase alfa or agalasidase beta in preventing morbidity. | Alpha-galactosidase A catalyzes the hydrolysis of globotriaosylceramide (GL-3) and other a-galactyl-terminated neutral glycosphingolipids, such as galabiosylceramide and blood group B substances to ceramide dihexoside and galactose. | Data regarding overdoses of agalsidase beta are not readily available.6 Patients experiencing an overdose of agalsidase beta may experience an increased incidence and severity of adverse effects.6 Overdose can be managed through the use of symptomatic and supportive measures. | Data regarding the metabolism of agalsidase beta is not readily available.6 However, protein drugs are expected to be degraded by proteases and other catalytic enzymes to smaller peptides and amino acids. | A 1 mg/kg dose of agalsidase beta with a mean infusion length of 115 minutes reaches a Cmax 5.0 ± 1.1 µg/mL with an AUC of 496 ± 137 µg*min/mL | A 1 mg/kg dose of agalsidase beta with a mean infusion length of 115 minutes has a VSS of 112 ± 13 mL/kg | A 1 mg/kg dose of agalsidase beta with a mean infusion length of 115 minutes has a clearance of 2.1 ± 0.7 mL/min/kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Enzymes,Enzymes and Coenzymes,Galactosidases,Glycoside Hydrolases,Hydrolases,Hydrolytic Lysosomal Neutral Glycosphingolipid-specific Enzyme,Protein Isoforms,Proteins | CA2265464 | 26-Jun-2007 | 12-Sep-2017 | NA | Globotriaosylceramide | Fabrazyme | Genzyme Corp | Genzyme Corp | Routine prophylaxis to prevent or reduce the frequency of bleeding episodes. | NA | Each 5 mg vial contains 5.5 mg of agalsidase beta as well as 33.0 mg mannitol, 3.0 mg sodium phosphate monobasic monohydrate, and 8.8 mg sodium phosphate dibasic heptahydrate. Following reconstitution as directed, 5 mg of agalsidase beta (1 mL) may be extracted from each 5 mg vial. | Sterile, nonpyrogenic, white to off-white, lyophilized cake or powder for reconstitution with Sterile Water for Injection, uSp. Each 35 mg vial contains 37 mg of agalsidase beta as well as 222 mg mannitol, 20.4 mg sodium phosphate monobasic monohydrate, and 59.2 mg sodium phosphate dibasic heptahydr | NA | NA | This is not a complete list of possible side effects. If you notice other effects not listed above, contact your doctor or pharmacist. | difficulty breathing; closing of the throat; hives; rash; itching; fever; shaking; chest tightness; high or low blood pressure; fast heartbeats; muscle pain; stomach pain; nausea or vomiting; dizziness; numbness or tingling; and headache have occurred upon injection of agalsidase beta in many patients. Most patients treated with agalsidase beta develop antibodies to agalsidase beta and many will develop symptoms of an infusion reaction. A slow rate of injection of the medication and pretreatment with other medications may decrease. | Link | NA | NA |
| 10502 | Th1096 | Idursulfase | >Th1096_Idursulfase SETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVPSFHVELCREGKNLLKHFRFRDLEEDPYLPG | 76000 | C2654H4000N688O774S14 | NA | NA | NA | 44 ± 19 minutes | Recombinant (from human cell line) form of human lysosomal enzyme, iduronate-2-sulfatase. Idursulfase is a 525-amino acid glycoprotein, which contains 8 N-linked glycosylation sites, occupied by complex oligosaccharide structures. Its enzyme activity depends on the post-translational modification of a specific cysteine to formylglycine. | For the treatment of Hunter syndrome in adults and children ages 5 and older. | Idursulfase is a purified form of the lysosomal enzyme human iduronate-2-sulfatase of recombinant DNA origin. It is designed to replace the natural enzyme, increasing catabolism of certain accumulated glycosaminoglycans (GAG), which abnormally accumulate in multiple tissue types in patients with mucopolysaccharidosis II (MPS-II, or Hunter syndrome). | Hunter's Syndrome is an X-linked recessive disease caused by insufficient levels of the lysosomal enzyme iduronate-2-sulfatase. This enzyme cleaves the terminal 2-O-sulfate moieties from the glycosaminoglycans (GAG) dermatan sulfate and heparan sulfate. Due to the missing or defective iduronate-2-sulfatase enzyme in patients with Hunter's Syndrome, GAG progressively accumulate in the lysosomes of a variety of cells, leading to cellular engorgement, organomegaly, tissue destruction and organ system dysfunction. Treatment of Hunter's Syndrome patients with idursulfase provides exogenous enzyme for uptake into cellular lysosomes. Targeting of idursulfase to the lysosome occurs by endocytosis from the cell surface. Mannose-6-phosphate (M6P) residues on the oligosaccharide chains allow specific binding of the enzymes to the M6P receptors on the cell surface, leading to cellular internalization of the enzyme, targeting to intracellular lysosomes and subsequent catabolism of accumulated GAG. | There is no experience with overdosage of Idursulfase in humans. Single intravenous doses of idursulfase up to 20 mg/kg were not lethal in male rats and cynomolgus monkeys (approximately 6.5 and 13 times, respectively, of the recommended human dose based on body surface area) and there were no clinical signs of toxicity. | NA | NA | NA | 3 mL/min/kg [Patients (7.7 - 27 years) with Hunter syndrome with treatment week 1(0.5 mg/kg ELAPRASE administered weekly as a 3-hour infusion)] . 3.4 mL/min/kg [patients (7.7 - 27 years) with Hunter syndrome with treatment week 27 (0.5 mg/kg ELAPRASE administered weekly as a 3-hour infusion)] | Alimentary Tract and Metabolism,Enzymes,Enzymes and Coenzymes,Esterases,Hydrolases,Hydrolytic Lysosomal Glycosaminoglycan-specific Enzyme,Sulfatases | NA | NA | NA | NA | Dermatan sulfate,Heparan sulfate,Perilipin-3 | Elaprase | SHIRE | SHIRE | indicated for patients with Hunter syndrome (Mucopolysaccharidosis II, MPS II). ELAPRASE has been shown to improve walking capacity in patients 5 years and older. The safety and efficacy of ELAPRASE have not been established in pediatric patients less than 16 months of age | NA | Each vial contains an extractable volume of 3 mL with an idursulfase concentration of 2 mg/mL at a pH of approximately 6. Each vial contains 6 mg idursulfase, sodium chloride (24 mg), sodium phosphate monobasic monohydrate (6.75 mg), sodium phosphate dibasic heptahydrate (2.97 mg), and polysorbate 20 (0.66 mg). ELAPRASE does not contain preservatives. Each vial is for single use only. | Sterile, nonpyrogenic clear to slightly opalescent, colorless solution that must be diluted prior to administration in 0.9% Sodium Chloride Injection, USP | Intravenous infusion | dosage regimen of ELAPRASE is 0.5 mg per kg of body weight administered once weekly as an Intravenous infusion. | Life-threatening anaphylactic reactions have occurred in some patients during and up to 24 hours after ELAPRASE infusions. Anaphylaxis, presenting as respiratory distress, hypoxia, hypotension, urticaria and/or angioedema of throat or tongue have been reported to occur during and after ELAPRASE infusions, regardless of duration of the course of treatment. Closely observe patients during and after ELAPRASE administration and be prepared to manage anaphylaxis. Inform patients of the signs and symptoms of anaphylaxis and have them seek immediate medical care should symptoms occur. Patients with compromised respiratory function or acute respiratory disease may be at risk of serious acute exacerbation of their respiratory compromise due to hypersensitivity reactions, and require additional monitoring | Bone or muscle pain, chest pain, chills, cough, fast, pounding, or irregular heartbeat or pulse, feeling of warmth, fever, headache, hives or welts, itching, rash, redness of the face, neck, arms, and occasionally, upper chest redness of the skin, sneezing, sore throat, tightness in the chest, unusual tiredness or weakness. | Link | NA | NA |
| 10503 | Th1097 | Alglucosidase alfa | >Th1097_Alglucosidase_alfa AHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC | 105270.8 | C4435H6739N1175O1279S32 | NA | NA | NA | 2.3 ± 0.4 hours. | Recombinant (CHO cell derived) form of the human lysosomal enzyme, acid alpha-glucosidase (GAA), which is essential for the degradation of glygogen to glucose. It hydrolyses the alfa-1,4- and alfa-1,6- glycosidic linkages of lysosomal glycogen. The mature polypeptide is 883 residue long with a mass of 98,008 daltons and a total mass of approximately 109,000 daltons of the full-length glycosylated protein | For the treatment of Pompe disease (GAA deficiency) in infants and pediatric patients. | Pompe disease (glycogen storage disease type II, GSD II, glycogenosis type II, acid maltase deficiency) is an inherited disorder of glycogen metabolism caused by the absence or marked deficiency of the lysosomal enzyme GAA. In the infantile-onset form, Pompe disease results in intralysosomal accumulation of glycogen in various tissues, particularly cardiac and skeletal muscles, and hepatic tissues, leading to the development of cardiomyopathy, progressive muscle weakness, and impairment of respiratory function. In the juvenile- and adult-onset forms, intralysosomal accumulation of glycogen is limited primarily to skeletal muscle, resulting in progressive muscle weakness. Death in all forms is usually related to respiratory failure. Alglucosidase alfa provides an exogenous source of GAA. Binding to mannose-6-phosphate receptors on the cell surface has been shown to occur via carbohydrate groups on the GAA molecule, after which it is internalized and transported into lysosomes, where it undergoes proteolytic cleavage that results in increased enzymatic activity. It then exerts enzymatic activity in cleaving glycogen. | Alglucosidase alfa is designed to act as an exogenous source of GAA, acting to correct GAA deficiency that is the hallmark of Pompe disease. Alglucosidase alfa binds to mannose-6-phosphate receptors on the cell surface via carbohydrate groups on the GAA molecule, after which it is internalized and transported into lysosomes, where it undergoes proteolytic cleavage that results in increased enzymatic activity. It then exerts enzymatic activity in cleaving glycogen. Specifically, it hydrolyses alpha-1,4-glucose bonds. | There have been no reports of overdose with alglucosidase alfa. | NA | NA | 96 ± 16 mL/kg [20 mg/kg dose] 119 ± 28 mL/kg [40 mg/kg dose] | 25+/- 4 mL/hr/kg [4-hour IV infusion of 20 mg/kg] | Alimentary Tract and Metabolism,alpha-Glucosidases,Enzymes,Enzymes and Coenzymes,Glucosidases,Glycogen Storage Disease Type II,Glycoside Hydrolases,Hydrolases,Hydrolytic Lysosomal Glycogen-specific Enzyme | CA2416492 | 29-Apr-2008 | 10-Jul-2021 | NA | Cation-dependent mannose-6-phosphate receptor,Glycogen | LUMIZYME | Genzyme | Genzyme | LUMIZYME (alglucosidase alfa) [see DESCRIPTION] is a hydrolytic lysosomal glycogen-specific enzyme indicated for patients with Pompe disease (acid α-glucosidase (GAA) deficiency). | NA | Each 50 mg vial contains 52.5 mg alglucosidase alfa, 210 mg mannitol, 0.5 mg polysorbate 80, 9.9 mg sodium phosphate dibasic heptahydrate, 31.2 mg sodium phosphate monobasic monohydrate. Following reconstitution as directed, each vial contains 10.5 mL reconstituted solution and a total extractable volume of 10 mL at 5 mg/mL alglucosidase alfa. Alglucosidase alfa does not contain preservatives; each vial is for single use only. | Sterile, nonpyrogenic, white to off-white, lyophilized cake or powder for reconstitution with 10.3 Ml Sterile Water for Injection, USP | Intravenous infusion | The recommended dosage of alglucosidase alfa is 20 mg/kg body weight administered every 2 weeks as an Intravenous infusion. | NA | In clinical trials, the most common adverse reactions ( ≥ 5%) following alglucosidase alfa treatment were hypersensitivity reactions, and included anaphylaxis, rash, pyrexia, flushing/feeling hot, urticaria, headache, hyperhidrosis, nausea, cough, decreased oxygen saturation, tachycardia, tachypnea, chest discomfort, dizziness, muscle twitching, agitation, cyanosis, erythema, hypertension/increased blood pressure, pallor, rigors, tremor, vomiting, fatigue, and myalgia. | Link | NA | NA |
| 10504 | Th1097 | Alglucosidase alfa | >Th1097_Alglucosidase_alfa AHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC | 105270.8 | C4435H6739N1175O1279S32 | NA | NA | NA | 2.3 ± 0.4 hours. | Recombinant (CHO cell derived) form of the human lysosomal enzyme, acid alpha-glucosidase (GAA), which is essential for the degradation of glygogen to glucose. It hydrolyses the alfa-1,4- and alfa-1,6- glycosidic linkages of lysosomal glycogen. The mature polypeptide is 883 residue long with a mass of 98,008 daltons and a total mass of approximately 109,000 daltons of the full-length glycosylated protein | For the treatment of Pompe disease (GAA deficiency) in infants and pediatric patients. | Pompe disease (glycogen storage disease type II, GSD II, glycogenosis type II, acid maltase deficiency) is an inherited disorder of glycogen metabolism caused by the absence or marked deficiency of the lysosomal enzyme GAA. In the infantile-onset form, Pompe disease results in intralysosomal accumulation of glycogen in various tissues, particularly cardiac and skeletal muscles, and hepatic tissues, leading to the development of cardiomyopathy, progressive muscle weakness, and impairment of respiratory function. In the juvenile- and adult-onset forms, intralysosomal accumulation of glycogen is limited primarily to skeletal muscle, resulting in progressive muscle weakness. Death in all forms is usually related to respiratory failure. Alglucosidase alfa provides an exogenous source of GAA. Binding to mannose-6-phosphate receptors on the cell surface has been shown to occur via carbohydrate groups on the GAA molecule, after which it is internalized and transported into lysosomes, where it undergoes proteolytic cleavage that results in increased enzymatic activity. It then exerts enzymatic activity in cleaving glycogen. | Alglucosidase alfa is designed to act as an exogenous source of GAA, acting to correct GAA deficiency that is the hallmark of Pompe disease. Alglucosidase alfa binds to mannose-6-phosphate receptors on the cell surface via carbohydrate groups on the GAA molecule, after which it is internalized and transported into lysosomes, where it undergoes proteolytic cleavage that results in increased enzymatic activity. It then exerts enzymatic activity in cleaving glycogen. Specifically, it hydrolyses alpha-1,4-glucose bonds. | There have been no reports of overdose with alglucosidase alfa. | NA | NA | 96 ± 16 mL/kg [20 mg/kg dose] 119 ± 28 mL/kg [40 mg/kg dose] | 25+/- 4 mL/hr/kg [4-hour IV infusion of 20 mg/kg] | Alimentary Tract and Metabolism,alpha-Glucosidases,Enzymes,Enzymes and Coenzymes,Glucosidases,Glycogen Storage Disease Type II,Glycoside Hydrolases,Hydrolases,Hydrolytic Lysosomal Glycogen-specific Enzyme | CA2416492 | 29-Apr-2008 | 10-Jul-2021 | NA | Cation-dependent mannose-6-phosphate receptor,Glycogen | Myozyme | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10521 | Th1101 | Galsulfase | >Th1101_Galsulfase SGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM | 56012.6 | C2534H3851N691O719S16 | NA | NA | NA | 9 (6 to 21) minutes during the first week of treatment, 26 (8 to 40) minutes by the 24th week.. | A recombinant variant form of the polymorphic human enzyme, N-acetylgalactosamine 4-sulfatase. It is a glycoprotein with a molecular weight of approximately 56 kD and comprises 495 amino acids. It contains 6 N-linked glycosylation sites, four of which carry a bis-mannose-6-phosphate manose7 oligosaccharide for specific cellular recognition. It requires Ca-formylglycine for its catalytic activity. This residue is a post-translational modification of Cys53 and conserved in all members of the sulfatase enzyme family. | For the treatment of adults and children with Mucopolysaccharidosis VI. | Mucopolysaccharide storage disorders are caused by the deficiency of specific lysosomal enzymes required for the catabolism of GAG. Mucopolysaccharidosis VI (MPS VI, Maroteaux-Lamy syndrome) is characterized by the absence or marked reduction in N-acetylgalactosamine 4-sulfatase. The sulfatase activity deficiency results in the accumulation of the GAG substrate dermatan sulfate, throughout the body. This accumulation leads to widespread cellular, tissue, and organ dysfunction. Galsulfase is intended to provide an exogenous enzyme that will be taken up into lysosomes and increase the catabolism of GAG. Galsulfase uptake by cells into lysosomes is most likely mediated by the binding of mannose-6-phosphate-terminated oligosaccharide chains of galsulfase to specific mannose-6-phosphate receptors. | Galsulfase supplies recombinant-engineered galsulfase, a normal variant form of the polymorphic human enzyme, N-acetylgalactosamine 4-sulfatase. It is a lysosomal hydrolase that catalyzes the cleavage of the sulfate ester from terminal N-acetylgalactosamine 4-sulfate residues of GAG chondroitin 4-sulfate and dermatan sulfate. Increased catabolism of GAG in turn reduces systemic dermatan sulfate accumulation, thereby reducing the primary symptoms of MPS VI. | There is no experience with overdose of galsulfase. | NA | NA | Week 1: 56-323 mL/kg and 59-2799 mL/kg by week 24 | NA | Enzyme Replacement Agents | NA | NA | NA | NA | Dermatan sulfate,Perilipin-3 | Naglazyme | BioMarin | BioMarin | NAGLAZYME (galsulfase) is indicated for patients with Mucopolysaccharidosis VI (MPS VI, Maroteaux-Lamy syndrome). NAGLAZYME has been shown to improve walking and stair-climbing capacity. | NA | NAGLAZYME is supplied in clear Type I glass 5 mL vials. Each vial provides 5 mg galsulfase, 43.8 mg sodium chloride, 6.20 mg sodium phosphate monobasic monohydrate, 1.34 mg sodium phosphate dibasic heptahydrate, and 0.25 mg polysorbate 80 in a 5 mL extractable solution with pH of approximately 5.8. NAGLAZYME does not contain preservatives. Each vial is for single use only. | Sterile, nonpyrogenic, colorless to pale yellow, clear to slightly opalescent solution that must be diluted with 0.9% Sodium Chloride Injection, USP, prior to administration | Intravenous infusion | The recommended dosage regimen of NAGLAZYME is 1 mg per kg of body weight administered once weekly as an Intravenous infusion. Pretreatment with antihistamines with or without antipyretics is recommended 30 to 60 minutes prior to the start of the infusion. | NA | Serious adverse reactions experienced in this trial include apnea, pyrexia, and respiratory distress. Severe adverse reactions include chest pain, dyspnea, laryngeal edema, and conjunctivitis. The most common adverse reactions requiring interventions were infusion reactions. | Link | NA | NA |
| 10538 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | US5750497 | 12-May-1998 | 16-Jun-2019 | NA | Insulin receptor,Insulin-like growth factor 1 receptor | LEVEMIR | Novo Nordisk | Novo Nordisk | LEVEMIR is indicated to improve glycemic control in adults and children with diabetes mellitus. | NA | Each milliliter of LEVEMIR contains 100 units (14.2 mg/mL) insulin detemir, 65.4 meg inc, 2.06 mg m-cresol, 16.0 mg glycerol, 1.80 mg phenol, 0.89 mg disodium phosphate dihydrate, 1.17 mg sodium chloride, and water for injection. Hydrochloric acid and/or sodium hydroxide may be added to adjust pH. LEVEMIR has a pH of approximately 7.4 | Clear, colorless, aqueous, neutral Sterile solution | Subcutaneous | Patients who require twice-daily dosing can administer the evening dose with the evening meal, at bedtime, or 12 hours after the morning dose. The dose of LEVEMIR must be individualized based on clinical response. Blood glucose monitoring is essential in all patients receiving insulin therapy. | LEVEMIR is not recommended for the treatment of diabetic ketoacidosis. Intravenous rapid-acting or short-acting insulin is the preferred treatment for this condition. LEVEMIR is contraindicated in patients with hypersensitivity to LEVEMIR or any of its excipients. Reactions have included anaphylaxis. | Hypoglycemia, upper respiratory tract infection, Headache, Pharyngitis, Influenza-like illness, Abdominal Pain | Link | NA | NA |
| 10539 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | US6011007 | 1-Apr-2000 | 2-Feb-2014 | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10540 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | CA2171424 | 6-Apr-2002 | 16-09-2014 | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10541 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10542 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10543 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10544 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10545 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10546 | Th1106 | Insulin detemir | >Th1106_Insulin_detemir GIVEQCCTSICSLYQLENYCN | 5916.9 | C267H402N64O76S6 | NA | NA | NA | 5 to 7 hours | Recombinant (from yeast cells), long-acting human insulin analogue. It has a myristic acid (14-C fatty acid), bound to lysine at position B29, which increases self-association and albumin binding. Coupled with its slow systemic absorption from the injection site, prolongs its distribution into tissues enabling it to act for a longer time than native insulin. LEVEMIR | For the treatment of type 1 or 2 diabetes mellitus. May be used in combination with oral anti-diabetic agents in type 2 diabetic patients who are not in adequate metabolic control with oral anti-diabetic agents alone. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Increased insulin secretion following meals is responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin detemir is a long-acting insulin analogue with a flat and predictable action profile. It is used to mimic the basal levels of insulin in diabetic individuals. The onset of action of insulin detemir is 1 to 2 hours and its duration of action is up to 24 hours. Interestingly, it has a lower affinity (30%) for the insulin receptor than human insulin. | Insulin detemir binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. Insulin detemir's long duration of action appears to be a result of slow systemic absorption from the injection site and delayed distribution to target tissues. The myristic acid side chain on insulin detemir increases self-association and gives it a high binding affinity to serum albumin. These features slows its distribution into target tissues and prolongs its duration of action. | Hypoglycemia may occur with inappropriately high doses. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. Injection site reactions may also occur. Symptoms include: redness, inflammation, bruising, swelling and itching at the injection site. | As with natural insulin, all metabolites formed are inactive. | Maximum serum concentrations are reached 6 to 8 hours following subcutaneous injection. When single dose of 0.5 units/kg of insulin detemir was given to adult type 1 diabetes patients, the maximum serum concentration (Cmax) was 4,641 ± 2,299 pmol/L. Absorption is also dependent on the site of injection. When injected into the thigh, the AUC was lower than when injected into the deltoid and abdominal regions. Bioavailability is approximately 60%. | 0.1 L/kg | Apparent clearance (CL/F), type 1 diabetes adult patients = 3.41 ± 1.00 L/min·kg | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Long-Acting,Pancreatic Hormones,Peptide Hormones,Peptides | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10547 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | US6960561 | 11-Jan-2005 | 25-01-2023 | NA | Insulin receptor,Insulin-like growth factor 1 receptor | APIDRA | sanofi-aventis | sanofi-aventis | APIDRA is indicated to improve glycemic control in adults and children with diabetes mellitus. | NA | Each milliliter of APIDRA contains 100 units (3.49 mg) insulin glulisine, 3.15 mg metacresol, 6 mg tromethamine, 5 mg sodium chloride, 0.01 mg polysorbate 20, and water for injection. APIDRA has a pH of approximately 7.3. The pH is adjusted by addition of aqueous solutions of hydrochloric acid and/or sodium hydroxide | Sterile, aqueous, clear, and colorless solution | NA | APIDRA is a recombinant insulin analog that is equipotent to human insulin (i.e. one unit of APIDRA has the same glucose-lowering effect as one unit of regular human insulin) when given intravenously. When given subcutaneously, APIDRA has a more rapid onset of action and a shorter duration of action than regular human insulin. The dosage of APIDRA must be individualized. Blood glucose monitoring is essential in all patients receiving insulin therapy. The total daily insulin requirement may vary and is usually between 0.5 to 1 Unit/kg/day. Insulin requirements may be altered during stress, major illness, or with changes in exercise, meal patterns, or coadministered drugs. | APIDRA is contraindicated: during episodes of hypoglycemia, in patients who are hypersensitive to APIDRA or to any of its excipients When used in patients with known hypersensitivity to APIDRA or its excipients, patients may develop localized or generalized hypersensitivity reactions. | Hypoglycemia, Hypokalemia | Link | NA | NA |
| 10548 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | US6221633 | 24-04-2001 | 18-06-2018 | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10549 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10550 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10551 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10552 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10553 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10554 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10555 | Th1107 | Insulin glulisine | >Th1107_Insulin_glulisine GIVEQCCTSICSLYQLENYCN | 5823 | C258H384N64O78S6 | NA | NA | NA | Elimination half life= 42 minutes (SC injection) | Insulin glulisine is a recombinant (E. Coli derived), rapid-acting analog of human insulin. It contains two mutations, one at position B3, where R is replaced by K and the other at position B29, where K is replaced by E. This results in decrease hexamer formation and increased stability of the monomer, thus increasing the rate of absorption and quicker action as compared to native insulin. | For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). Insulin glulisine is a rapid-acting insulin analogue used to mimic postprandial insulin spikes in diabetic individuals. The onset of action of insulin glulisine is approximately 15 minutes. Its activity peaks 60 minutes following subcutaneous injection and its duration of action is 2-4 hours. | Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action. | Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia. | NA | Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection. | 13 L | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Hypoglycemia-Associated Agents,Insulin,Insulin Analog,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10630 | Th1128 | Velaglucerase alfa | >Th1128_Velaglucerase_alfa ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ | 63000 | C2532H3850N672O711S16 | NA | NA | NA | 11-12 Minutes | Gene-activated human recombinant glucocerebrosidase. It is used to treat Type 1 Gaucher disease, caused by a deficiency of the lysosomal enzyme glucocerebrosidase. Additionally, Velaglucerase alfa has also been investigated for use in Type 3 Gaucher disease. | Velaglucerase alfa is a hydrolytic lysosomal glucocerebroside-specific enzyme indicated for long-term enzyme replacement therapy for pediatric and adult patients with type 1 Gaucher disease. | NA | Velaglucerase alfa catalyzes the hydrolysis of glucocerebroside, reducing the amount of accumulated glucocerebroside. | NA | NA | NA | The mean volume of distribution at steady state ranges from 82 to 108 mL/kg (8.2% to 10.8% of body weight). | Mean clearance ranges from 6.72 to 7.56 mL/min/kg. | Enzymes | US7138262 | 21-11-2006 | 18-08-2020 | NA | Glucosylceramidase | VPRIV | Shire | Shire | long-term enzyme replacement therapy (ERT) for pediatric and adult patients with type 1 Gaucher disease. | NA | velaglucerase alfa (400 Units), citric acid, monohydrate (5.04 mg), polysorbate 20(0.44 mg), sodium citrate, dihydrate (51.76 mg), sucrose (200 mg) | VPRIV is supplied as a sterile, preservative free, lyophilized powder | Intravenous infusion | The recommended dose is 60 Units/kg administered every other week as a 60-minute Intravenous infusion. | NA | Headache, Dizziness, Abdominal pain, Nausea, Back pain, Joint pain (knee), Upper respiratory tract infection, Activated partial thromboplastin time prolonged, Infusion-related reaction*, Pyrexia, Asthenia/Fatigue | Link | NA | NA |
| 10636 | Th1131 | Taliglucerase alfa | >Th1131_Taliglucerase_alfa EFARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRR | 56637.94 | C2580H3918N680O727S17 | 10.54 | NA | NA | between 18.9 to 28.7 min. | Recombinant human glucocerebrosidase (a lysosomal enzyme) . Elelyso used in patients with type 1 Gaucher's disease | For the treatment of adult Type 1 Gaucher disease. | Patient's with Type 1 Gaucher disease have a long-term deficiency in the enzyme, glucocerebrosidase. Taliglucerase alfa is a modified form of glucocerebrosidase and is provided to counter this enzyme deficiency, resulting in smaller liver and spleen size, and improved thrombocytopenia and anemia. | Taliglucerase alfa is different from human glucocerebrosidase by two amino acids at the N terminal and up to 7 amino acids at the C terminal. This recombinant enzyme allows the hydrolysis reaction of glucocerebroside to glucose and ceramide that naturally occurs in healthy individuals. | The most common toxic reaction seen was infusion reactions such as urticaria, arthralgia, headache, and chest pain due to IV administration. | Metabolism was not determined. | Taliglucerase alfa is administered IV so absorption is 100%. | The steady state volume of distribution is between 7.30 to 11.7 L. | The systemic clearance was approximately 30 L/hr and 20 L/hr for 30 and 60 units/kg, respectively. | Enzymes | NA | NA | NA | NA | Glucocerebroside | Elelyso | Pfizer | Pfizer | long-term enzyme replacement therapy (ERT) for adult and pediatric patients with a confirmed diagnosis of Type 1 Gaucher disease. | NA | The quantitative composition of each 200 unit vial is D-mannitol (206.7 mg), polysorbate 80 (0.56 mg), sodium citrate (30.4 mg), and taliglucerase alfa (212 units). Citric acid may be added to adjust the pH at the time of manufacture. | ELELYSO is supplied as a sterile, non-pyrogenic, lyophilized powder. | Intravenous infusion | 60 units per kg of body weight | NA | pruritus, flushing, headache, arthralgia, pain in extremity, abdominal pain, vomiting, fatigue, back pain, dizziness, nausea, and rash. | Link | NA | NA |
| 10649 | Th1134 | Asparaginase erwinia chrysanthemi | >Th1134_Asparaginase_erwinia_chrysanthemi ADKLPNIVILATGGTIAGSAATGTQTTGYKAGALGVDTLINAVPEVKKLANVKGEQFSNMASENMTGDVVLKLSQRVNELLARDDVDGVVITHGTDTVEESAYFLHLTVKSDKPVVFVAAMRPATAISADGPMNLLEAVRVAGDKQSRGRGVMVVLNDRIGSARYITKTNASTLDTFKANEEGYLGVIIGNRIYYQNRIDKLHTTRSVFDVRGLTSLPKVDILYGYQDDPEYLYDAAIQHGVKGIVYAGMGAGSVSVRGIAGMRKAMEKGVVVIRSTRTGNGIVPPDEELPGLVSDSLNPAHARILLMLALTRTSDPKVIQEYFHTY | 140000 | C1546H2510N432O476S9 | NA | NA | NA | 18.2 hours | Erwinaze (asparaginase from Erwiniachryanthemi) is an asparaginase specific enzyme derived from Erwiniachrysanthemi. L-asparaginase is a homo-tetramer with each subnuit having a molecular weight of about 35 kDa. It is an antineoplastic agent and was FDA approved in November 19, 2011. | Asparaginase Erwinia chryanthemi is for the treatment of patients with acute lymphoblastic leukemia (ALL) that have developed a hypersensitivity to Escherichia coli-derivied asparaginase. It is a component of a multi-agent chemotherpeutic regimen for the treatment of the aforementioned disease and is considered second- or third- line treatment in European and American protocols. | NA | Asparaginase Erwinia chrysanthemi catalyzes the deamidation of asparagine to aspartic acid and ammonia, resulting in a reduction in circulating levels of asparagine in the plasma. The mechanism of action of Erwinaze is thought to be based on the inability of leukemic cells to synthesize asparagine due to lack of asparagine synthetase activity, resulting in cytotoxicity specific for leukemic cells that depend on an exogenous source of the amino acid asparagine for their protein metabolism and survival. | There are no known cases of overdose with asparaginase _Erwinia chrysanthemi_.[L149] In clinical trials, the most common adverse effects were hypersensitivity reactions, pancreatic toxicity, blood clots, hemorrhage, and liver toxicity.[L34714] Pancreatitis occurs in 8-14% of pediatric patients, with adolescents at the highest risk for developing this adverse event. Pancreatitis typically occurs after the first few weeks of asparaginase administration, which suggests this complication occurs from an underlying predisposition rather than a cumulative drug effect.[A7464] | Metabolism of asparaginase _Erwinia chrysanthemi_ has not been fully characterized; however, it is suspected to be metabolized into small peptides by catabolic pathways.[L34719] | In patients two to 80 years of age, intramuscular administration of asparaginase _Erwinia chrysanthemi_ 25,000 International Units (IU)/m2 resulted in serum trough asparaginase concentrations = 0.1 IU/mL at either 48-hour (n=35) or 72-hour (n=13) post third dose. 80% of patients evaluted at 48 hours and 38% of patients evaluated at 72 hours had serum asparaginase activity levels > 0.4 IU/mL.[L149] For asparaginase _Erwinia chrysanthemi_ (recombinant)-rywn, the median tmax is 10 hours and the mean absolute bioavailability is 37% in healthy subjects.[L34719] | The volume of distribution of asparaginase _Erwinia chrysanthemi_ can be up to 5 L/m2.[L1448] The geometric mean (%CV) apparent volume of distribution of asparaginase _Erwinia chrysanthemi_ (recombinant)-rywn was 1.48 L/m2 (49%).[L34719] While asparaginases are not detectable in cerebrospinal fluid, asparagine in cerebrospinal fluid is depleted with systemic administration of any formulation of asparaginases.[L1448] | The geometric mean (%CV) apparent clearance of asparaginase _Erwinia chrysanthemi_ (recombinant)-rywn is 0.31 L/hour/m2 (36%).[L34719] | Amidohydrolases,Antineoplastic Agents,Asparaginase,Asparagine-specific Enzyme,Enzymes,Enzymes and Coenzymes,Hepatotoxic Agents,Hydrolases,Narrow Therapeutic Index Drugs,Thyroxine-binding globulin inhibitors | NA | NA | NA | NA | NA | Erwinaze | EUSA Pharma | EUSA Pharma | acute lymphoblastic leukemia | NA | Each vial contains 10,000 International Units of asparaginase Erwinia chrysanthemi, and the following inactive ingredients: glucose monohydrate (5.0 mg), sodium chloride (0.5 mg). | ERWINAZE is supplied as a Sterile, lyophilized, white powder in vials. | Intramuscular | 25,000 International Units/m² | Hypersensitivity reactions to ERWINAZE, including anaphylaxis., pancreatitis with prior L-asparaginase therapy, thrombosis with prior L-asparaginase therapy, hemorrhagic events with prior L-asparaginase therapy. | Hypersensitivity reactions, Pancreatitis, Glucose intolerance, Thrombosis and hemorrhage | Link | NA | NA |
| 10651 | Th1136 | Glucarpidase | >Th1136_Glucarpidase MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMARRLIMDLGAGK | 83000 | C3670H5926N10114O1140S12 | NA | NA | NA | Elimination half-life of 5.6 hours | Recombinant (E. Coli derived) form of the Pseudomonas sp. (strain RS-16) enzyme, carboxypeptidase G2. It inactivates methotrexate and other antifolates by hydrolyzing glutamate on the carboxyl terminal of these compounds. Since methotrexate is eliminated enzymatically and not by the kidneys, glucarpidase is indicated in patients on methotrexate treatment who have kidney dysfunction, and are experiencing an abnormally high plasma concentration of methotrexate (>1 micromole per liter). | Used in patients on methotrexate treatment who have kidney dysfunction, and are experiencing an abnormally high plasma concentration of methotrexate (> 1 micromole per liter). | Glucarpidase acts as an antidote to toxic methotrexate levels by elminating methotrexate by a non-kidney route. | Glucarpidase inactivates methotrexate, and other antifolates, by hydrolyzing glutamate on the carboxyl terminal of these compounds. For methotrexate specifically, it is hydrolyzed to the inactive metabolites glutamate and 4-deoxy-4-amino-N10-methylpteroic acid (DAMPA). | Most common adverse reactions include hypotension, flushing, nausea, vomiting, headache, and paresthesia. | Metabolism was not determined. | In healthy patients not taking methotrexate, the average maximum concentration for glucarpidase was 3.3 µg/mL. | Glucarpidase is likely limited to the plasma volume since its volume of distribution is 3.6 L. | In healthy patients not taking methotrexate, glucarpidase has a clearance of 7.5 mL/min. | Enzymes | NA | NA | NA | NA | Methotrexate | Voraxaze | BTG International | BTG International | toxic plasma methotrexate concentrations | NA | Each vial contains 1,000 Units of glucarpidase, lactose monohydrate (10 mg), Tris-HCl (0.6 mg) and zinc acetate dihydrate (0.002 mg). | VORAXAZE is supplied as a Sterile, preservative-free, white lyophilized powder in single-use vials | Intravenous Injection | 50 Units per kg | NA | paraesthesias, flushing, nausea and/or vomiting, hypotension, and headache | Link | NA | NA |
| 10687 | Th1152 | Drotrecogin alfa | >Th1152_Drotrecogin_alfa LIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP | 55000 | C1786H2779N509O519S29 | 6.78 | -0.291 | NA | 5.5 Hrs (Mammalian reticulocytes,in vitro | Drotrecogin alfa is activated human protein C that is synthesized by recombinant DNA technology. It is a glycoprotein of approximately 55 kilodalton molecular weight, consisting of a heavy chain and a light chain linked by a disulfide bond. Drotrecogin alfa was withdrawn from the market after a major study indicated that it was not effective in improving outcomes in patients with sepsis. | For reduction of mortality in patients with severe sepsis. | Drotrecogin alfa is activated human protein C that is synthesized by recombinant DNA technology. It is a glycoprotein of approximately 55 kilodalton molecular weight, consisting of a heavy chain and a light chain linked by a disulfide bond. Drotrecogin alfa inhibits factor Va and VIIIa, thereby reducing the coagulability of blood. | Activated protein C combines with protein S on platelet surfaces and then degrades factor Va and factor VIIIa, thereby reducing blood coagulability. | NA | NA | NA | NA | * 40 L/hr [severe sepsis adults] * 30 +/- 8 L/hr [patients without sepsis undergoing hemodialysis] * 28 +/- 9 L/hr [heathy] | Amino Acids, Peptides, and Proteins,Anti-Infective Agents,Anticoagulants,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Enzyme Precursors,Enzymes,Enzymes and Coenzymes,Fibrinolytic Agents,Glycoconjugates,Glycoproteins,Proteins,Recombinant Activated Protein C | CA2036894 | 15-01-2002 | 22-02-2011 | Clopidogrel, Enoxaprin, Dalteparin, Fondaparinux, Tinzaparin, enhance the adverse or toxic effect of drotrecogin alfa | Coagulation factor VIII,Coagulation factor V,Plasminogen activator inhibitor 1,Thrombomodulin,Vitamin K-dependent protein S,Prothrombin,Platelet factor 4,Plasma serine protease inhibitor,Serpin B6,Endothelial protein C receptor | Xigris | Eli Lilly and Company | Eli Lilly and Company | Xigris (drotrecogin alfa) is indicated for the reduction of mortality in adult patients with severe sepsis (sepsis associated with acute organ dysfunction) who have a high risk of death | NA | The 5 and 20 mg vials of Xigris contain 5.3 mg and 20.8 mg of drotrecogin alfa (activated), respectively. The 5 and 20 mg vials of Xigris (drotrecogin alfa) also contain 40.3 and 158.1 mg of sodium chloride, 10.9 and 42.9 mg of sodium citrate, and 31.8 and 124.9 mg of sucrose, respectively. | Xigris (drotrecogin alfa) is supplied as a sterile, lyophilized, white to off-white powder | Intravenous Infusion | Xigris (drotrecogin alfa) should be administered intravenously at an infusion rate of 24 mcg/kg/hr (based on actual body weight) for a total duration of infusion of 96 hours. Dose adjustment based on clinical or laboratory | Xigris (drotrecogin alfa) increases the risk of bleeding. Xigris (drotrecogin alfa) is contraindicated in the active internal bleeding, hemorraghic stroke, intracranial surgery, Trauma, Intracranial neospasm | Bleeding is the most commonly reported adverse reaction in patients receiving Xigris therapy | Link | NA | NA |
| 10688 | Th1152 | Drotrecogin alfa | >Th1152_Drotrecogin_alfa LIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP | 55000 | C1786H2779N509O519S30 | 6.78 | -0.291 | NA | 5.5 Hrs (Mammalian reticulocytes,in vitro | NA | NA | NA | NA | NA | NA | NA | NA | * 40 L/hr [severe sepsis adults] * 30 +/- 8 L/hr [patients without sepsis undergoing hemodialysis] * 28 +/- 9 L/hr [heathy] | Amino Acids, Peptides, and Proteins,Anti-Infective Agents,Anticoagulants,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Enzyme Precursors,Enzymes,Enzymes and Coenzymes,Fibrinolytic Agents,Glycoconjugates,Glycoproteins,Proteins,Recombinant Activated Protein C | CA2139468 | 21-08-2007 | 1-Mar-2015 | Tolmetin, Treprostinil, Urokinase, Heparin, Ketoprofen, Nadroparin, Tenecteplase, Vilazodone, Warfarin | Coagulation factor VIII,Coagulation factor V,Plasminogen activator inhibitor 1,Thrombomodulin,Vitamin K-dependent protein S,Prothrombin,Platelet factor 4,Plasma serine protease inhibitor,Serpin B6,Endothelial protein C receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10691 | Th1155 | Urokinase | >Th1155_Urokinase KPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLMSPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL | 31126.5 | C1376H2145N383O406S18 | 8.66 | -0.466 | 76°C | 12.6±6.2 minutes | Low molecular weight form of human urokinase, that consists of an A chain of 2,000 daltons linked by a sulfhydryl bond to a B chain of 30,400 daltons. Recombinant urokinase plasminogen activator | Urokinase can be used for the treatment of pulminary embolism, coronary artery thrombosis, IV catheter clearance, and venous and arterial blood clots. | Urokinase is used for the treatment of pulmonary embolisms. The low molecular weight form of human urokinase consists of an A chain of 2,000 daltons linked by a sulfhydryl bond to a B chain of 30,400 daltons. Urokinase is an enzyme (protein) produced by the kidney, and found in the urine. There are two forms of urokinase which differ in molecular weight but have similar clinical effects. Urokinase is the low molecular weight form. Urokinase acts on the endogenous fibrinolytic system. It converts plasminogen to the enzyme plasmin. Plasmin degrades fibrin clots as well as fibrinogen and some other plasma proteins. | Urokinase acts on the endogenous fibrinolytic system. It cleaves the Arg-Val bond in plasminogen to produce active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. | Patients experiencing an overdose may present with bleeding.[L12141] Treat patients with symptomatic and supportive measures which may include application of local pressure, administration of whole blood or plasma, and administration of aminocaproic acid.[L12141] | Because urokinase is a protein, it is expected to be metabolized by proteases to smaller proteins and amino acids. | Urokinase is delivered intravenously, so the bioavailability is high. | The volume of distribution of urokinase is 11.5L.[L12138] | Data regarding the clearance of urokinase is not readily available. | Agents causing angioedema,Amino Acids, Peptides, and Proteins,Anticoagulants,Biological Factors,Blood and Blood Forming Organs,Blood Proteins,Endopeptidases,Enzymes,Enzymes and Coenzymes,Fibrinolytic Agents,Hydrolases,Increased Thrombolysis,Peptide Hydrolases,Plasminogen Activators,Proteins,Serine Endopeptidases,Serine Proteases,Urokinase-Type Plasminogen Activator, antagonists & inhibitors | US4258030 | NA | NA | Drotrecogin alfa, Gingko biloba, Ginseng increases risk of bleeding. | Plasminogen,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1,Plasminogen activator inhibitor 2,Plasma serine protease inhibitor,Low-density lipoprotein receptor-related protein 2,Suppressor of tumorigenicity 14 protein,Nidogen-1 | Kinlytic | NA | NA | For the lysis of acute massive pulmonary emboli, defined as obstruction of blood flow to a lobe or multiple segments; For the lysis of pulmonary emboli accompanied by unstable hemodynamics, i.e., failure to maintain blood pressure without supportive measures. | NA | Each mL contains 50,000 international units of urokinase activity, 0.5% mannitol, 5% Albumin (Human), and 1% sodium chloride (pH range 6.0 to 7.5). | Kinlytic (urokinase injection) is supplied as a sterile lyophilized white powder | Intravenous infusion | The loading dose of 4,400 international units per kilogram of Kinlyticâ„¢ (urokinase injection) is given at a rate of 90 mL per hour over a period of 10 minutes. | The use of Kinlytic (urokinase injection) is contraindicated in patients with a history of hypersensitivity to the product. It is also containdicated in stages like active internal bleeding, cardiopulmonary resustication, intracranial surgery. | hypoxia, cyanosis, dyspnea, tachycardia, hypotension, hypertension, acidosis, fever and/or chills/rigors, back pain, vomiting, and nausea. | Link | NA | NA |
| 10714 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | Enhanced anticoagulant effect; increased risk of bleeding complications with Heparin; Heparin also Decreases half-life of antithrombin III | Antithrombin-III | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | Link | NA | NA |
| 10715 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | The anticoagulant effect of heparin is enhanced by concurrent treatment with Antithrombin III (Human), THROMBATE III® (antithrombin) in patients with hereditary AT-III deficiency. Thus, in order to avoid bleeding, reduced dosage of heparin is recommended during treatment with THROMBATE (antithrombin) III. | Antithrombin-III | Thrombate III | GRIFOLS USA, LLC | GRIFOLS USA, LLC | Indicated for the treatment of patients with hereditary antithrombin III deficiency in connection with surgical or obstetrical procedures or when they suffer from thromboembolism. | NA | NA | kit | NA | Dosage should be determined on an individual basis based on the pre-therapy plasma antithrombin III (AT-III) level, in order to increase plasma AT-III levels to the level found in normal human plasma (100%). It is recommended that following an initial dose of THROMBATE (antithrombin) III, plasma levels of AT-III be initially monitored at least every 12 hours and before the next infusion of THROMBATE (antithrombin) III to maintain plasma AT-III levels greater than 80%. | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | NA | NA | NA |
| 10716 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | The anticoagulant effect of heparin is enhanced by concurrent treatment with Antithrombin III (Human), THROMBATE III® (antithrombin) in patients with hereditary AT-III deficiency. Thus, in order to avoid bleeding, reduced dosage of heparin is recommended during treatment with THROMBATE (antithrombin) III. | Antithrombin-III | Thrombate III | Grifols Therapeutics Inc | Grifols Therapeutics Inc | Indicated for the treatment of patients with hereditary antithrombin III deficiency in connection with surgical or obstetrical procedures or when they suffer from thromboembolism. | NA | 500 unit | powder for solution | NA | Dosage should be determined on an individual basis based on the pre-therapy plasma antithrombin III (AT-III) level, in order to increase plasma AT-III levels to the level found in normal human plasma (100%). It is recommended that following an initial dose of THROMBATE (antithrombin) III, plasma levels of AT-III be initially monitored at least every 12 hours and before the next infusion of THROMBATE (antithrombin) III to maintain plasma AT-III levels greater than 80%. | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | NA | NA | NA |
| 10717 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | The anticoagulant effect of heparin is enhanced by concurrent treatment with Antithrombin III (Human), THROMBATE III® (antithrombin) in patients with hereditary AT-III deficiency. Thus, in order to avoid bleeding, reduced dosage of heparin is recommended during treatment with THROMBATE (antithrombin) III. | Antithrombin-III | Thrombate III | Grifols Therapeutics Inc | Grifols Therapeutics Inc | Indicated for the treatment of patients with hereditary antithrombin III deficiency in connection with surgical or obstetrical procedures or when they suffer from thromboembolism. | NA | 1000 unit | powder for solution | NA | Dosage should be determined on an individual basis based on the pre-therapy plasma antithrombin III (AT-III) level, in order to increase plasma AT-III levels to the level found in normal human plasma (100%). It is recommended that following an initial dose of THROMBATE (antithrombin) III, plasma levels of AT-III be initially monitored at least every 12 hours and before the next infusion of THROMBATE (antithrombin) III to maintain plasma AT-III levels greater than 80%. | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | NA | NA | NA |
| 10718 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | The anticoagulant effect of heparin is enhanced by concurrent treatment with Antithrombin III (Human), THROMBATE III® (antithrombin) in patients with hereditary AT-III deficiency. Thus, in order to avoid bleeding, reduced dosage of heparin is recommended during treatment with THROMBATE (antithrombin) III. | Antithrombin-III | Thrombate III | GRIFOLS USA, LLC | GRIFOLS USA, LLC | Indicated for the treatment of patients with hereditary antithrombin III deficiency in connection with surgical or obstetrical procedures or when they suffer from thromboembolism. | NA | NA | kit | NA | Dosage should be determined on an individual basis based on the pre-therapy plasma antithrombin III (AT-III) level, in order to increase plasma AT-III levels to the level found in normal human plasma (100%). It is recommended that following an initial dose of THROMBATE (antithrombin) III, plasma levels of AT-III be initially monitored at least every 12 hours and before the next infusion of THROMBATE (antithrombin) III to maintain plasma AT-III levels greater than 80%. | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | NA | NA | NA |
| 10719 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | The anticoagulant effect of heparin is enhanced by concurrent treatment with Antithrombin III (Human), THROMBATE III® (antithrombin) in patients with hereditary AT-III deficiency. Thus, in order to avoid bleeding, reduced dosage of heparin is recommended during treatment with THROMBATE (antithrombin) III. | Antithrombin-III | Thrombate III Pws IV 1000iu/vial | Miles Inc. Pharmaceutical Division | Miles Inc. Pharmaceutical Division | Indicated for the treatment of patients with hereditary antithrombin III deficiency in connection with surgical or obstetrical procedures or when they suffer from thromboembolism. | NA | 1000 unit | powder for solution | NA | Dosage should be determined on an individual basis based on the pre-therapy plasma antithrombin III (AT-III) level, in order to increase plasma AT-III levels to the level found in normal human plasma (100%). It is recommended that following an initial dose of THROMBATE (antithrombin) III, plasma levels of AT-III be initially monitored at least every 12 hours and before the next infusion of THROMBATE (antithrombin) III to maintain plasma AT-III levels greater than 80%. | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | NA | NA | NA |
| 10720 | Th1165 | Antithrombin III human | NA | 58000 | NA | NA | NA | NA | 2.5 - 3.8 hs | A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. | Short-term replacement therapy for prevention or treatment of thromboembolism in selected patients with congenital antithrombin III deficiency at high risk for thromboembolism (i.e., those undergoing surgical or obstetrical procedures) or those with thromboembolism | It s the major plasma inhibitor of thrombin. Inactivation of thrombin by AT-III occurs by formation of a covalent bond resulting in an inactive 1:1 stoichiometric complex between the two, involving an interaction of the active serine of thrombin and an arginine reactive site on AT-III. AT-III is also capable of inactivating other components of the coagulation cascade including factors IXa, Xa, XIa, and XIIa, as well as plasmin. | Neutralizes serine proteinases such as thrombin, plasmin, and activated coagulation factors IX, X, XI, and XII; Principally neutralizes thrombin and activated coagulation factor X (Xa); Neutralization of factor Xa prevents thrombin generation (e.g., decreased formation of prothrombin fragment 1.2 [F1 and F2]); Neutralization of thrombin prevents conversion of fibrinogen to fibrin; lowly and irreversibly complexes stoichiometrically with these coagulation factors; such reactions are rapid in presence of endogenous heparin-like proteoglycans or exogenous heparin; Inhibits thrombus formation. | NA | <5% metabolized to low molecular weight breakdown products. | Therapeutic target plasma concentrations in patients with congenital antithrombin III deficiency range from 80–120% of values in healthy adults. At plasma concentrations =70% of normal, increased thrombin generation. Supraphysiologic plasma concentrations (e.g., 150–200% of normal) have increased bleeding risk in patients with sepsis and disseminated intravascular coagulation, not known whether supraphysiologic concentrations increase bleeding risk in patients with congenital antithrombin III deficiency. | Distributed into plasma (39%), extravascular space (49%), and vascular endothelial cells (11%). | NA | Alpha-Globulins,Amino Acids, Peptides, and Proteins,Anticoagulants,Antithrombin III,Antithrombin III, agonists,Antithrombin Proteins,Biological Factors,Blood and Blood Forming Organs,Blood Coagulation Factor Inhibitors,Blood Proteins,Carbohydrates,Drugs that are Mainly Renally Excreted,Enzyme Inhibitors,Globulins,Glycosaminoglycans,Hematologic Agents,Oligosaccharides,Peptides,Polysaccharides,Proteins,Serum Globulins | NA | NA | NA | The anticoagulant effect of heparin is enhanced by concurrent treatment with Antithrombin III (Human), THROMBATE III® (antithrombin) in patients with hereditary AT-III deficiency. Thus, in order to avoid bleeding, reduced dosage of heparin is recommended during treatment with THROMBATE (antithrombin) III. | Antithrombin-III | Thrombate III Pws IV 500iu/vial | Miles Inc. Pharmaceutical Division | Miles Inc. Pharmaceutical Division | Indicated for the treatment of patients with hereditary antithrombin III deficiency in connection with surgical or obstetrical procedures or when they suffer from thromboembolism. | NA | 500 unit | powder for solution | NA | Dosage should be determined on an individual basis based on the pre-therapy plasma antithrombin III (AT-III) level, in order to increase plasma AT-III levels to the level found in normal human plasma (100%). It is recommended that following an initial dose of THROMBATE (antithrombin) III, plasma levels of AT-III be initially monitored at least every 12 hours and before the next infusion of THROMBATE (antithrombin) III to maintain plasma AT-III levels greater than 80%. | NA | Dizziness, chest tightness, nausea, foul taste, chills, cramps, shortness of breath, chest pain, film over eye, lightheadedness, bowel fullness, hives, fever, oozing, hematoma formation. | NA | NA | NA |
| 10721 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180000 | C7108H11008N1968O2206S56 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10722 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180001 | C7108H11008N1968O2206S57 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharma Ghbh | Alexion Pharma Ghbh | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 100 mg | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10723 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180002 | C7108H11008N1968O2206S58 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharmaceuticals Inc. | Alexion Pharmaceuticals Inc. | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 18 mg/.45mL | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10724 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180003 | C7108H11008N1968O2206S59 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharma Ghbh | Alexion Pharma Ghbh | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 40 mg | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10725 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180004 | C7108H11008N1968O2206S60 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharma Ghbh | Alexion Pharma Ghbh | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 40 mg | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10726 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180005 | C7108H11008N1968O2206S61 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharma Ghbh | Alexion Pharma Ghbh | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 40 mg | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10727 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180006 | C7108H11008N1968O2206S62 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharma Ghbh | Alexion Pharma Ghbh | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 40 mg | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10728 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180007 | C7108H11008N1968O2206S63 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharmaceuticals Inc. | Alexion Pharmaceuticals Inc. | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 80 mg/.8mL | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10729 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180008 | C7108H11008N1968O2206S64 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharmaceuticals Inc. | Alexion Pharmaceuticals Inc. | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 40 mg/mL | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10730 | Th1166 | Asfotase Alfa | >Th1166_Asfotase_Alfa LVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSLKDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKDIDDDDDDDDDD | 180009 | C7108H11008N1968O2206S65 | NA | NA | NA | Approximately 5 days. | Asfotase Alfa is a first-in-class bone-targeted enzyme replacement therapy designed to address the underlying cause of hypophosphatasia (HPP)â€â€deficient alkaline phosphatase (ALP). Hypophosphatasia is almost always fatal when severe skeletal disease is obvious at birth. By replacing deficient ALP, treatment with Asfotase Alfa aims to improve the elevated enzyme substrate levels and improve the body’s ability to mineralize bone, thereby preventing serious skeletal and systemic patient morbidity and premature death. Asfotase alfa was first approved by Pharmaceuticals and Medicals Devices Agency of Japan (PMDA) on July 3, 2015, then approved by the European Medicine Agency (EMA) on August 28, 2015, and was approved by the U.S. Food and Drug Administration (FDA) on October 23, 2015. | Indicated for the treatment of patients with perinatal/infantile and juvenile onset hypophosphatasia (HPP). | Perinatal/infantile- and juvenile-onset HPP patients treated with Asfotase alfa had reductions in plasma TNSALP (tissue non-specific alkaline phosphatase) substrates, PPi and pyridoxal 5'-phosphate (PLP) within 6 to 12 weeks of treatment. Reductions in plasma PPi and PLP levels did not correlate with clinical outcomes. Bone biopsy data from perinatal/infantile-onset and juvenile-onset HPP patients treated with Asfotase alfa demonstrated decreases in osteoid volume and thickness indicating improved bone mineralization. | HPP is caused by a deficiency in TNSALP (tissue non-specific alkaline phosphatase) enzyme activity, which leads to elevations in several TNSALP substrates, including inorganic pyrophosphate (PPi). Elevated extracellular levels of PPi block hydroxyapatite crystal growth which inhibits bone mineralization and causes an accumulation of unmineralized bone matrix which manifests as rickets and bone deformation in infants and children and as osteomalacia (softening of bones) once growth plates close, along with muscle weakness. Replacement of the TNSALP enzyme upon Asfotase alfa treatment reduces the enzyme substrate levels. | There are no available human data on Asfotase Alfa use in pregnant women to inform a drug associated risk. In animal reproduction studies, Asfotase Alfa administered intravenously to pregnant rats and rabbits during the period of organogenesis showed no evidence of fetotoxicity, embryolethality or teratogenicity at doses causing plasma exposures up to 21 and 24 times, respectively, the exposure at the recommended human dose. | NA | NA | NA | NA | Enzymes Alimentary Tract and Metabolism | NA | NA | NA | NA | Pyrophosphate | Strensiq | Alexion Pharmaceuticals Inc. | Alexion Pharmaceuticals Inc. | STRENSIQâ„¢ is indicated for the treatment of patients with perinatal/infantile-and juvenile-onset hypophosphatasia (HPP). | NA | 28 mg/.7mL | Solution | Subcutaneous | The recommended dosage regimen of STRENSIQ for the treatment of perinatal/infantileonset HPP is 6 mg/kg per week administered subcutaneously as either: 2 mg/kg three times per week, or 1 mg/kg six times per week. Injection site reactions may limit the tolerability of the six times per week regimen | NA | Hypersensitivity Reactions; Lipodystrophy; Ectopic Calcifications. | Link | NA | NA |
| 10763 | Th1177 | Elosulfase alfa | >Th1177_Elosulfase_alfa APQPPNILLLLMDDMGWGDLGVYGEPSRETPLCSPSRAALLTGRLPIRNGFYTTNAHARNLLKKAGYVSKIVGKWHLGHRPQFHPLKHGFNIPVYRDWEMVGRYYEEFPINLKTGEANLTFLYWAVDATHAPVYASKPFLGTSQRGRYGDVADNTFVFFTSDNGAALISAPEQGGSNGPFPGHVTAGQVSHQLGSIMDLFTTSLALAGLTLMDRPIFYYRGDTLMAATLGQHKAHFWTWTVTTHNLEDHTKLPLIFHLGRDPGERFPLSFEALVPAQPQLNVCNWAVMNWAPPGCEKLGKPNLDRMAAEGLLFPNFYSANAYTPQEIVGGIPDSEQLLPEDEWFGSPNCHFGPYDNKARPQIYLQEALDFIKRQARHHPFAVREIDDSIGKILELLQDLHLCGKQTTFEGGMREPALAWWPPSDRAIDGLNLLPTLLQGRNSWENFRQGIDFCPGQNVSGASAEYQEALSRITSVVQQHQCLTPPESIPKKCLWSH | 110800 | C5020H7588N1364O1418S34 | NA | NA | NA | week 0: 7.52 min week 22: 35.9 min | Elosulfase alfa is a synthetic version of the enzyme N-acetylgalactosamine-6-sulfatase. It was approved by the FDA in 2014 for the treatment of Morquio syndrome. Elosulfase alfa was developed by BioMarin Pharmaceutical Inc. and is marketed under the brand Vimizimâ„¢. The recommended dose is 2 mg per kg given intravenously over a minimum range of 3.5 to 4.5 hours, based on infusion volume, once every week. | Vimizim is a hydrolytic lysosomal glycosaminoglycan (GAG)-specific enzyme indicated for patients with Mucopolysaccharidosis type IVA (MPS IVA; Morquio A syndrome). | AUC: 238 min x μg/mL, standard deviation 100. | Mucopolysaccharidoses comprise a group of lysosomal storage disorders caused by the deficiency of specific lysosomal enzymes required for the catabolism of glycosaminoglycans (GAG). Mucopolysaccharidosis IVA (MPS IVA, Morquio A Syndrome) is characterized by the absence or marked reduction in N-acetylgalactosamine-6-sulfatase activity. The sulfatase activity deficiency results in the accumulation of the GAG substrates, KS and C6S, in the lysosomal compartment of cells throughout the body. The accumulation leads to widespread cellular, tissue, and organ dysfunction. Vimizim is intended to provide the exogenous enzyme N-acetylgalactosamine-6-sulfatase that will be taken up into the lysosomes and increase the catabolism of the GAGs KS and C6S. Elosulfase alfa uptake by cells into lysosomes is mediated by the binding of mannose-6-phosphate-terminated oligosaccharide chains of elosulfase alfa to mannose-6-phosphate receptors. In the absence of an animal disease model that recapitulates the human disease phenotype, elosulfase alfa pharmacological activity was evaluated using human primary chondrocytes from two MPS IVA patients. Treatment of MPS IVA chondrocytes with elosulfase alfa induced clearance of KS lysosomal storage from the chondrocytes. | NA | NA | Cmax: 1.49 µg/mL, standard deviation 0.534. | 396 mL/kg, standard deviation 316. | 10.0 mL/min/kg. (standard deviation: 3.73). | Enzymes; Alimentary Tract and Metabolism | NA | NA | NA | NA | N-acetylgalactosamine-6-sulfatase | NA | NA | NA | NA | NA | NA | Injection, solution | IV | NA | NA | NA | NA | NA | NA |
| 10764 | Th1177 | Elosulfase alfa | >Th1177_Elosulfase_alfa APQPPNILLLLMDDMGWGDLGVYGEPSRETPLCSPSRAALLTGRLPIRNGFYTTNAHARNLLKKAGYVSKIVGKWHLGHRPQFHPLKHGFNIPVYRDWEMVGRYYEEFPINLKTGEANLTFLYWAVDATHAPVYASKPFLGTSQRGRYGDVADNTFVFFTSDNGAALISAPEQGGSNGPFPGHVTAGQVSHQLGSIMDLFTTSLALAGLTLMDRPIFYYRGDTLMAATLGQHKAHFWTWTVTTHNLEDHTKLPLIFHLGRDPGERFPLSFEALVPAQPQLNVCNWAVMNWAPPGCEKLGKPNLDRMAAEGLLFPNFYSANAYTPQEIVGGIPDSEQLLPEDEWFGSPNCHFGPYDNKARPQIYLQEALDFIKRQARHHPFAVREIDDSIGKILELLQDLHLCGKQTTFEGGMREPALAWWPPSDRAIDGLNLLPTLLQGRNSWENFRQGIDFCPGQNVSGASAEYQEALSRITSVVQQHQCLTPPESIPKKCLWSH | 110800 | C5020H7588N1364O1418S34 | NA | NA | NA | week 0: 7.52 min week 22: 35.9 min | Elosulfase alfa is a synthetic version of the enzyme N-acetylgalactosamine-6-sulfatase. It was approved by the FDA in 2014 for the treatment of Morquio syndrome. Elosulfase alfa was developed by BioMarin Pharmaceutical Inc. and is marketed under the brand Vimizimâ„¢. The recommended dose is 2 mg per kg given intravenously over a minimum range of 3.5 to 4.5 hours, based on infusion volume, once every week. | Vimizim is a hydrolytic lysosomal glycosaminoglycan (GAG)-specific enzyme indicated for patients with Mucopolysaccharidosis type IVA (MPS IVA; Morquio A syndrome). | AUC: 238 min x μg/mL, standard deviation 100. | Mucopolysaccharidoses comprise a group of lysosomal storage disorders caused by the deficiency of specific lysosomal enzymes required for the catabolism of glycosaminoglycans (GAG). Mucopolysaccharidosis IVA (MPS IVA, Morquio A Syndrome) is characterized by the absence or marked reduction in N-acetylgalactosamine-6-sulfatase activity. The sulfatase activity deficiency results in the accumulation of the GAG substrates, KS and C6S, in the lysosomal compartment of cells throughout the body. The accumulation leads to widespread cellular, tissue, and organ dysfunction. Vimizim is intended to provide the exogenous enzyme N-acetylgalactosamine-6-sulfatase that will be taken up into the lysosomes and increase the catabolism of the GAGs KS and C6S. Elosulfase alfa uptake by cells into lysosomes is mediated by the binding of mannose-6-phosphate-terminated oligosaccharide chains of elosulfase alfa to mannose-6-phosphate receptors. In the absence of an animal disease model that recapitulates the human disease phenotype, elosulfase alfa pharmacological activity was evaluated using human primary chondrocytes from two MPS IVA patients. Treatment of MPS IVA chondrocytes with elosulfase alfa induced clearance of KS lysosomal storage from the chondrocytes. | NA | NA | Cmax: 1.49 µg/mL, standard deviation 0.534. | 396 mL/kg, standard deviation 316. | 10.0 mL/min/kg. (standard deviation: 3.73). | Enzymes; Alimentary Tract and Metabolism | NA | NA | NA | NA | N-acetylgalactosamine-6-sulfatase | Vimizim | Biomarin International Limited | Biomarin International Limited | Vimizim (elosulfase alfa) is indicated for patients with Mucopolysaccharidosis type IVA (MPS IVA; Morquio A syndrome). | NA | 1 mg | Solution | IV | The recommended dose is 2 mg per kg given intravenously over a minimum range of 3.5 to 4.5 hours, based on infusion volume, once every week. Pre-treatment with antihistamines with or without antipyretics is recommended 30 to 60 minutes prior to the start of the infusion | NA | Anaphylaxis and hypersensitivity reactions. | NA | NA | NA |
| 10765 | Th1177 | Elosulfase alfa | >Th1177_Elosulfase_alfa APQPPNILLLLMDDMGWGDLGVYGEPSRETPLCSPSRAALLTGRLPIRNGFYTTNAHARNLLKKAGYVSKIVGKWHLGHRPQFHPLKHGFNIPVYRDWEMVGRYYEEFPINLKTGEANLTFLYWAVDATHAPVYASKPFLGTSQRGRYGDVADNTFVFFTSDNGAALISAPEQGGSNGPFPGHVTAGQVSHQLGSIMDLFTTSLALAGLTLMDRPIFYYRGDTLMAATLGQHKAHFWTWTVTTHNLEDHTKLPLIFHLGRDPGERFPLSFEALVPAQPQLNVCNWAVMNWAPPGCEKLGKPNLDRMAAEGLLFPNFYSANAYTPQEIVGGIPDSEQLLPEDEWFGSPNCHFGPYDNKARPQIYLQEALDFIKRQARHHPFAVREIDDSIGKILELLQDLHLCGKQTTFEGGMREPALAWWPPSDRAIDGLNLLPTLLQGRNSWENFRQGIDFCPGQNVSGASAEYQEALSRITSVVQQHQCLTPPESIPKKCLWSH | 110800 | C5020H7588N1364O1418S35 | NA | NA | NA | week 0: 7.52 min week 22: 35.9 min | Elosulfase alfa is a synthetic version of the enzyme N-acetylgalactosamine-6-sulfatase. It was approved by the FDA in 2014 for the treatment of Morquio syndrome. Elosulfase alfa was developed by BioMarin Pharmaceutical Inc. and is marketed under the brand Vimizimâ„¢. The recommended dose is 2 mg per kg given intravenously over a minimum range of 3.5 to 4.5 hours, based on infusion volume, once every week. | Vimizim is a hydrolytic lysosomal glycosaminoglycan (GAG)-specific enzyme indicated for patients with Mucopolysaccharidosis type IVA (MPS IVA; Morquio A syndrome). | AUC: 238 min x μg/mL, standard deviation 100. | Mucopolysaccharidoses comprise a group of lysosomal storage disorders caused by the deficiency of specific lysosomal enzymes required for the catabolism of glycosaminoglycans (GAG). Mucopolysaccharidosis IVA (MPS IVA, Morquio A Syndrome) is characterized by the absence or marked reduction in N-acetylgalactosamine-6-sulfatase activity. The sulfatase activity deficiency results in the accumulation of the GAG substrates, KS and C6S, in the lysosomal compartment of cells throughout the body. The accumulation leads to widespread cellular, tissue, and organ dysfunction. Vimizim is intended to provide the exogenous enzyme N-acetylgalactosamine-6-sulfatase that will be taken up into the lysosomes and increase the catabolism of the GAGs KS and C6S. Elosulfase alfa uptake by cells into lysosomes is mediated by the binding of mannose-6-phosphate-terminated oligosaccharide chains of elosulfase alfa to mannose-6-phosphate receptors. In the absence of an animal disease model that recapitulates the human disease phenotype, elosulfase alfa pharmacological activity was evaluated using human primary chondrocytes from two MPS IVA patients. Treatment of MPS IVA chondrocytes with elosulfase alfa induced clearance of KS lysosomal storage from the chondrocytes. | NA | NA | Cmax: 1.49 µg/mL, standard deviation 0.534. | 396 mL/kg, standard deviation 316. | 10.0 mL/min/kg. (standard deviation: 3.73). | Enzymes; Alimentary Tract and Metabolism | NA | NA | NA | NA | N-acetylgalactosamine-6-sulfatase | Vimizim | Bio Marin Pharmaceutical Inc. | Bio Marin Pharmaceutical Inc. | Vimizim (elosulfase alfa) is indicated for patients with Mucopolysaccharidosis type IVA (MPS IVA; Morquio A syndrome). | NA | 5 mg/5mL | Injection, solution | IV | The recommended dose is 2 mg per kg given intravenously over a minimum range of 3.5 to 4.5 hours, based on infusion volume, once every week. Pre-treatment with antihistamines with or without antipyretics is recommended 30 to 60 minutes prior to the start of the infusion | NA | Anaphylaxis and hypersensitivity reactions. | NA | NA | NA |
| 10830 | Th1196 | Siltuximab | >Th1196_Siltuximab EVQLVESGGKLLKPGGSLKLSCAASGFTFSSFAMSWFRQSPEKRLEWVAEISSGGSYTYYPDTVTGRFTISRDNAKNTLYLEMSSLRSEDTAMYYCARGLWGYYALDYWGQGTSVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK | 145000 | C6450H9932N1688O2016S50 | NA | NA | NA | The mean terminal half life after the first intravenous infusion of 11 mg/kg is 20.6 days. | Siltuximab is a chimeric (human-mouse) monoclonal immunoglobulin G1-kappa antibody produced in a Chinese hamster ovary (CHO) cell line by recombinant DNA technology. Siltuximab prevents the binding of IL-6 to soluble and membrane-bound IL-6 receptors by forming high affinity complexes with human interleukin-6 (IL-6). Its use is indicated for the treatment of adult patients with multicentric Castleman’s disease (MCD) who are human immunodeficiency virus (HIV) negative and human herpesvirus-8 (HHV-8) negative. MCD is a rare blood disorder caused by dysregulated IL-6 production, proliferation of lymphocytes, and subsequent enlargement of the lymph nodes. It is administered as a 1 hour intravenous infusion every 3 weeks. | It is indicated for the treatment of patients with multicentric Castleman's disease (MCD) who are human immunodeficiency virus (HIV) negative and human herpesvirus-8 (HHV-8) negative. Siltuximab did not bind to virally produced IL-6 in a nonclinical study and was therefore not studied in patients with MCD who are HIV or HHV-8 positive. | Siltuximab-neutralized antibody-IL-6 complexes interfere with current immunological-based IL-6 quantification methods, therefore measurement of serum or plasma IL-6 concentrations should not be used as a pharmacodynamic marker during treatment. As well, cytochrome P450 enzymes in the liver are down regulated by infection and inflammation stimuli, which includes cytokines such as IL-6. By preventing IL-6 signalling through treatment with siltuximab, CYP450 activity may be increased leading to faster metabolism of drugs that are CYP450 substrates. | Siltuximab complexes with human IL-6 and prevents binding to soluble and membrane-bound IL-6 receptors, thereby inhibiting the proliferation of lymphocytes. | The most common side effects that occurred during siltuximab treatment were pruritis, increased weight, rash, hyperuricemia, and upper respiratory tract infection. Siltuximab should not be administered to patients with severe infections as it may mask signs and symptoms of acute inflammation including suppression of fever and acute phase reactants such as C-reactive protein (CRP). Gastrointestinal perforation has been reported in clinical trials, therefore use with caution in patients who may be at increased risk for GI perforation. | As siltuximab is an antibody, the expected consequence of metabolism is proteolytic degradation to small peptides and individual amino acids, and receptor-mediated clearance. | NA | Based on population pharmacokinetic analysis, the central volume of distribution in a male subject with body weight of 70 kg is 4.5 L. | Body weight was identified as the only statistically significant covariate of siltuximab clearance, therefore body weight based dosing is appropriate. Based on population pharmacokinetic analysis, the clearance of situximab in patients is 0.23 L/day. | Agents reducing cytokine levels,Amino Acids, Peptides, and Proteins,Antibodies,Antineoplastic Agents,Antineoplastic and Immunomodulating Agents,Blood Proteins,Cytochrome P-450 CYP3A Inducers,Cytochrome P-450 CYP3A Inhibitors,Cytochrome P-450 CYP3A4 Inducers,Cytochrome P-450 CYP3A4 Inducers (weak),Cytochrome P-450 CYP3A4 Inhibitors,Cytochrome P-450 CYP3A4 Inhibitors (weak),Cytochrome P-450 Enzyme Inducers,Cytochrome P-450 Enzyme Inhibitors,Globulins,Immunoglobulins,Immunoproteins,Immunosuppressive Agents,Immunotherapy,Interleukin Inhibitors,Interleukin-6 Antagonist,Proteins,Serum Globulins | US7612182 | 11-Mar-2009 | 8-Jan-2027 | Abiraterone, Alfuzosin, Alprazolam, Aminophylline, Amiodarone, Amlodipine, Apixaban, Apremilast, Aprepitant, Aripiprazole, Armodafinil, Atazanavir, Atorvastatin, Avanafil, Axitinib, Bedaquiline, Belimumab, Benzphetamine, Bisoprolol, Boceprevir, Bortezomib, Bosutinib, Brexpiprazole, Buprenorphine, Buspirone, Cabazitaxel, Cabozantinib, Calcitriol, Carbamazepine, Ceritinib, Chlordiazepoxide, Chloroquine, Cilostazol, Citalopram, Clarithromycin, Clonazepam, Clorazepate, Cobicistat, Cobimetinib, Conivaptan, Crizotinib, Cyclosporine, Cyproterone acetate, Daclatasvir, Dantrolene, Dapsone, Darifenacin, Darunavir, Dasatinib, Delavirdine, Denosumab, Dexamethasone, Diazepam, Dienogest, Diltiazem, Disopyramide, Docetaxel, Doxazosin, Doxorubicin, Dronedarone, Efavirenz, Eliglustat, Elvitegravir, Enzalutamide, Eplerenone, Erlotinib, Erythromycin, Escitalopram, Estradiol, Estrone sulfate, Eszopiclone, Ethosuximide, Etoposide, Etravirine, Everolimus, Exemestane, Felbamate, Felodipine, Fesoterodine, Flibanserin, Flunisolide, Flurazepam, Flutamide, Fosamprenavir, Fosaprepitant, Gefitinib, Guanfacine, Haloperidol, Hydrocodone, Hydroxyprogesterone caproate, Ibrutinib, Idelalisib, Imatinib, Indinavir, Irinotecan, Isavuconazonium, Isosorbide, Isosorbide Dinitrate, Isosorbide Mononitrate, Isradipine, Itraconazole, Ivabradine, Ivacaftor, Ixabepilone, Ixazomib, Ketoconazole, Lansoprazole, Lapatinib, Leflunomide, Levonorgestrel, Lidocaine, Lomitapide, Losartan, Lovastatin, Lurasidone, Macitentan, Maraviroc, Medroxyprogesterone acetate, Mefloquine, Methadone, Midazolam, Mifepristone, Mirtazapine, Modafinil, Naloxegol, Natalizumab, Nateglinide, Nefazodone, Nelfinavir, Nevirapine, Nicardipine, Nifedipine, Nilotinib, Nimodipine, Nisoldipine, Norethisterone, Olaparib, Ondansetron, Ospemifene, Oxycodone, Paclitaxel, Palbociclib, Panobinostat, Pazopanib, Perampanel, Pimecrolimus, Pimozide, Pipotiazine, Praziquantel, Primaquine, Progesterone, Quetiapine, Quinidine, Quinine, Rabeprazole, Ranolazine, Regorafenib, Repaglinide, Rifabutin, Rilpivirine, Riociguat, Ritonavir, Rivaroxaban, Roflumilast, Rolapitant, Ruxolitinib, Saquinavir, Sildenafil, Silodosin, Simeprevir, Simvastatin, Sipuleucel-T, Sirolimus, Solifenacin, Sonidegib, Spiramycin, Stiripentol, Sunitinib, Suvorexant, Tacrolimus, Tamoxifen, Tamsulosin, Tasimelteon, Telaprevir, Telithromycin, Temsirolimus, Teniposide, Tetracycline, Theophylline, Tiagabine, Ticagrelor, Ticlopidine, Tipranavir, Tofacitinib, Tolterodine, Tolvaptan, Toremifene, Trabectedin, Tramadol, Trastuzumab, Trazodone, Triazolam, Trimethoprim, Trimipramine, Ulipristal, Vandetanib, Vemurafenib, Venlafaxine, Verapamil, Vilazodone, Vinblastine, Vincristine, Vinorelbine, Vortioxetine, Zolpidem, Zonisamide, Zopiclone | Interleukin-6 | Sylvant | Janssen Inc | Janssen Inc | NA | NA | 100 mg | Lyophilized powder | Intravenous infusion | SYLVANT 11 mg/kg is given over 1 hour as an intravenous infusion administered every 3 weeks until treatment failure. | Severe hypersensitivity reaction to siltuximab or any of the excipients in SYLVANT. | Concurrent active severe infections; Infusion-related reactions and hypersensitivity | Link | NA | NA |
| 10831 | Th1197 | Sebelipase alfa | >Th1197_Sebelipase_alfa SGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ | 55000 | C1968H2945N507O551S15 | NA | NA | NA | 5.4-6.6 mins | Sebelipase alfa is a recombinant form of the enzyme lysosomal acid lipase (LAL) approved for the treatment of lysosomal acid lipase deficiency (LAL-D). The amino acid sequence for sebelipase alfa is the same as the amino acid sequence for human LAL. Sebelipase alfa is an orphan drug which is expected to cost about $310,000 for annual treatment in the United States. Sebelipase alfa is marketed under the brand name Kanumaâ„¢ by Alexion Pharmaceuticals, Inc. | Sebelipase alfa is a hydrolytic lysosomal cholesteryl ester and triacylglycerol-specific enzyme indicated for the treatment of patients with a diagnosis of Lysosomal Acid Lipase (LAL) deficiency. | In clinical trials, after initiation of dosing with KANUMA, breakdown of accumulated lysosomal lipid led to initial increases in LDL-c and triglycerides within the first 2 to 4 weeks of treatment. In general, following increases in LDL-c and triglycerides, these parameters decreased to below pre-treatment values within 8 weeks of treatment with KANUMA. | LAL deficiency is an autosomal recessive lysosomal storage disorder characterized by a genetic defect resulting in a marked decrease or loss in activity of the lysosomal acid lipase (LAL) enzyme. The primary site of action of the LAL enzyme is the lysosome, where the enzyme normally causes the breakdown of lipid particles including LDL-c. Deficient LAL enzyme activity results in progressive complications due to the lysosomal accumulation of cholesteryl esters and triglycerides in multiple organs, including the liver, spleen, intestine, and the walls of blood vessels. The resulting lipid accumulation in the liver may lead to increased liver fat content and progression of liver disease, including fibrosis and cirrhosis. Lipid accumulation in the intestinal wall leads to malabsorption and growth failure. In parallel, dyslipidemia due to impaired degradation of lysosomal lipid is common with elevated LDL-c and triglycerides and low HDL-cholesterol (HDL-c). Sebelipase alfa binds to cell surface receptors via glycans expressed on the protein and is subsequently internalized into lysosomes. Sebelipase alfa catalyzes the lysosomal hydrolysis of cholesteryl esters and triglycerides to free cholesterol, glycerol and free fatty acids. | There are no data regarding overdose with sebelipase alfa. Patients in clinical trials were exposed to doses as high as 7.5 mg/kg once weekly with no specific adverse effects observed.[L39342] | As with other therapeutic proteins, the metabolism of sebelipase alfa likely occurs via catabolism to smaller peptides and amino acids. | In patients 4-11 years old, the AUC and Cmax of sebelipase alfa following intravenous administration of 1 mg/kg every other week were 942 ng.hr/mL and 490 ng/mL, respectively.[L39337] In patients =12 years old, the AUC and Cmax ranged between 1454-1861 ng.hr/mL and 784-957 ng/mL, respectively.[L39337] The approximate Tmax of sebelipase alfa was similar across all age groups tested and ranged between 1.1-1.3 hours.[L39337] | In patients 4-11 years old, the central volume of distribution was approximately 3.6 L.[L39337] In patients =12 years old, the central volume of distribution ranged from approximately 5.3 to 5.4 L.[L39337] | Across all age groups included in pharmacokinetic testing, the mean clearance of sebelipase alpha following intravenous administration of 1 mg/kg every other week ranged from 31.1 - 38.2 L/h.[L39337] | Enzymes | NA | NA | NA | NA | NA | Kanuma | Alexion Pharmaceuticals, Inc. | Alexion Pharmaceuticals, Inc. | KANUMAâ„¢ is indicated for the treatment of patients with a diagnosis of Lysosomal Acid Lipase (LAL) deficiency. | NA | 20 mg/10 mL | Aqueous solution | Intravenous infusion | The recommended starting dosage is 1 mg/kg administered once weekly as an intravenous infusion. For patients who do not achieve an optimal clinical response, increase to 3 mg/kg once weekly. | NA | Diarrhea, vomiting, fever, rhinitis, anemia, cough, nasopharyngitis, urticaria. | Link | NA | NA |
| 10832 | Th1198 | Sacrosidase | NA | 100000 | NA | NA | NA | NA | NA | Sacrosidase is a liquid enzyme preparation from S.cerevisiae used for the treatment of congenital sucrose-isomaltase deficiency (CSID). People with CSID have variable amounts of sucrose-isomaltase enzyme activity and therefore have issues metabolizing dietary disaccharide sucrose causing chronic or intermittent watery diarrhea in infants and children. Treatment options for these patients are limited and usually consists of a lifelong sucrose-free diet; therefore, sacrosidase offers a potential alternative for symptom relief. | For the treatment of congenital sucrose-isomaltase deficiency (CSID). | Sucrase is naturally produced in the brush border of the small intestine, primarily the distal duodenum and jejunum. Sucrase hydrolyzes the disaccharide sucrose into its component monosaccharides, glucose and fructose. Isomaltase breaks down disaccharides from starch into simple sugars. SUCRAID does not contain isomaltase. | Sacrosidase is a [beta]-fructofuranoside fructohydrolase that hydrolyzes sucrose. Unlike human intestinal sucrase-isomaltase, it has no activity with oligosaccharides containing 1,6 glucosyl bonds. | NA | NA | It has been suggested that sucrose is better absorbed (and sacrosidase activity preserved) when patients were given milk before sacrosidase rather than consuming the enzyme product alone. Therefore, it has been recommended to take half dose of sacrosidase just after a protein-containing meal, and the other half of the dose approximately half-way through the meal. | NA | NA | Alimentary Tract and Metabolism,Enzymes,Enzymes and Coenzymes,Glycoside Hydrolases,Hydrolases,Sucrose-specific Enzyme | NA | NA | NA | NA | NA | Sucraid | QOL Medical, LLC | QOL Medical, LLC | NA | ß,D-fructofuranoside fructohydrolase | NA | Solution | Oral | The recommended dosage is 1 or 2 mL (8,500 to 17,000 I.U.) or 1 or 2 full measuring scoops (each full measuring scoop equals 1mL; 28 drops from the SUCRAID container tip equals 1mL) taken orally with each meal or snack diluted with 2 to 4 ounces of water, milk or infant formula. The beverage or infant formula should be served cold or at room temperature. The beverage or infant formula should not be warmed or heated before or after addition of SUCRAID because heating is likely to decrease potency. SUCRAID should not be reconstituted or consumed with fruit juice since its acidity may reduce the enzyme activity. It is recommended that approximately half of the dosage be taken at the beginning of the meal or snack and the remainder be taken during the meal or snack. | Patients known to be hypersensitive to yeast, yeast products, glycerin (glycerol), or papain. | Abdominal pain, vomiting; nausea; diarrhea; constipation; insomnia; headache; nervousness and dehydration. | Link | NA | NA |
| 10849 | Th1212 | Insulin Pork | >Th1212_Insulin_Pork GIVEQCCTSICSLYQLENYCN | 5795.6 | C257H387N65O76S6 | 5.39 | 0.218 | NA | NA | Insulin isolated from pig pancreas. Composed of alpha and beta chains, processed from pro-insulin. Forms a hexameric structure. | For the treatment of type I and II diabetes mellitus. | Insulin is used in the treatment of type I and type II diabetes. The primary activity of insulin is the regulation of glucose metabolism. In muscle and other tissues (except the brain), insulin causes rapid transport of glucose and amino acids intracellularly. It also promotes anabolism, and inhibits protein catabolism. In the liver, insulin promotes the uptake and storage of glucose in the form of glycogen, inhibits gluconeogenesis, and promotes the conversion of excess glucose into fat. | Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism. | NA | Insulin is predominantly cleared by metabolic degradation via a receptor-mediated process. | NA | NA | NA | Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Cytochrome P-450 CYP1A2 Inducers,Cytochrome P-450 CYP1A2 Inducers (strength unknown),Cytochrome P-450 Enzyme Inducers,Drugs Used in Diabetes,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Insulin,Insulin, Short-Acting,Insulins and Analogues for Injection, Fast-Acting,Pancreatic Hormones,Peptide Hormones,Peptides,Protein Precursors,Proteins | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | Iletin II | Lilly | Lilly | NA | NA | 100 units/mL (U-100) | sterile suspension | Subcutaneous | NA | NA | NA | Link | NA | NA |
| 10873 | Th1233 | Pegloticase | >Th1233_Pegloticase TYKKNDEVEFVRTGYGKDMIKVLHIQRDGKYHSIKEVATTVQLTLSSKKDYLHGDNSDVIPTDTIKNTVNVLAKFKGIKSIETFAVTICEHFLSSFKHVIRAQVYVEEVPWKRFEKNGVKHVHAFIYTPTGTHFCEVEQIRNGPPVIHSGIKDLKVLKTTQSGFEGFIKDQFTTLPEVKDRCFATQVYCKWRYHQGRDVDFEATWDTVRSIVLQKFAGPYDKGEYSPSVQKTLYDIQVLTLGQVPEIEDMEISLPNIHYLNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLSSRL | 34192.85 | C1549H2430N408O448S8 | NA | NA | NA | Median: ~14 days | Pegloticase is a recombinant procine-like uricase drug indicated for the treatment of severe, treatment-refractory, chronic gout. Similarly to rasburicase, pegloticase metabolises the conversion of uric acid to allantoin. This reduces the risk of precipitate formation and development of gout, since allantoin is five to ten times more soluble than uric acid. In contrast to rasburicase, pegloticase is pegylated to increase its elimination half-life from about eight hours to ten or twelve days, and to decrease the immunogenicity of the foreign uricase protein. This modification allows for an application just once every two to four weeks, making this drug suitable for long-term treatment. | For the treatment of chronic gout in adult patients refractory to conventional therapy. | NA | Pegloticase is a recombinant uricase that catalyzes the metabolism of uric acid to allantoin. | Conditions that should be monitored for when starting treatment with pegloticase include anaphylaxis, infusion reactions, an increase in gout flares, and/or an exacerbation of pre-existing congestive heart failure. | NA | Approximately 24 hours following the first dose, mean plasma uric acid levels were 0.7 mg/dL. The duration of suppression of plasma uric acid appeared to be positively associated with pegloticase dose. Sustained decrease in plasma uric acid below the solubility concentration of 6 mg/dL for more than 300 hours was observed with doses of 8 mg and 12 mg. | NA | NA | Enzymes | NA | NA | NA | The risk or severity of adverse effects can be increased while combining Pegloticase with Allopurinol, Certolizumab pegol, Febuxostat, Pegademase bovine, Pegaptanib, Pegaspargase, Pegfilgrastim, Peginterferon alfa-2a, Peginterferon alfa-2b, Pegvisomant etc | Uric acid | Pegloticase (Krystexxa) | NA | NA | Treating chronic gout in certain patients | NA | NA | Solid | Intravenous | Gout: IV: 8 mg every 2 weeks | Hypersensitivity to the active substance | Chest pain or discomfort, cough, difficult or labored breathing, difficulty with swallowing, dizziness, facial swelling, fast heartbeat, fever or chills, flushing or redness of the skin, gout flare, headache, hives or welts, itching, or skin rash, nausea or vomiting, puffiness or swelling of the eyelids or around the eyes, face, lips, or tongue, redness of the skin, tightness in the chest, unusual tiredness or weakness, unusually warm skin | Link | NA | NA |
| 11018 | Th1241 | Asparaginase Escherichia coli | >Th1241_Asparaginase_Escherichia_coli MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | NA | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | Plasma half life of L-asparagine derived from _E. coli_ following intravenous injection was 8-30 hrs [FDA Label]. Plasma half-life was 34 to 49 hours after intramuscular injection [FDA Label]. Half-life (mean ± SD) of native _E. coli_ asparaginase is approximately 1.28 ± 0.35 days [A31999]. | Asparaginase derived from _Escherichia coli_ (L-asparagine amidohydrolase, EC 3.5.1.1) is an enzyme responsible for the metabolism of L-asparagine, by catalyzing L-asparagine into L-aspartic acid and ammonia. It also facilitates the production of oxaloacetate which is needed for general cellular metabolism. Asparaginase from _E. coli_ has clinically shown to exhibit antitumor actions in models of leukaemias [A31996, A31997]. L-asparaginase of _E. coli_ is marketed under several different trade names, including Elspar, for the treatment of acute lymphoblastic leukemia (ALL) as part of a multi-agent chemotherapeutic regimen. It is available as intramuscular or intravenous injections. Therapeutic L-asparaginase from _E. coli_ works by depleting the levels of non-essential amino acid, asparagine, in lymphoblastic leukemic cells thus promoting apoptotic cell death [A31999]. For patients who develop hypersensitivity to _E. coli_-derived formulations of L-asparaginase, the use of PEGylated or non-PEGylated [DB08886] is recommended [A31999]. | Indicated as a component of a multi-agent chemotherapeutic regimen for the treatment of patients with acute lymphoblastic leukemia (ALL) [FDA Label]. | In clinical trials of patients with previously untreated, standard-risk ALL, administration of asparaginase resulted in a decrease of plasma asparagine levels from average of 41 µM to less than 3 µM [FDA Label]. The native asparaginase in whom plasma enzyme activity before treatment was greater than 0.1 International Units/mL [FDA Label]. In this study, cerebrospinal fluid asparagine levels in patients treated with asparaginase decreased from 2.8 µM (pretreatment) to 1.0 µM and 0.3 µM at day 7 and day 28 of induction, respectively [FDA Label]. Native E. coli asparaginase results in asparagine depletion in 14 to 23 days following administration [A31999]. | Asparagine is a non-essential amino acid that maintains DNA, RNA and protein synthesis and promotes cell growth. While healthy and normal cells are capable of obtaining asparagine via dietary intake or synthesizing the asparagine from aspartate via asparagine synthetase activity, lymphoblastic leukemic cells lack the asparagine synthetase enzyme and cannot produce asparagine _de novo_ [A31999]. Thus, leukemic cells rely on exogenous source of asparagine for protein synthesis and cell survival [A31999]. L-asparagine from E. coli serves to deplete plasma levels of asparagine in leukemic cells by converting L-asparagine to L-aspartic acid and ammonia [A31999], leading to reduced reduced DNA, RNA and protein synthesis; inhibition of cell growth; and ultimately the activation of apoptotic cell-death mechanisms [A31999]. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase [FDA Label]. | No studies assessing the mutagenic or carcinogenic potential of _E. coli_ L-asparagine have been conducted. In the Ames assay, no mutagenic effect was demonstrated when tested against Salmonella typhimurium strains [FDA Label]. No studies have been performed on impairment of fertility [FDA Label]. Following a single, intravenous injection of 12,500 to 50,000 International Units L-asparagine/kg in rabbits, edema and necrosis of pancreatic islets were observed. The clinical relevance of this finding is unclear as it does not indicate pancreatitis [FDA Label]. | NA | In a study in patients with metastatic cancer and leukemia, daily intravenous administration of L-asparaginase derived from _E. coli_ resulted in a cumulative increase in plasma levels. Following intramuscular injection in patients with metastatic cancer and leukemia, peak plasma levels of asparaginase was achieved 14 to 24 hours post-dosing [FDA Label]. Peak asparaginase activity of native _E. coli_ asparaginase can be observed in 24 to 48 hours following administration [A31999]. | Apparent volume of distribution was slightly greater than the plasma volume. Asparaginase levels in cerebrospinal fluid were less than 1% of concurrent plasma levels [A31999]. | NA | Asparagine-specific Enzyme | NA | NA | NA | NA | L-asparagine | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11019 | Th1241 | Asparaginase Escherichia coli | >Th1241_Asparaginase_Escherichia_coli MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | NA | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | Plasma half life of L-asparagine derived from _E. coli_ following intravenous injection was 8-30 hrs [FDA Label]. Plasma half-life was 34 to 49 hours after intramuscular injection [FDA Label]. Half-life (mean ± SD) of native _E. coli_ asparaginase is approximately 1.28 ± 0.35 days [A31999]. | Asparaginase derived from _Escherichia coli_ (L-asparagine amidohydrolase, EC 3.5.1.1) is an enzyme responsible for the metabolism of L-asparagine, by catalyzing L-asparagine into L-aspartic acid and ammonia. It also facilitates the production of oxaloacetate which is needed for general cellular metabolism. Asparaginase from _E. coli_ has clinically shown to exhibit antitumor actions in models of leukaemias [A31996, A31997]. L-asparaginase of _E. coli_ is marketed under several different trade names, including Elspar, for the treatment of acute lymphoblastic leukemia (ALL) as part of a multi-agent chemotherapeutic regimen. It is available as intramuscular or intravenous injections. Therapeutic L-asparaginase from _E. coli_ works by depleting the levels of non-essential amino acid, asparagine, in lymphoblastic leukemic cells thus promoting apoptotic cell death [A31999]. For patients who develop hypersensitivity to _E. coli_-derived formulations of L-asparaginase, the use of PEGylated or non-PEGylated [DB08886] is recommended [A31999]. | Indicated as a component of a multi-agent chemotherapeutic regimen for the treatment of patients with acute lymphoblastic leukemia (ALL) [FDA Label]. | In clinical trials of patients with previously untreated, standard-risk ALL, administration of asparaginase resulted in a decrease of plasma asparagine levels from average of 41 µM to less than 3 µM [FDA Label]. The native asparaginase in whom plasma enzyme activity before treatment was greater than 0.1 International Units/mL [FDA Label]. In this study, cerebrospinal fluid asparagine levels in patients treated with asparaginase decreased from 2.8 µM (pretreatment) to 1.0 µM and 0.3 µM at day 7 and day 28 of induction, respectively [FDA Label]. Native E. coli asparaginase results in asparagine depletion in 14 to 23 days following administration [A31999]. | Asparagine is a non-essential amino acid that maintains DNA, RNA and protein synthesis and promotes cell growth. While healthy and normal cells are capable of obtaining asparagine via dietary intake or synthesizing the asparagine from aspartate via asparagine synthetase activity, lymphoblastic leukemic cells lack the asparagine synthetase enzyme and cannot produce asparagine _de novo_ [A31999]. Thus, leukemic cells rely on exogenous source of asparagine for protein synthesis and cell survival [A31999]. L-asparagine from E. coli serves to deplete plasma levels of asparagine in leukemic cells by converting L-asparagine to L-aspartic acid and ammonia [A31999], leading to reduced reduced DNA, RNA and protein synthesis; inhibition of cell growth; and ultimately the activation of apoptotic cell-death mechanisms [A31999]. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase [FDA Label]. | No studies assessing the mutagenic or carcinogenic potential of _E. coli_ L-asparagine have been conducted. In the Ames assay, no mutagenic effect was demonstrated when tested against Salmonella typhimurium strains [FDA Label]. No studies have been performed on impairment of fertility [FDA Label]. Following a single, intravenous injection of 12,500 to 50,000 International Units L-asparagine/kg in rabbits, edema and necrosis of pancreatic islets were observed. The clinical relevance of this finding is unclear as it does not indicate pancreatitis [FDA Label]. | NA | In a study in patients with metastatic cancer and leukemia, daily intravenous administration of L-asparaginase derived from _E. coli_ resulted in a cumulative increase in plasma levels. Following intramuscular injection in patients with metastatic cancer and leukemia, peak plasma levels of asparaginase was achieved 14 to 24 hours post-dosing [FDA Label]. Peak asparaginase activity of native _E. coli_ asparaginase can be observed in 24 to 48 hours following administration [A31999]. | Apparent volume of distribution was slightly greater than the plasma volume. Asparaginase levels in cerebrospinal fluid were less than 1% of concurrent plasma levels [A31999]. | NA | Enzymes | NA | NA | NA | NA | L-asparagine | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11020 | Th1241 | Asparaginase Escherichia coli | >Th1241_Asparaginase_Escherichia_coli MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | NA | C1377H2208N382O442S17 | 4.67 | 0.059 | NA | Plasma half life of L-asparagine derived from _E. coli_ following intravenous injection was 8-30 hrs [FDA Label]. Plasma half-life was 34 to 49 hours after intramuscular injection [FDA Label]. Half-life (mean ± SD) of native _E. coli_ asparaginase is approximately 1.28 ± 0.35 days [A31999]. | Asparaginase derived from _Escherichia coli_ (L-asparagine amidohydrolase, EC 3.5.1.1) is an enzyme responsible for the metabolism of L-asparagine, by catalyzing L-asparagine into L-aspartic acid and ammonia. It also facilitates the production of oxaloacetate which is needed for general cellular metabolism. Asparaginase from _E. coli_ has clinically shown to exhibit antitumor actions in models of leukaemias [A31996, A31997]. L-asparaginase of _E. coli_ is marketed under several different trade names, including Elspar, for the treatment of acute lymphoblastic leukemia (ALL) as part of a multi-agent chemotherapeutic regimen. It is available as intramuscular or intravenous injections. Therapeutic L-asparaginase from _E. coli_ works by depleting the levels of non-essential amino acid, asparagine, in lymphoblastic leukemic cells thus promoting apoptotic cell death [A31999]. For patients who develop hypersensitivity to _E. coli_-derived formulations of L-asparaginase, the use of PEGylated or non-PEGylated [DB08886] is recommended [A31999]. | Indicated as a component of a multi-agent chemotherapeutic regimen for the treatment of patients with acute lymphoblastic leukemia (ALL) [FDA Label]. | In clinical trials of patients with previously untreated, standard-risk ALL, administration of asparaginase resulted in a decrease of plasma asparagine levels from average of 41 µM to less than 3 µM [FDA Label]. The native asparaginase in whom plasma enzyme activity before treatment was greater than 0.1 International Units/mL [FDA Label]. In this study, cerebrospinal fluid asparagine levels in patients treated with asparaginase decreased from 2.8 µM (pretreatment) to 1.0 µM and 0.3 µM at day 7 and day 28 of induction, respectively [FDA Label]. Native E. coli asparaginase results in asparagine depletion in 14 to 23 days following administration [A31999]. | Asparagine is a non-essential amino acid that maintains DNA, RNA and protein synthesis and promotes cell growth. While healthy and normal cells are capable of obtaining asparagine via dietary intake or synthesizing the asparagine from aspartate via asparagine synthetase activity, lymphoblastic leukemic cells lack the asparagine synthetase enzyme and cannot produce asparagine _de novo_ [A31999]. Thus, leukemic cells rely on exogenous source of asparagine for protein synthesis and cell survival [A31999]. L-asparagine from E. coli serves to deplete plasma levels of asparagine in leukemic cells by converting L-asparagine to L-aspartic acid and ammonia [A31999], leading to reduced reduced DNA, RNA and protein synthesis; inhibition of cell growth; and ultimately the activation of apoptotic cell-death mechanisms [A31999]. Normal cells, however, are able to synthesize asparagine and thus are affected less by the rapid depletion produced by treatment with the enzyme asparaginase [FDA Label]. | No studies assessing the mutagenic or carcinogenic potential of _E. coli_ L-asparagine have been conducted. In the Ames assay, no mutagenic effect was demonstrated when tested against Salmonella typhimurium strains [FDA Label]. No studies have been performed on impairment of fertility [FDA Label]. Following a single, intravenous injection of 12,500 to 50,000 International Units L-asparagine/kg in rabbits, edema and necrosis of pancreatic islets were observed. The clinical relevance of this finding is unclear as it does not indicate pancreatitis [FDA Label]. | NA | In a study in patients with metastatic cancer and leukemia, daily intravenous administration of L-asparaginase derived from _E. coli_ resulted in a cumulative increase in plasma levels. Following intramuscular injection in patients with metastatic cancer and leukemia, peak plasma levels of asparaginase was achieved 14 to 24 hours post-dosing [FDA Label]. Peak asparaginase activity of native _E. coli_ asparaginase can be observed in 24 to 48 hours following administration [A31999]. | Apparent volume of distribution was slightly greater than the plasma volume. Asparaginase levels in cerebrospinal fluid were less than 1% of concurrent plasma levels [A31999]. | NA | Enzymes and Coenzymes | NA | NA | NA | NA | L-asparagine | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11240 | Th1244 | Insulin human | >Th1244_Insulin_human GIVEQCCTSICSLYQLENYCN | 5808 | C257H383N65O77S6 | NA | NA | 81 °C | Systemic insulin disposition (apparent terminal half-life) following oral inhalation of 4 to 48 units of human insulin was 120-206 minutes. | Human Insulin, also known as Regular Insulin, is a short-acting form of insulin used for the treatment of hyperglycemia caused by Type 1 and Type 2 Diabetes. Human insulin is produced by recombinant DNA technology and is identical to endogenously produced insulin. Typically prescribed for the management of diabetes mellitus, insulin is a peptide hormone produced by beta cells of the pancreas that promotes glucose metabolism. Insulin is released from the pancreas following a meal to promote the uptake of glucose from the blood into internal organs and tissues such as the liver, fat cells, and skeletal muscle. Absorption of glucose into cells allows for its transformation into glycogen or fat for storage. Insulin also inhibits hepatic glucose production, enhances protein synthesis, and inhibits lipolysis and proteolysis among many other functions. Insulin is an important treatment in the management of Type 1 Diabetes (T1D) which is caused by an autoimmune reaction that destroys the beta cells of the pancreas, resulting in the body not being able to produce or synthesize the insulin needed to manage circulating blood sugar levels. As a result, people with T1D rely primarily on exogenous forms of insulin to lower glucose levels in the blood. Insulin is also used in the treatment of Type 2 Diabetes (T2D), another form of diabetes mellitus that is a slowly progressing metabolic disorder caused by a combination of genetic and lifestyle factors that promote chronically elevated blood sugar levels. Without treatment or improvement in non-pharmacological measures such as diet and exercise to lower blood glucose, high blood sugar eventually causes cellular resistance to endogenous insulin, and in the long term, damage to pancreatic islet cells. Insulin is typically prescribed later in the course of T2D, after trying several oral medications such as [DB00331], [DB01120], or [DB01261] have been tried, when sufficient damage has been caused to pancreatic cells that the body is no longer able to produce insulin on its own. Marketed as the brand name product Humulin R or Novolin R, human insulin begins to exert its effects within 30 minutes of subcutaneous administration, while peak levels occur 3-4 hours after administration. Due to its quick onset of action, human insulin is considered "bolus insulin" as it provides high levels of insulin in a short period of time to mimic the release of endogenous insulin from the pancreas after meals. Bolus insulin is often combined with once daily, long-acting "basal insulin" such as [DB01307], [DB09564], and [DB00047] to provide low concentrations of background insulin that can keep blood sugar stable between meals or overnight. Use of basal and bolus insulin together is intended to mimic the pancreas' production of endogenous insulin, with a goal of avoiding any periods of hypoglycemia. Human insulin is also available in an inhalable form, intended to be used as a bolus meal-time insulin. Exubera was the first inhaled insulin available on the market and was developed by Inhale Therapeutics (later named Nektar Therapeutics). Unfortunately, limited uptake by physicians and patients, poor sales, bulky packaging, and concerns over the possible impact on lung cancer development resulted in Exubera products being withdrawn from the US markets [A176005]. Exubera was followed by Afrezza, a monomeric inhaled insulin developed by Mannkind Corporation, which received FDA approval in 2016. While still available in the US, Afrezza has had similar concerns associated with its use, and had an FDA "black box" warning added to it to warn about use in patients with chronic lung disease. Afrezza does not currently have Health Canada or European Medicines Agency approval for marketing in Canada or the EU. Human Insulin is a 51 residue peptide hormone produced by recombinant DNA technology by inserting the human insulin gene into Escherichia coli bacteria or Saccharomyces cerevisiae. The structure is identical to native human insulin, with two amino acid chains covalently linked by disulfide bonds. Human insulin is also available in an intermediate-acting form as NPH (Neutral Protamine Hagedorn) as the marketed products Novolin N and Humulin N. NPH insulin is provided as a crystalline suspension of insulin with protamine and zinc, resulting in an onset of action in 1 to 3 hours, duration of action up to 24 hours, and peak action from 6 to 8 hours. Due to the added crystals, NPH insulin is typically cloudy when compared to other forms of insulin and has a neutral pH. Without an adequate supply of insulin to promote absorption of glucose from the bloodstream, blood sugar levels can climb to dangerously high levels and can result in symptoms such as fatigue, headache, blurred vision, and increased thirst. If left untreated, the body starts to break down fat, instead of glucose, for energy which results in a build-up of ketone acids in the blood and a syndrome called ketoacidosis, which is a life-threatening medical emergency. In the long term, elevated blood sugar levels increase the risk of heart attack, stroke, and diabetic neuropathy. | Human insulin is indicated to improve glycemic control in adults and pediatric patients with diabetes mellitus. | Insulin is a natural hormone produced by beta cells of the pancreas. In non-diabetic individuals, a basal level of insulin is supplemented with insulin spikes following meals. Postprandial insulin spikes are responsible for the metabolic changes that occur as the body transitions from a postabsorptive to absorptive state. Insulin promotes cellular uptake of glucose, particularly in muscle and adipose tissues, promotes energy storage via glycogenesis, opposes catabolism of energy stores, increases DNA replication and protein synthesis by stimulating amino acid uptake by liver, muscle and adipose tissue, and modifies the activity of numerous enzymes involved in glycogen synthesis and glycolysis. Insulin also promotes growth and is required for the actions of growth hormone (e.g. protein synthesis, cell division, DNA synthesis). | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. | NA | The metabolism and elimination of orally inhaled human insulin are comparable to regular human insulin. | When injected subcutaneously, the glucose-lowering effect of human insulin begins approximately 30 minutes post-dose. After a single subcutaneous administration of 0.1 unit/kg of human insulin to healthy subjects, peak insulin concentrations occurred between 1.5 to 2.5 hours post-dose. When administered in an inhaled form (as the product Afrezza), the time to maximum serum insulin concentration ranges from 10-20 minutes after oral inhalation of 4 to 48 units of human insulin. Serum insulin concentrations declined to baseline by approximately 60-240 minutes for these dose levels. Intrapatient variability in insulin exposure measured by AUC and Cmax is approximately 16% (95% CI 12-23%) and 21% (95% CI 16-30%), respectively. | NA | NA | Cytochrome P-450 Enzyme Inducers | 6546929 | 15-04-2003 | 14-05-2019 | NA | Insulin receptor,Insulin-like growth factor 1 receptor,Carboxypeptidase E,Protein NOV homolog,Low-density lipoprotein receptor-related protein 2,Insulin-like growth factor-binding protein 7 | Actraphane 40 Penfill | Novo Nordisk | Novo Nordisk | Subcutaneous | 100 iu/ml | NA | The most common side effect with Actraphane (seen in more than 1 patient in 10) is hypoglycaemia (low blood glucose levels). | Actraphane is a suspension for injection that contains the active substance human insulin. It is available as vials, cartridges (Penfill) or prefilled pens (InnoLet or FlexPen). Actraphane contains both fast-acting (soluble) and long-acting (isophane) insulin: Actraphane 30: soluble insulin 30% and isophane insulin 70%; Actraphane 40: soluble insulin 40% and isophane insulin 60%; Actraphane 50: soluble insulin 50% and isophane insulin 50%. | Actraphane is used to treat diabetes. | NA | NA | Link | Link | NA |
| 11378 | Th1245 | Interferon alfa-2a | >Th1245_Interferon_alfa-2a CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 19241.1 | C860H1353N227O255S9 | 5.99 | -0.336 | NA | The IM half-life of interferon alfa-2a is 6 hours to 8 hours; the half-life for IV infusion is 3.7 hours to 8.5 hours (mean 5.1 hours). | Interferon a (human leukocyte protein moiety reduced). A type I interferon consisting of 165 amino acid residues with lysine in position 23. This protein is produced by recombinant DNA technology and resembles interferon secreted by leukocytes. It is used extensively as an antiviral or antineoplastic agent. An oral form is being developed by Amarillo Biosciences. | For the treatment of chronic hepatitis C, hairy cell leukemia, AIDS-related Kaposi's sarcoma, and chronic myelogenous leukemia. Also for the treatment of oral warts arising from HIV infection. | Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. | Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription)which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. | Interferon alfa-2 may cause serious adverse effects such as anemia; autoimmune diseases, including vasculitis, arthritis, hemolytic anemia, and erythematosus syndrome; cardiotoxicity; hepatotoxicity; hyperthyroidism or hypothyroidism; transient ischemic attacks; leukopenia; neurotoxicity; peripheral neuropathy; and thrombocytopenia. Some lesser side effects that may not need medical attention include blurred vision, change in taste or metallic taste, cold sores or stomatitis, diarrhea, dizziness, dry mouth, dry skin or itching, flu-like syndrome, increased sweating, leg cramps, loss of appetite, nausea or vomiting, skin rash, unusual tiredness, weight loss, and partial loss of hair. | NA | Absorption is high (greater than 80%) when administered intramuscularly or subcutaneously. | * 0.223 to 0.748 L/kg [healthy people] | * 2.14 - 3.62 mL/min/kg [healthy] | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | Interferon alpha/beta receptor 1,Interferon alpha/beta receptor 2 | Roferon-A | Genentech, Inc. | Genentech, Inc. | Subcutaneous | 33.3 ug/0.5mL | Roferon-A (interferon alfa-2a, recombinant) is contraindicated in patients with: Hypersensitivity to Roferon-A (interferon alfa-2a, recombinant) or any of its components Autoimmune hepatitis Hepatic decompensation (Child-Pugh class B and C) before or during treatment Roferon-A (interferon alfa-2a, recombinant) is contraindicated in neonates and infants because it contains benzyl alcohol. Benzyl alcohol is associated with an increased incidence of neurologic and other complications in neonates and infants, which are sometimes fatal. | lu like symptoms such as fatigue (58% to 95%), fever (25% to 92%), myalgia (68% to 71%), headache (44% to 66%), chills (23% to 64%), arthralgia/bone pain (25% to 47%), asthenia (6%), sweating (5%), leg cramps (3%), and malaise (1%). Weight loss (25% to 33%), change in taste or smell (3% to 25%), pain (24%), back pain (16%), night sweats (8%), menstrual irregularity (4%), reversible hearing loss, and tinnitus have also been reported | Alpheon is a solution for injection that contains the active substance interferon alfa-2a. | Roferon-A (interferon alfa-2a, recombinant) is indicated for the treatment of chronic hepatitis C and hairy cell leukemia in patients 18 years of age or older. In addition, it is indicated for chronic phase, Philadelphia chromosome (Ph) positive chronic myelogenous leukemia (CML) patients who are minimally pretreated (within 1 year of diagnosis). | NA | NA | Link | Link | NA |
| 11393 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Enzyme Precursors | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase RT | Novo Nordisk | Novo Nordisk | Intravenous | 8 mg / vial | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11394 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Enzymes | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Novoseven | Novo Nordisk | Novo Nordisk | Intravenous | 50 KIU | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | fever, headache, injection site reactions (pain, redness, or irritation), dizziness, nausea, or vomiting. | NovoSeven RT with MixPro is a man-made protein similar to a natural protein in the body that helps the blood to clot. NovoSeven RT with MixPro is used to treat or prevent bleeding in people with hemophilia A or hemophilia B, or factor VII deficiency. NovoSeven RT with MixPro may also be used for purposes... | NovoSeven (coagulation factor viia (recombinant)) is indicated for: | NA | REFERENCES | Link | Link | NA |
| 11395 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Enzymes and Coenzymes | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Novoseven | Novo Nordisk | Novo Nordisk | Intravenous | 100 KIU | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | fever, headache, injection site reactions (pain, redness, or irritation), dizziness, nausea, or vomiting. | NovoSeven RT with MixPro is a man-made protein similar to a natural protein in the body that helps the blood to clot. NovoSeven RT with MixPro is used to treat or prevent bleeding in people with hemophilia A or hemophilia B, or factor VII deficiency. NovoSeven RT with MixPro may also be used for purposes... | NovoSeven (coagulation factor viia (recombinant)) is indicated for: | NA | REFERENCES | Link | Link | NA |
| 11433 | Th1248 | Collagenase clostridium histolyticum | >Th1248_Collagenase_clostridium_histolyticum MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.35-6.20 | -0.714 | 49-54 | NA | Collagenase clostridium histolyticum is an enzyme produced by the bacterium Clostridium histolyticum. It is beneficial in the breakdown of collagen plaques for the treatment of Dupuytren's contracture and Peyronie's disease.[L14882] The topical formulation is used for the debridement of necrotic tissue due to burns or chronic ulcers.[L14912] On July 6, 2020 a combination of injectable bacterial collagenases was approved by the FDA for the treatment of cellulite in adult women.[L14872] Also known as Qwo, this injection is the first approved injectable treatment for cellulite and was developed by Endo International.[L14892] | Collagenase clostridium histolyticum is indicated for the treatment of adults with Dupuytren's contracture with a palpable cord. Additionally, it is used to treat men with Peyronie's disease diagnosed with a penile curvature deformity of at least a 30-degree angle at the beginning of therapy in addition to palpable plaques.[L14882] Collagenase ointment is used for the tissue debridement of chronic dermal ulcers and severely burned tissues.[L14952] The combination collagenase product, also known as Qwo, is used for the treatment of moderate to severe cellulite in the buttocks of adult women.[L14872] | Collagenase digests collagen, treating conditions such as Peyronie's disease, cellulite, chronic ulcers, burns, and contractures.[L14872,L14882,L14912] | Peyronie's disease is a fibrous lesion of the tunica albuginea in the penile tissues.[A215067] Cellulite is a multifactorial condition resulting in the accumulation of fibrotic dermal septae and the expansion of subcutaneous fat.[A215062] Dupuytren's contracture is a fibroproliferative disease that results in the fibrous deposition of collagen in the hands, limiting mobility and functionality of the hands.[A215072] The collagen deposition in the abovementioned conditions is the target of collagenase enzyme therapy.[A215157,A215167] These enzymes are proteinases acting to hydrolyze collagen's triple-helical conformation, resulting in the lysis of collagen deposits and relief from the necrotic tissue and plaques associated with several conditions.[L14882,L14912] On a molecular level, collagenases cleave polypeptide chains that make up the collagen triple helix structure at various loci, leading to solubilization from the collagen fibril.[A215197] | No clinical reaction has been attributed to an overdose of collagenase in clinical trials.[L14912] If required, the collagenase enzymes can be inactivated with a povidone-iodine wash.[L14912] | No formal systemic metabolism studies have been performed with collagenase histolyticum.[A215277] | There is currently limited readily available regarding the absorption of collagenase through the skin.[L14912] In a pharmacokinetic study, the serum concentrations of clostridium type I collagenase (AUX-I) and clostridium type II collagenase (AUX-II) were measured. Both were detected under the lower limit of quantitation of 5 ng/mL and 25 ng/mL, respectively, in volunteers administered one dose of the collagenase histolyticum combination product, Qwo, at a dose of up to 3.36 mg in a maximum of 4 body areas.[L14872] | NA | NA | Collagen-specific Enzyme | NA | NA | NA | Bivalirudin,Abciximab,Dicoumarol,Argatroban,Ardeparin,Phenindione,Fondaparinux,Warfarin,Pentosan polysulfate,Phenprocoumon,Edetic acid,Heparin,Enoxaparin,Acenocoumarol,Ximelagatran,Ancrod,Rivaroxaban,Sulodexide,Idraparinux,Apixaban,Otamixaban,Dabigatran etexilate,Danaparoid,Dalteparin,Ferulic acid,Ethyl biscoumacetate,Nadroparin,Edoxaban,Dextran,Desirudin,Protocatechualdehyde,Protein C,Antithrombin III human,Letaxaban,Darexaban,Nafamostat,Gabexate,Troxerutin,Fluindione,Protein S human,Melagatran,Potassium citrate,Sodium citrate,Tenecteplase,Drotrecogin alfa,Defibrotide,Tinzaparin,Brinase,Saruplase,Streptokinase,Desmoteplase,Fibrinolysin,Astaxanthin,Urokinase,Dipyridamole,Epoprostenol,Beraprost,Prasugrel,Cangrelor,Triflusal,Ticagrelor,Ditazole,Vorapaxar,Bemiparin,Parnaparin,Clorindione,Diphenadione,Tioclomarol,Lepirudin,Alteplase,Reteplase,Anistreplase,Tocopherylquinone,Amediplase,4-hydroxycoumarin,(R)-warfarin,(S)-Warfarin,Betrixaban,Edetate calcium disodium anhydrous,Zinc citrate,Antithrombin Alfa,Coumarin,Dabigatran,Semuloparin,Monteplase,Reviparin,Dermatan sulfate,SR-123781A,Dociparstat sodium,Doxycycline,Lymecycline,Clomocycline,Tigecycline,Oxytetracycline,Demeclocycline,Tetracycline,Metacycline,Minocycline,Rolitetracycline,Chlortetracycline,Sarecycline,Eravacycline,Omadacycline,Meclocycline,Penimepicycline | Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain | Collagenase Santyl | Healthpoint | Healthpoint | Topical | 250 [arb'U]/1g | Collagenase Santyl® Ointment is contraindicated in patients who have shown local or systemic hypersensitivity to collagenase. | No allergic sensitivity or toxic reactions have been noted in clinical use when used as directed. However, one case of systemic manifestations of hypersensitivity to collagenase in a patient treated for more than one year with a combination of collagenase and cortisone has been reported. | NA | NA | NA | NA | Link | Link | NA |
| 11437 | Th1248 | Collagenase clostridium histolyticum | >Th1248_Collagenase_clostridium_histolyticum MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.35-6.20 | -0.714 | 49-54 | NA | Collagenase clostridium histolyticum is an enzyme produced by the bacterium Clostridium histolyticum. It is beneficial in the breakdown of collagen plaques for the treatment of Dupuytren's contracture and Peyronie's disease.[L14882] The topical formulation is used for the debridement of necrotic tissue due to burns or chronic ulcers.[L14912] On July 6, 2020 a combination of injectable bacterial collagenases was approved by the FDA for the treatment of cellulite in adult women.[L14872] Also known as Qwo, this injection is the first approved injectable treatment for cellulite and was developed by Endo International.[L14892] | Collagenase clostridium histolyticum is indicated for the treatment of adults with Dupuytren's contracture with a palpable cord. Additionally, it is used to treat men with Peyronie's disease diagnosed with a penile curvature deformity of at least a 30-degree angle at the beginning of therapy in addition to palpable plaques.[L14882] Collagenase ointment is used for the tissue debridement of chronic dermal ulcers and severely burned tissues.[L14952] The combination collagenase product, also known as Qwo, is used for the treatment of moderate to severe cellulite in the buttocks of adult women.[L14872] | Collagenase digests collagen, treating conditions such as Peyronie's disease, cellulite, chronic ulcers, burns, and contractures.[L14872,L14882,L14912] | Peyronie's disease is a fibrous lesion of the tunica albuginea in the penile tissues.[A215067] Cellulite is a multifactorial condition resulting in the accumulation of fibrotic dermal septae and the expansion of subcutaneous fat.[A215062] Dupuytren's contracture is a fibroproliferative disease that results in the fibrous deposition of collagen in the hands, limiting mobility and functionality of the hands.[A215072] The collagen deposition in the abovementioned conditions is the target of collagenase enzyme therapy.[A215157,A215167] These enzymes are proteinases acting to hydrolyze collagen's triple-helical conformation, resulting in the lysis of collagen deposits and relief from the necrotic tissue and plaques associated with several conditions.[L14882,L14912] On a molecular level, collagenases cleave polypeptide chains that make up the collagen triple helix structure at various loci, leading to solubilization from the collagen fibril.[A215197] | No clinical reaction has been attributed to an overdose of collagenase in clinical trials.[L14912] If required, the collagenase enzymes can be inactivated with a povidone-iodine wash.[L14912] | No formal systemic metabolism studies have been performed with collagenase histolyticum.[A215277] | There is currently limited readily available regarding the absorption of collagenase through the skin.[L14912] In a pharmacokinetic study, the serum concentrations of clostridium type I collagenase (AUX-I) and clostridium type II collagenase (AUX-II) were measured. Both were detected under the lower limit of quantitation of 5 ng/mL and 25 ng/mL, respectively, in volunteers administered one dose of the collagenase histolyticum combination product, Qwo, at a dose of up to 3.36 mg in a maximum of 4 body areas.[L14872] | NA | NA | Enzymes | NA | NA | NA | NA | Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain | Santyl | Smith & Nephew, Inc. | Smith & Nephew, Inc. | Topical | 250 unit / g | Collagenase Santyl® Ointment is contraindicated in patients who have shown local or systemic hypersensitivity to collagenase. | pain or a burning feeling at the affected area, or temporary redness or irritation in the skin around the affected area. Treatment of burns and skin ulcers by breaking up and removing dead skin and tissue may infrequently increase the risk for serious infection (sepsis) and may be a side effect of Santyl. | Santyl (for the skin) is used to treat severe burns or skin ulcers in adults. Santyl helps remove dead skin tissue and aid in wound healing. Santyl may also be used for purposes not listed in this medication guide. Warnings Use only as directed. Tell your doctor if you use other medicines or have other... | Santyl is a prescription medicine used to treat the symptoms of Dermal Ulcers. Santyl may be used alone or with other medications. | NA | Collagenase Santyl® Ointment is a sterile enzymatic debriding ointment which contains 250 collagenase units per gram of white petrolatum USP. The enzyme collagenase is derived from the fermentation by Clostridium histolyticum. It possesses the unique ability to digest collagen in necrotic tissue. | Link | Link | NA |
| 11438 | Th1248 | Collagenase clostridium histolyticum | >Th1248_Collagenase_clostridium_histolyticum MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTVSYLKTLNYYDLVDLLVKTEIENLPDLFQYSSDAKEFYGNKTRMSFIMDEIGRRAPQYTEIDHKGIPTLVEVVRAGFYLGFHNKELNEINKRSFKERVIPSILAIQKNPNFKLGTEVQDKIVSATGLLAGNETAPPEVVNNFTPILQDCIKNIDRYALDDLKSKALFNVLAAPTYDITEYLRATKEKPENTPWYGKIDGFINELKKLALYGKINDNNSWIIDNGIYHIAPLGKLHSNNKIGIETLTEVMKVYPYLSMQHLQSADQIKRHYDSKDAEGNKIPLDKFKKEGKEKYCPKTYTFDDGKVIIKAGARVEEEKVKRLYWASKEVNSQFFRVYGIDKPLEEGNPDDILTMVIYNSPEEYKLNSVLYGYDTNNGGMYIEPEGTFFTYEREAQESTYTLEELFRHEYTHYLQGRYAVPGQWGRTKLYDNDRLTWYEEGGAELFAGSTRTSGILPRKSIVSNIHNTTRNNRYKLSDTVHSKYGASFEFYNYACMFMDYMYNKDMGILNKLNDLAKNNDVDGYDNYIRDLSSNYALNDKYQDHMQERIDNYENLTVPFVADDYLVRHAYKNPNEIYSEISEVAKLKDAKSEVKKSQYFSTFTLRGSYTGGASKGKLEDQKAMNKFIDDSLKKLDTYSWSGYKTLTAYFTNYKVDSSNRVTYDVVFHGYLPNEGDSKNSLPYGKINGTYKGTEKEKIKFSSEGSFDPDGKIVSYEWDFGDGNKSNEENPEHSYDKVGTYTVKLKVTDDKGESSVSTTTAEIKDLSENKLPVIYMHVPKSGALNQKVVFYGKGTYDPDGSIAGYQWDFGDGSDFSSEQNPSHVYTKKGEYTVTLRVMDSSGQMSEKTMKIKITDPVYPIGTEKEPNNSKETASGPIVPGIPVSGTIENTSDQDYFYFDVITPGEVKIDINKLGYGGATWVVYDENNNAVSYATDDGQNLSGKFKADKPGRYYIHLYMFNGSYMPYRINIEGSVGR | 112023.2 | C5028H7666N1300O1564S21 | 5.35-6.20 | -0.714 | 49-54 | NA | Collagenase clostridium histolyticum is an enzyme produced by the bacterium Clostridium histolyticum. It is beneficial in the breakdown of collagen plaques for the treatment of Dupuytren's contracture and Peyronie's disease.[L14882] The topical formulation is used for the debridement of necrotic tissue due to burns or chronic ulcers.[L14912] On July 6, 2020 a combination of injectable bacterial collagenases was approved by the FDA for the treatment of cellulite in adult women.[L14872] Also known as Qwo, this injection is the first approved injectable treatment for cellulite and was developed by Endo International.[L14892] | Collagenase clostridium histolyticum is indicated for the treatment of adults with Dupuytren's contracture with a palpable cord. Additionally, it is used to treat men with Peyronie's disease diagnosed with a penile curvature deformity of at least a 30-degree angle at the beginning of therapy in addition to palpable plaques.[L14882] Collagenase ointment is used for the tissue debridement of chronic dermal ulcers and severely burned tissues.[L14952] The combination collagenase product, also known as Qwo, is used for the treatment of moderate to severe cellulite in the buttocks of adult women.[L14872] | Collagenase digests collagen, treating conditions such as Peyronie's disease, cellulite, chronic ulcers, burns, and contractures.[L14872,L14882,L14912] | Peyronie's disease is a fibrous lesion of the tunica albuginea in the penile tissues.[A215067] Cellulite is a multifactorial condition resulting in the accumulation of fibrotic dermal septae and the expansion of subcutaneous fat.[A215062] Dupuytren's contracture is a fibroproliferative disease that results in the fibrous deposition of collagen in the hands, limiting mobility and functionality of the hands.[A215072] The collagen deposition in the abovementioned conditions is the target of collagenase enzyme therapy.[A215157,A215167] These enzymes are proteinases acting to hydrolyze collagen's triple-helical conformation, resulting in the lysis of collagen deposits and relief from the necrotic tissue and plaques associated with several conditions.[L14882,L14912] On a molecular level, collagenases cleave polypeptide chains that make up the collagen triple helix structure at various loci, leading to solubilization from the collagen fibril.[A215197] | No clinical reaction has been attributed to an overdose of collagenase in clinical trials.[L14912] If required, the collagenase enzymes can be inactivated with a povidone-iodine wash.[L14912] | No formal systemic metabolism studies have been performed with collagenase histolyticum.[A215277] | There is currently limited readily available regarding the absorption of collagenase through the skin.[L14912] In a pharmacokinetic study, the serum concentrations of clostridium type I collagenase (AUX-I) and clostridium type II collagenase (AUX-II) were measured. Both were detected under the lower limit of quantitation of 5 ng/mL and 25 ng/mL, respectively, in volunteers administered one dose of the collagenase histolyticum combination product, Qwo, at a dose of up to 3.36 mg in a maximum of 4 body areas.[L14872] | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain | Xiaflex | Endo Pharmaceuticals Inc. | Endo Pharmaceuticals Inc. | Intralesional | 0.9 mg/1 | XIAFLEX is contraindicated in: the treatment of Peyronie’s plaques that involve the penile urethra due to potential risk to this structure. patients with a history of hypersensitivity to XIAFLEX or to collagenase used in any other therapeutic application or application method [see WARNINGS AND PRECAUTIONS]. | mild pain or tenderness in the treated hand, cracked skin, underarm pain, tendon or ligament damage, nerve injury, and allergic reactions | Xiaflex is made from a mixture of proteins derived from a certain bacteria. Xiaflex is used to treat Dupuytren's contracture in adults. This condition causes an abnormal thickening of the tissue in the palm of the hand. This condition may get worse over time and form a "cord" in your palm, causing a... | Xiaflex is a prescription medicine used to treat the symptoms of Dupuytren Contracture and Peyronie Disease. Xiaflex may be used alone or with other medications. | NA | XIAFLEX contains purified collagenase clostridium histolyticum, consisting of two microbial collagenases in a defined mass ratio, Collagenase AUX-I and Collagenase AUX-II, which are isolated and purified from the fermentation of Clostridium histolyticum bacteria. | Link | Link | NA |
| 11455 | Th1249 | Somatotropin | >Th1249_Somatotropin FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | 22129 | C990H1532N262O300S7 | 5.27 | -0.411 | 76 °C at pH 3.5 | When somatotropin was administered subcutaneously at the dose of 0.024 mg/kg or 3 IU/m2, the mean apparent terminal half-life was Following intravenous infusion of 33 ng/kg/min of somatotropin in patients with growth hormone deficiency, the terminal elimination half-life was approximately 21.1 (±5.1) minutes.[L10971] | Human growth hormone (HGH), also known as somatotropin, is a peptide hormone that is synthesized and secreted by the somatotropic cells of the anterior pituitary gland.[A228183] Growth hormone plays an essential role in growth regulation during childhood as well as other basal metabolic functions, muscle and fat mass regulation, blood glucose level regulation, and lipid regulation in both children and adults.[A228183, L31508] Synthesized in a strain of _Escherichia coli_, recombinant HGH is a polypeptide hormone that contains 191 amino acid residues with a molecular weight of 22 kDa. It has an identical primary protein structure to endogenous human growth hormone.[A228188] Recombinant HGH has been commercially available since 1985 after its development by Genentech. [Somatrem] was the first available recombinant HGH and was largely replaced by somatropin, another form of recombinant HGH.[A228183] Growth hormone therapy is approved for various disorders of growth hormone deficiency, growth failure, or short stature including Turner syndrome, chronic renal insufficiency before transplantation, Prader-Willi syndrome, a history of fetal growth restriction, short stature homeobox (SHOX) haploinsufficiency, Noonan syndrome, idiopathic short stature, and adult- or childhood-onset growth hormone deficiency.[A228188] Recombinant growth hormone is available as a subcutaneous injection for children and adults under a wide variety of brand names. | Somatotropin is indicated for the treatment of pediatric patients who have growth failure due to an inadequate secretion of endogenous growth hormone, short stature associated with Turner syndrome, Prader-Willi syndrome (PWS), idiopathic short stature (ISS), short stature or growth failure in short stature homeobox-containing gene (SHOX) deficiency, and short stature born small for gestational age (SGA).[L31513, L31518] It is indicated for the treatment of growth failure in children associated with chronic kidney disease up to the time of renal transplantation.[L31523] It is also indicated for adults with adult-onset growth hormone deficiency, either alone or associated with multiple hormone deficiencies (hypopituitarism), as a result of pituitary disease, hypothalamic disease, surgery, radiation therapy, or trauma. It is also used to treat childhood-onset growth hormone deficiency in adults due to congenital, genetic, acquired, or idiopathic causes.[L31518] Somatotropin is indicated for the treatment of wasting or cachexia in patients with human immunodeficiency virus (HIV) who are receiving antiretroviral therapy to increase lean body mass and body weight and improve physical endurance.[L31498] Somatotropin is indicated for the treatment of short bowel syndrome in adult patients receiving specialized nutritional support.[L31493] | Somatotropin induces growth in nearly every tissue and organ in the body.[L31508] It stimulates linear growth and cartilaginous growth of long bones. In children with short stature, growth hormone increases both the number and size of muscle cells. It also promotes the growth of internal organs, and it also increases red cell mass. By promoting nitrogen retention, growth hormone increases cellular protein synthesis. Growth hormone also retains potassium and phosphorus in the serum, which may be the result of cell growth. Growth hormone stimulates the synthesis of chondroitin sulfate and collagen and increases the urinary excretion of hydroxyproline. It has negligible effects on serum calcium levels. Although increased calcium excretion in the urine is observed, calcium absorption from the intestine is simultaneously enhanced.[L10971] In end-stage renal disease, growth hormone was shown to improve several nutritional parameters, such as increases in serum insulin-like growth factor-I (IGF-I), serum albumin, and transferrin, as well as a reduction in blood urea nitrogen.[A228403] The metabolic effects of growth hormone are caused by the upregulation of insulin-like growth factor-1. Generally, growth hormone leads cells to enter an anabolic protein state with increased amino acid uptake, protein synthesis, and decreased catabolism of proteins.[L31508] The diabetogenic effect of larger doses of growth hormone is well documented in the literature: somatotropin antagonizes insulin action _in vivo_, causing insulin resistance and glucose intolerance. It increases glucose production through gluconeogenesis and glycogenolysis from the liver and kidney [A228398] and suppresses glucose uptake in the adipose tissue.[A228388] In mice, growth hormone increased mRNA expression of 2 major gluconeogenic genes, phosphoenolpyruvate carboxy-kinase and glucose-6-phosphatase.[A228398] The risk for impaired glucose tolerance and reduced insulin sensitivity may be increased in susceptible patients, especially in those with risk factors for diabetes mellitus, such as obesity, Turner syndrome, or a family history of diabetes mellitus. The development of new-onset type 2 Diabetes Mellitus was observed in patients receiving somatotropin treatment.[L10971] Growth hormone stimulates lipolysis via activation of the hormone-sensitive lipase in the adipose tissue, thereby increasing circulating levels of free fatty acids and triglycerides in the plasma. It also leads to a reduction of fat stores and decreased serum levels of low-density lipoprotein (LDL) cholesterol.[L10971] In contrast to the effects seen in the adipose tissue, growth hormone promotes cellular uptake of free fatty acids in skeletal muscle by increasing the activity of lipoprotein lipase. Growth hormone may cause hyperinsulinism following beta-cell compensation for insulin resistance; however, there is some evidence that growth hormone directly promotes beta-cell proliferation and glucose-stimulated insulin secretion.[A228398] | In conditions of growth failure, growth hormone deficiency, low body mass, and malnutrition, somatotropin treatment acts to mimic and restore the actions of endogenous growth hormone of stimulating linear bone growth, increasing bone mass, increasing muscle and reduced fat mass, and regulating blood glucose and lipid levels.[A228183] Somatotropin mediates its effects both directly by somatotropin and indirectly by insulin-like growth factor-1 (IGF-1), which is upregulated by growth hormone. It binds to the human growth hormone receptor (GHR), which is a dimeric receptor expressed in target cells in the liver and cartilage.[L10971] Upon binding of growth hormone, GHR dimerizes and interacts with Janus kinase 2 (JAK2), subsequently leading to tyrosine phosphorylation of JAK2 and the GH receptor. The signal transducer activator of transcription (STAT) pathway is initiated, where transcription factors such as STAT1, STAT3, and STAT5 are translocated into the nucleus to stimulate target gene transcription.[L31508] At the epiphysis or growth plate, growth hormone increases linear growth by promoting differentiation of prechondrocytes and expansion of osteoblasts. Growth hormone binding to its receptor in the liver and cartilage promotes the production of IGF-1, which acts on type 1 IGF receptors to also stimulate linear growth. In the liver, activated growth hormone receptor signalling leads to increased production of IGF binding protein-3 (IGFBP-3) and acid-labile subunit (ALS), which are proteins that bind to IGF-1 in a ternary complex to increase its half-life.[A228183] | The oral LD50 is 242 mg/kg in rats and 828 mg/kg in mice. The inhalatory LD50 is 710 mg/m3 and dermal LD50 is 1100 mg/kg in rats. The intraperitoneal LD50 in mice is 828 mg/kg.[L31528] Hypoglycemia followed by hyperglycemia, possibly with fluid retention, can be observed in somatropin overdose. Long-term or excessive use of growth hormone can lead to the signs and symptoms of gigantism and acromegaly.[L10971] | Information is unavailable. | When somatotropin was administered subcutaneously at the dose of 0.024 mg/kg or 3 IU/m2, the Cmax ranged from 13.8 (±5.8) to 17.1 (±10.0) ng/mL and the Tmax was four to five hours. Following intravenous infusion of 33 ng/kg/min of somatotropin in patients with growth hormone deficiency, the mean steady-state serum levels of approximately 23.1 (±15.0) ng/mL were reached at 150 minutes.[L10971] | NA | NA | Cytochrome P-450 Enzyme Inducers | 8920383 | 30-12-2014 | 17-01-2027 | NA | Growth hormone receptor,Prolactin receptor | Genotropin | Pharmacia and Upjohn Company LLC | Pharmacia and Upjohn Company LLC | Subcutaneous | 0.4 mg/0.25mL | Acute Critical Illness Treatment with pharmacologic amounts of somatropin is contraindicated in patients with acute critical illness due to complications following open heart surgery, abdominal surgery or multiple accidental trauma, or those with acute respiratory failure [see WARNINGS AND PRECAUTIONS]. Prader-Willi Syndrome In Children Somatropin is contraindicated in patients with Prader-Willi syndrome who are severely obese, have a history of upper airway obstruction or sleep apnea, or have severe respiratory impairment. There have been reports of sudden death when somatropin was used in such patients [see WARNINGS AND PRECAUTIONS]. Active Malignancy In general, somatropin is contraindicated in the presence of active malignancy. Any preexisting malignancy should be inactive and its treatment complete prior to instituting therapy with somatropin. Somatropin should be discontinued if there is evidence of recurrent activity. Since growth hormone deficiency may be an early sign of the presence of a pituitary tumor (or, rarely, other brain tumors), the presence of such tumors should be ruled out prior to initiation of treatment. Somatropin should not be used in patients with any evidence of progression or recurrence of an underlying intracranial tumor. Hypersensitivity GENOTROPIN is contraindicated in patients with a known hypersensitivity to somatropin or any of its excipients. The 5 mg and 12 mg presentations of GENOTROPIN lyophilized powder contain m-cresol as a preservative. Systemic hypersensitivity reactions have been reported with post-marketing use of somatropin products [see WARNINGS AND PRECAUTIONS] . Diabetic Retinopathy Somatropin is contraindicated in patients with active proliferative or severe non-proliferative diabetic retinopathy. Closed Epiphyses Somatropin should not be used for growth promotion in pediatric patients with closed epiphyses. | growth failure in children and adults who lack natural growth hormone, and in those with chronic kidney failure, Noonan syndrome, Turner syndrome, short stature at birth with no catch-up growth, and other causes | Genotropin is a form of human growth hormone important for the growth of bones and muscles. Genotropin is used to treat growth failure in children and adults who lack natural growth hormone. This includes people with short stature due to Noonan syndrome, Turner syndrome, Prader-Willi syndrome, short... | NA | NA | NA | Link | Link | NA |
| 11456 | Th1249 | Somatotropin | >Th1249_Somatotropin FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | 22129 | C990H1532N262O300S7 | 5.27 | -0.411 | 76 °C at pH 3.5 | When somatotropin was administered subcutaneously at the dose of 0.024 mg/kg or 3 IU/m2, the mean apparent terminal half-life was Following intravenous infusion of 33 ng/kg/min of somatotropin in patients with growth hormone deficiency, the terminal elimination half-life was approximately 21.1 (±5.1) minutes.[L10971] | Human growth hormone (HGH), also known as somatotropin, is a peptide hormone that is synthesized and secreted by the somatotropic cells of the anterior pituitary gland.[A228183] Growth hormone plays an essential role in growth regulation during childhood as well as other basal metabolic functions, muscle and fat mass regulation, blood glucose level regulation, and lipid regulation in both children and adults.[A228183, L31508] Synthesized in a strain of _Escherichia coli_, recombinant HGH is a polypeptide hormone that contains 191 amino acid residues with a molecular weight of 22 kDa. It has an identical primary protein structure to endogenous human growth hormone.[A228188] Recombinant HGH has been commercially available since 1985 after its development by Genentech. [Somatrem] was the first available recombinant HGH and was largely replaced by somatropin, another form of recombinant HGH.[A228183] Growth hormone therapy is approved for various disorders of growth hormone deficiency, growth failure, or short stature including Turner syndrome, chronic renal insufficiency before transplantation, Prader-Willi syndrome, a history of fetal growth restriction, short stature homeobox (SHOX) haploinsufficiency, Noonan syndrome, idiopathic short stature, and adult- or childhood-onset growth hormone deficiency.[A228188] Recombinant growth hormone is available as a subcutaneous injection for children and adults under a wide variety of brand names. | Somatotropin is indicated for the treatment of pediatric patients who have growth failure due to an inadequate secretion of endogenous growth hormone, short stature associated with Turner syndrome, Prader-Willi syndrome (PWS), idiopathic short stature (ISS), short stature or growth failure in short stature homeobox-containing gene (SHOX) deficiency, and short stature born small for gestational age (SGA).[L31513, L31518] It is indicated for the treatment of growth failure in children associated with chronic kidney disease up to the time of renal transplantation.[L31523] It is also indicated for adults with adult-onset growth hormone deficiency, either alone or associated with multiple hormone deficiencies (hypopituitarism), as a result of pituitary disease, hypothalamic disease, surgery, radiation therapy, or trauma. It is also used to treat childhood-onset growth hormone deficiency in adults due to congenital, genetic, acquired, or idiopathic causes.[L31518] Somatotropin is indicated for the treatment of wasting or cachexia in patients with human immunodeficiency virus (HIV) who are receiving antiretroviral therapy to increase lean body mass and body weight and improve physical endurance.[L31498] Somatotropin is indicated for the treatment of short bowel syndrome in adult patients receiving specialized nutritional support.[L31493] | Somatotropin induces growth in nearly every tissue and organ in the body.[L31508] It stimulates linear growth and cartilaginous growth of long bones. In children with short stature, growth hormone increases both the number and size of muscle cells. It also promotes the growth of internal organs, and it also increases red cell mass. By promoting nitrogen retention, growth hormone increases cellular protein synthesis. Growth hormone also retains potassium and phosphorus in the serum, which may be the result of cell growth. Growth hormone stimulates the synthesis of chondroitin sulfate and collagen and increases the urinary excretion of hydroxyproline. It has negligible effects on serum calcium levels. Although increased calcium excretion in the urine is observed, calcium absorption from the intestine is simultaneously enhanced.[L10971] In end-stage renal disease, growth hormone was shown to improve several nutritional parameters, such as increases in serum insulin-like growth factor-I (IGF-I), serum albumin, and transferrin, as well as a reduction in blood urea nitrogen.[A228403] The metabolic effects of growth hormone are caused by the upregulation of insulin-like growth factor-1. Generally, growth hormone leads cells to enter an anabolic protein state with increased amino acid uptake, protein synthesis, and decreased catabolism of proteins.[L31508] The diabetogenic effect of larger doses of growth hormone is well documented in the literature: somatotropin antagonizes insulin action _in vivo_, causing insulin resistance and glucose intolerance. It increases glucose production through gluconeogenesis and glycogenolysis from the liver and kidney [A228398] and suppresses glucose uptake in the adipose tissue.[A228388] In mice, growth hormone increased mRNA expression of 2 major gluconeogenic genes, phosphoenolpyruvate carboxy-kinase and glucose-6-phosphatase.[A228398] The risk for impaired glucose tolerance and reduced insulin sensitivity may be increased in susceptible patients, especially in those with risk factors for diabetes mellitus, such as obesity, Turner syndrome, or a family history of diabetes mellitus. The development of new-onset type 2 Diabetes Mellitus was observed in patients receiving somatotropin treatment.[L10971] Growth hormone stimulates lipolysis via activation of the hormone-sensitive lipase in the adipose tissue, thereby increasing circulating levels of free fatty acids and triglycerides in the plasma. It also leads to a reduction of fat stores and decreased serum levels of low-density lipoprotein (LDL) cholesterol.[L10971] In contrast to the effects seen in the adipose tissue, growth hormone promotes cellular uptake of free fatty acids in skeletal muscle by increasing the activity of lipoprotein lipase. Growth hormone may cause hyperinsulinism following beta-cell compensation for insulin resistance; however, there is some evidence that growth hormone directly promotes beta-cell proliferation and glucose-stimulated insulin secretion.[A228398] | In conditions of growth failure, growth hormone deficiency, low body mass, and malnutrition, somatotropin treatment acts to mimic and restore the actions of endogenous growth hormone of stimulating linear bone growth, increasing bone mass, increasing muscle and reduced fat mass, and regulating blood glucose and lipid levels.[A228183] Somatotropin mediates its effects both directly by somatotropin and indirectly by insulin-like growth factor-1 (IGF-1), which is upregulated by growth hormone. It binds to the human growth hormone receptor (GHR), which is a dimeric receptor expressed in target cells in the liver and cartilage.[L10971] Upon binding of growth hormone, GHR dimerizes and interacts with Janus kinase 2 (JAK2), subsequently leading to tyrosine phosphorylation of JAK2 and the GH receptor. The signal transducer activator of transcription (STAT) pathway is initiated, where transcription factors such as STAT1, STAT3, and STAT5 are translocated into the nucleus to stimulate target gene transcription.[L31508] At the epiphysis or growth plate, growth hormone increases linear growth by promoting differentiation of prechondrocytes and expansion of osteoblasts. Growth hormone binding to its receptor in the liver and cartilage promotes the production of IGF-1, which acts on type 1 IGF receptors to also stimulate linear growth. In the liver, activated growth hormone receptor signalling leads to increased production of IGF binding protein-3 (IGFBP-3) and acid-labile subunit (ALS), which are proteins that bind to IGF-1 in a ternary complex to increase its half-life.[A228183] | The oral LD50 is 242 mg/kg in rats and 828 mg/kg in mice. The inhalatory LD50 is 710 mg/m3 and dermal LD50 is 1100 mg/kg in rats. The intraperitoneal LD50 in mice is 828 mg/kg.[L31528] Hypoglycemia followed by hyperglycemia, possibly with fluid retention, can be observed in somatropin overdose. Long-term or excessive use of growth hormone can lead to the signs and symptoms of gigantism and acromegaly.[L10971] | Information is unavailable. | When somatotropin was administered subcutaneously at the dose of 0.024 mg/kg or 3 IU/m2, the Cmax ranged from 13.8 (±5.8) to 17.1 (±10.0) ng/mL and the Tmax was four to five hours. Following intravenous infusion of 33 ng/kg/min of somatotropin in patients with growth hormone deficiency, the mean steady-state serum levels of approximately 23.1 (±15.0) ng/mL were reached at 150 minutes.[L10971] | NA | NA | Cytochrome P-450 Enzyme Inhibitors | 7686786 | 30-03-2010 | 03-08-2026 | NA | Growth hormone receptor,Prolactin receptor | Genotropin | Pharmacia and Upjohn Company LLC | Pharmacia and Upjohn Company LLC | Subcutaneous | 0.6 mg/0.25mL | Acute Critical Illness Treatment with pharmacologic amounts of somatropin is contraindicated in patients with acute critical illness due to complications following open heart surgery, abdominal surgery or multiple accidental trauma, or those with acute respiratory failure [see WARNINGS AND PRECAUTIONS]. Prader-Willi Syndrome In Children Somatropin is contraindicated in patients with Prader-Willi syndrome who are severely obese, have a history of upper airway obstruction or sleep apnea, or have severe respiratory impairment. There have been reports of sudden death when somatropin was used in such patients [see WARNINGS AND PRECAUTIONS]. Active Malignancy In general, somatropin is contraindicated in the presence of active malignancy. Any preexisting malignancy should be inactive and its treatment complete prior to instituting therapy with somatropin. Somatropin should be discontinued if there is evidence of recurrent activity. Since growth hormone deficiency may be an early sign of the presence of a pituitary tumor (or, rarely, other brain tumors), the presence of such tumors should be ruled out prior to initiation of treatment. Somatropin should not be used in patients with any evidence of progression or recurrence of an underlying intracranial tumor. Hypersensitivity GENOTROPIN is contraindicated in patients with a known hypersensitivity to somatropin or any of its excipients. The 5 mg and 12 mg presentations of GENOTROPIN lyophilized powder contain m-cresol as a preservative. Systemic hypersensitivity reactions have been reported with post-marketing use of somatropin products [see WARNINGS AND PRECAUTIONS] . Diabetic Retinopathy Somatropin is contraindicated in patients with active proliferative or severe non-proliferative diabetic retinopathy. Closed Epiphyses Somatropin should not be used for growth promotion in pediatric patients with closed epiphyses. | growth failure in children and adults who lack natural growth hormone, and in those with chronic kidney failure, Noonan syndrome, Turner syndrome, short stature at birth with no catch-up growth, and other causes | Genotropin is a form of human growth hormone important for the growth of bones and muscles. Genotropin is used to treat growth failure in children and adults who lack natural growth hormone. This includes people with short stature due to Noonan syndrome, Turner syndrome, Prader-Willi syndrome, short... | NA | NA | NA | Link | Link | NA |
| 11560 | Th1250 | Pegademase | >Th1250_Pegademase MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAEQCL | 40788.2 | C1821H2834N484O552S14 | 5.33 | -0.428 | NA | plasma adenosine deaminase elimination half-life is 3 to >6 days | Bovine adenosine deaminase derived from bovine intestine that has been extensively pegylated for extended serum half life. | For treatment of adenosine deaminase deficiency | Used to replace deficient or inactive adenosine deaminase which leads to severe combined immunodeficiency disease (SCID). The enzyme is responsible for converting adenosine to inosine. In the absence of adenosine deaminase, the purine substrates adenosine, 2'-deoxyadenosine and their metabolites are actually toxic to lymphocytes thereby leading to diminished immune function. | Pegademase converts adenosine (toxic) to inosine (less toxic) by deamination. It also converts 2'-deoxyadenosine to 2'-deoxyinosine via deamination. | NA | NA | Time to peak for plasma adenosine deaminase is 2 to 3 days | NA | NA | Enzymes | NA | NA | NA | NA | Adenosine,Growth factor receptor-bound protein 2 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11561 | Th1250 | Pegademase | >Th1250_Pegademase MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAEQCL | 40788.2 | C1821H2834N484O552S14 | 5.33 | -0.428 | NA | plasma adenosine deaminase elimination half-life is 3 to >6 days | Bovine adenosine deaminase derived from bovine intestine that has been extensively pegylated for extended serum half life. | For treatment of adenosine deaminase deficiency | Used to replace deficient or inactive adenosine deaminase which leads to severe combined immunodeficiency disease (SCID). The enzyme is responsible for converting adenosine to inosine. In the absence of adenosine deaminase, the purine substrates adenosine, 2'-deoxyadenosine and their metabolites are actually toxic to lymphocytes thereby leading to diminished immune function. | Pegademase converts adenosine (toxic) to inosine (less toxic) by deamination. It also converts 2'-deoxyadenosine to 2'-deoxyinosine via deamination. | NA | NA | Time to peak for plasma adenosine deaminase is 2 to 3 days | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Adenosine,Growth factor receptor-bound protein 2 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11715 | Th1253 | Hyaluronidase (ovine) | >Th1253_Hyaluronidase_(ovine) MWTGLGPAVTLALVLVVAWATELKPTAPPIFTGRPFVVAWDVPTQDCGPRHKMPLDPKDMKAFDVQASPNEGFVNQNITIFYRDRLGMYPHFNSVGGSVHGGVPQNGSLWVHLEMLKGHVEHYIRTQEPAGLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASHHPDWPPERIVKEAQYEFEFAARQFMLETLRFVKAFRPRHLWGFYLFPDCYNHDYVQNWETYTGRCPDVEVSRNDQLSWLWAESTALFPSVYLEETLASSTHGRNFVSFRVQEALRVADVHHANHALPVYVFTRPTYSRGLTGLSEMDLISTIGESAALGAAGVILWGDAGFTTSNETCRRLKDYLTRSLVPYVVNVSWAAQYCSWAQCHGHGRCVRRDPNAHTFLHLSASSFRLVPSHAPDEPRLRPEGELSWADRNHLQTHFRCQCYLGWGGEQCQWDRRRAAGGASGAWAGFHLTGLLAVAVLAFTWTS | 53870.9 | C2455H3775N617O704S21 | 5.73 | -0.117 | NA | NA | Highly purified sheep hyaluronidase for administration by injection into the vitreous of the eye. | For increase of absorption and distribution of other injected drugs and for rehydration. | Hyaluronidase hydrolyzes hyaluronic acid and increase diffusion of injected drugs, thus facilitating their absorption. Hyaluronidase is used for enhancing absorption and distribution of other injected drugs. | Hyaluronidase is a spreading or diffusing substance. It increase the permeability of connective tissue through the hydrolysis of hyaluronic acid. Hyaluronidase hydrolyzes hyaluronic acid by splitting the glucosaminidic bond between C1 of the glucosamine moiety and C4 of glucuronic acid. This temporarily decreases the viscosity of the cellular cement and increases diffusion of injected fluids or of localized transudates or exudates, thus facilitating their absorption. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | Dopamine,Betamethasone,Fluocinolone acetonide,Triamcinolone,Hydrocortisone,Methylprednisolone,Trilostane,Dexamethasone,Corticotropin,Cortisone acetate,Paramethasone,Aldosterone,Fluprednidene,Fluprednisolone,Meprednisone,Dexamethasone isonicotinate,Melengestrol,Cortivazol,Prednylidene,Fluocortin,Fluperolone,Fluclorolone,Hydrocortisone succinate,Prednisolone hemisuccinate,Methylprednisolone hemisuccinate,Prednisone acetate,Clocortolone acetate,Melengestrol acetate,Betamethasone phosphate,Prednisolone,Clobetasol propionate,Prednisolone acetate,Fluorometholone,Cloprednol,Salicylic acid,Dersalazine,Phenyl aminosalicylate,Nitroaspirin,Aloxiprin,Guacetisal,Thiosalicylic acid,Acetylsalicylic acid,Lidocaine,Bupivacaine,Cinchocaine,Dyclonine,Prilocaine,Proparacaine,Oxybuprocaine,Mepivacaine,Benzocaine,Tetrodotoxin,Benzyl alcohol,Etidocaine,Articaine,Tetracaine,Butamben,Butacaine,Butanilicaine,Metabutethamine,Quinisocaine,Propoxycaine,Procaine,Phenol,Benzatropine,Ziprasidone,Cetirizine,Promazine,Imipramine,Chlorpromazine,Cimetidine,Hydroxyzine,Risperidone,Benzquinamide,Propiomazine,Brompheniramine,Ranitidine,Methdilazine,Famotidine,Methantheline,Azelastine,Dimenhydrinate,Promethazine,Mequitazine,Diphenhydramine,Chlorpheniramine,Orphenadrine,Cyclizine,Aripiprazole,Methotrimeprazine,Aceprometazine,Phenindamine,Zuclopenthixol,Methapyrilene,Esmirtazapine,Chloropyramine,Metiamide,Roxatidine acetate,Dimetotiazine,Butriptyline,Lafutidine,GSK-1004723,Lavoltidine,Deptropine,Tritoqualine,Quifenadine,Niperotidine,Aripiprazole lauroxil,GSK-239512,ABT-288,Olanzapine,Clemastine,Mirtazapine,Nizatidine,Epinastine,Pheniramine,Amitriptyline,Maprotiline,Emedastine,Dimetindene,Chlorphenoxamine,Trazodone,Antazoline,Bethanidine,Etomidate,Norepinephrine,Phenylephrine,Clonidine,Metaraminol,Dexmedetomidine,Epinephrine,Methoxamine,Dobutamine,Methyldopa,Ergometrine,Ephedrine,Mephentermine,4-Methoxyamphetamine,4-Bromo-2,5-dimethoxyphenethylamine,Tetryzoline,Adrafinil,Cirazoline,Synephrine,Amitraz,Medetomidine,Xylazine,Romifidine,Detomidine,Octopamine,Norfenefrine,Oxymetazoline,Etilefrine,Racepinephrine,Diethylstilbestrol,Chlorotrianisene,Conjugated estrogens,Estradiol,Ethinylestradiol,Mestranol,Estrone sulfate,Quinestrol,Hexestrol,Tibolone,Synthetic Conjugated Estrogens, A,Synthetic Conjugated Estrogens, B,Polyestradiol phosphate,Esterified estrogens,Zeranol,Equol,Methallenestril,Epimestrol,Moxestrol,Estradiol acetate,Estradiol benzoate,Estradiol cypionate,Estradiol valerate,Biochanin A,Formononetin,Estriol,Estetrol,Lorazepam,Midazolam,Halazepam,Diazepam,Camazepam,Ethyl loflazepate,Fludiazepam,1,2-Benzodiazepine,Loprazolam,Doxefazepam,Oxazepam acetate,Cinazepam,Bentazepam,Remimazolam,Clonazepam,Adinazolam,Delorazepam,Furosemide,Phenytoin,Fosphenytoin,Dexamethasone acetate | Hyaluronan,Transforming growth factor beta-1 | Vitrase | ISTA PHARMACUTICALS, INC | ISTA PHARMACUTICALS, INC | Subcutaneous | 6200 [USP'U]/5mL | VITRASE (hyaluronidase injection) is contraindicated in patients with known hypersensitivity to hyaluronidase or any other ingredient in the formulation. A preliminary skin test for hypersensitivity to VITRASE can be performed. The skin test is made by intradermal injection of approximately 0.02 mL (4 Units) of a 200 Units/mL solution [see DOSAGE AND ADMINISTRATION]. A positive reaction consists of a wheal with pseudopods appearing within 5 minutes and persisting for 20 to 30 minutes and accompanied by localized itching. Transient vasodilation at the site of the test, i.e., erythema, is not a positive reaction. Discontinue VITRASE if sensitization occurs. | local injection site reactions such as pain, itching, redness, or swelling. | NA | Vitrase is a prescription medicine used to treat the symptoms of Hypodermoclysis, Extravasation, and Skin Test. Vitrase may be used alone or with other medications. | NA | VITRASE (hyaluronidase injection) is supplied as a sterile, non-preserved, colorless solution with a pH of 6.4 to 7.2. Each mL contains 200 USP units of ovine hyaluronidase with 0.93 mg lactose, 0.36 mg potassium phosphate dibasic, 0.23 mg potassium phosphate monobasic, and 9.0 mg sodium chloride. | Link | Link | NA |
| 11716 | Th1253 | Hyaluronidase (ovine) | >Th1253_Hyaluronidase_(ovine) MWTGLGPAVTLALVLVVAWATELKPTAPPIFTGRPFVVAWDVPTQDCGPRHKMPLDPKDMKAFDVQASPNEGFVNQNITIFYRDRLGMYPHFNSVGGSVHGGVPQNGSLWVHLEMLKGHVEHYIRTQEPAGLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASHHPDWPPERIVKEAQYEFEFAARQFMLETLRFVKAFRPRHLWGFYLFPDCYNHDYVQNWETYTGRCPDVEVSRNDQLSWLWAESTALFPSVYLEETLASSTHGRNFVSFRVQEALRVADVHHANHALPVYVFTRPTYSRGLTGLSEMDLISTIGESAALGAAGVILWGDAGFTTSNETCRRLKDYLTRSLVPYVVNVSWAAQYCSWAQCHGHGRCVRRDPNAHTFLHLSASSFRLVPSHAPDEPRLRPEGELSWADRNHLQTHFRCQCYLGWGGEQCQWDRRRAAGGASGAWAGFHLTGLLAVAVLAFTWTS | 53870.9 | C2455H3775N617O704S21 | 5.73 | -0.117 | NA | NA | Highly purified sheep hyaluronidase for administration by injection into the vitreous of the eye. | For increase of absorption and distribution of other injected drugs and for rehydration. | Hyaluronidase hydrolyzes hyaluronic acid and increase diffusion of injected drugs, thus facilitating their absorption. Hyaluronidase is used for enhancing absorption and distribution of other injected drugs. | Hyaluronidase is a spreading or diffusing substance. It increase the permeability of connective tissue through the hydrolysis of hyaluronic acid. Hyaluronidase hydrolyzes hyaluronic acid by splitting the glucosaminidic bond between C1 of the glucosamine moiety and C4 of glucuronic acid. This temporarily decreases the viscosity of the cellular cement and increases diffusion of injected fluids or of localized transudates or exudates, thus facilitating their absorption. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Hyaluronan,Transforming growth factor beta-1 | Vitrase | Bausch & Lomb Incorporated | Bausch & Lomb Incorporated | Subcutaneous | 200 [USP'U]/1mL | VITRASE (hyaluronidase injection) is contraindicated in patients with known hypersensitivity to hyaluronidase or any other ingredient in the formulation. A preliminary skin test for hypersensitivity to VITRASE can be performed. The skin test is made by intradermal injection of approximately 0.02 mL (4 Units) of a 200 Units/mL solution [see DOSAGE AND ADMINISTRATION]. A positive reaction consists of a wheal with pseudopods appearing within 5 minutes and persisting for 20 to 30 minutes and accompanied by localized itching. Transient vasodilation at the site of the test, i.e., erythema, is not a positive reaction. Discontinue VITRASE if sensitization occurs. | local injection site reactions such as pain, itching, redness, or swelling. | NA | Vitrase is a prescription medicine used to treat the symptoms of Hypodermoclysis, Extravasation, and Skin Test. Vitrase may be used alone or with other medications. | NA | VITRASE (hyaluronidase injection) is supplied as a sterile, non-preserved, colorless solution with a pH of 6.4 to 7.2. Each mL contains 200 USP units of ovine hyaluronidase with 0.93 mg lactose, 0.36 mg potassium phosphate dibasic, 0.23 mg potassium phosphate monobasic, and 9.0 mg sodium chloride. | Link | Link | NA |
| 11836 | Th1260 | Alfimeprase | >Th1260_Alfimeprase SFPQRYVQLVIVADHRMNTKYNGDSDKIRQWVHQIVNTINEIYRPLNIQFTLVGLEIWSNQDLITVTSVSHDTLASFGNWRETDLLRRQRHDNAQLLTAIDFDGDTVGLAYVGGMCQLKHSTGVIQDHSAINLLVALTMAHELGHNLGMNHDGNQCHCGANSCVMAAMLSDQPSKLFSDCSKKDYQTFLTVNNPQCILNKP | NA | NA | NA | NA | NA | NA | Alfimeprase is a recombinant analog of fibrolase. Fibrolase is a zinc-containing metalloproteinase isolated from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix). It is a small protein that contains 203 residues (Randolph et al. 1992). Alfimeprase is being developed by Nuvelo. | Alfimeprase is being evaluated as a potential treatment for acute ischemic stroke, catheter occlusion (CO) and acute peripheral arterial occlusion (PAO). | Alfimeprase is a recombinant direct acting fibrinolytic (rDAF), or blood clot dissolver, that has the potential to rapidly and directly degrade fibrin, a protein that provides the scaffolding for blood clots, when delivered through a catheter to the site of a blood clot. | When delivered locally at the site of a blood clot, alfimeprase has the potential, through a unique mechanism of action, to directly and rapidly degrade fibrin, a protein that provides the scaffolding for blood clots. In addition, alfimeprase's thrombolytic activity appears to be localized to the site of delivery because it is rapidly inactivated by alpha-2 macroglobulin, a naturally occurring protein in the blood, as it moves away from the site of delivery and into the general blood circulation. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | Fibrinogen alpha chain,Fibrinogen beta chain | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11837 | Th1260 | Alfimeprase | >Th1260_Alfimeprase SFPQRYVQLVIVADHRMNTKYNGDSDKIRQWVHQIVNTINEIYRPLNIQFTLVGLEIWSNQDLITVTSVSHDTLASFGNWRETDLLRRQRHDNAQLLTAIDFDGDTVGLAYVGGMCQLKHSTGVIQDHSAINLLVALTMAHELGHNLGMNHDGNQCHCGANSCVMAAMLSDQPSKLFSDCSKKDYQTFLTVNNPQCILNKP | NA | NA | NA | NA | NA | NA | Alfimeprase is a recombinant analog of fibrolase. Fibrolase is a zinc-containing metalloproteinase isolated from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix). It is a small protein that contains 203 residues (Randolph et al. 1992). Alfimeprase is being developed by Nuvelo. | Alfimeprase is being evaluated as a potential treatment for acute ischemic stroke, catheter occlusion (CO) and acute peripheral arterial occlusion (PAO). | Alfimeprase is a recombinant direct acting fibrinolytic (rDAF), or blood clot dissolver, that has the potential to rapidly and directly degrade fibrin, a protein that provides the scaffolding for blood clots, when delivered through a catheter to the site of a blood clot. | When delivered locally at the site of a blood clot, alfimeprase has the potential, through a unique mechanism of action, to directly and rapidly degrade fibrin, a protein that provides the scaffolding for blood clots. In addition, alfimeprase's thrombolytic activity appears to be localized to the site of delivery because it is rapidly inactivated by alpha-2 macroglobulin, a naturally occurring protein in the blood, as it moves away from the site of delivery and into the general blood circulation. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Fibrinogen alpha chain,Fibrinogen beta chain | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11853 | Th1262 | Desmoteplase | >Th1262_Desmoteplase MVNTMKTKLLCVLLLCGAVFSLPRQETYRQLARGSRAYGVACKDEITQMTYRRQESWLRPEVRSKRVEHCQCDRGQARCHTVPVNSCSEPRCFNGGTCWQAVYFSDFVCQCPAGYTGKRCEVDTRATCYEGQGVTYRGTWSTAESRVECINWNSSLLTRRTYNGRMPDAFNLGLGNHNYCRNPNGAPKPWCYVIKAGKFTSESCSVPVCSKATCGLRKYKEPQLHSTGGLFTDITSHPWQAAIFAQNRRSSGERFLCGGILISSCWVLTAAHCFQESYLPDQLKVVLGRTYRVKPGEEEQTFKVKKYIVHKEFDDDTYNNDIALLQLKSDSPQCAQESDSVRAICLPEANLQLPDWTECELSGYGKHKSSSPFYSEQLKEGHVRLYPSSRCAPKFLFNKTVTNNMLCAGDTRSGEIYPNVHDACQGDSGGPLVCMNDNHMTLLGIISWGVGCGEKDVPGVYTKVTNYLGWIRDNMHL | NA | NA | NA | NA | NA | NA | Desmoteplase is a chemical in the saliva of vampire bats. It activates plasminogen to the serine protease, plasmin. Plasmin acts by breaking down fibrin blood clots. When a vampire bat bites its victim, it secretes an enzyme that prevents the blood from clotting. The enzyme is called DSPA (Desmodus rotundus salivary plasminogen activator) and scientists are using DSPA as stroke and heart attack medication. Desmoteplase is a recombinant form of vampire bat DSPA (Salivary plasminogen activator alpha 1). | Investigated for use/treatment in cerebral ischemia and strokes. | Desmoteplase is a novel thrombolytic agent derived from vampire-bat saliva. It is genetically related to the clot buster tissue plasminogen activator (t-PA) but is more potent and demonstrates a safer toxicity profile (desmoteplase does not promote kainate- or NMDA-mediated neurotoxicity in vivo). Plasminogen activators are enzymes found in all vertebrate species investigated so far. Their physiological function is the generation of localized proteolysis in the context of tissue remodeling, wound healing and neuronal plasticity. | Desmoteplase targets and destroys fibrin, the structural scaffold of blood clots. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | Plasminogen | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11854 | Th1262 | Desmoteplase | >Th1262_Desmoteplase MVNTMKTKLLCVLLLCGAVFSLPRQETYRQLARGSRAYGVACKDEITQMTYRRQESWLRPEVRSKRVEHCQCDRGQARCHTVPVNSCSEPRCFNGGTCWQAVYFSDFVCQCPAGYTGKRCEVDTRATCYEGQGVTYRGTWSTAESRVECINWNSSLLTRRTYNGRMPDAFNLGLGNHNYCRNPNGAPKPWCYVIKAGKFTSESCSVPVCSKATCGLRKYKEPQLHSTGGLFTDITSHPWQAAIFAQNRRSSGERFLCGGILISSCWVLTAAHCFQESYLPDQLKVVLGRTYRVKPGEEEQTFKVKKYIVHKEFDDDTYNNDIALLQLKSDSPQCAQESDSVRAICLPEANLQLPDWTECELSGYGKHKSSSPFYSEQLKEGHVRLYPSSRCAPKFLFNKTVTNNMLCAGDTRSGEIYPNVHDACQGDSGGPLVCMNDNHMTLLGIISWGVGCGEKDVPGVYTKVTNYLGWIRDNMHL | NA | NA | NA | NA | NA | NA | Desmoteplase is a chemical in the saliva of vampire bats. It activates plasminogen to the serine protease, plasmin. Plasmin acts by breaking down fibrin blood clots. When a vampire bat bites its victim, it secretes an enzyme that prevents the blood from clotting. The enzyme is called DSPA (Desmodus rotundus salivary plasminogen activator) and scientists are using DSPA as stroke and heart attack medication. Desmoteplase is a recombinant form of vampire bat DSPA (Salivary plasminogen activator alpha 1). | Investigated for use/treatment in cerebral ischemia and strokes. | Desmoteplase is a novel thrombolytic agent derived from vampire-bat saliva. It is genetically related to the clot buster tissue plasminogen activator (t-PA) but is more potent and demonstrates a safer toxicity profile (desmoteplase does not promote kainate- or NMDA-mediated neurotoxicity in vivo). Plasminogen activators are enzymes found in all vertebrate species investigated so far. Their physiological function is the generation of localized proteolysis in the context of tissue remodeling, wound healing and neuronal plasticity. | Desmoteplase targets and destroys fibrin, the structural scaffold of blood clots. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Plasminogen | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11892 | Th1265 | Ranpirnase | NA | NA | NA | NA | NA | NA | NA | Ranpirnase is a ribonuclease enzyme found in Rana pipiens oocytes. It is being studied in the treatment of cancer. It is manufactured by Alfacell Corporation. It is the first ribonuclease to enter cancer clinical trials. | For the treatment of various forms of cancer. | NA | Ranpirnase controls tumour growth by degrading RNA within cancer cells, resulting in inhibition of protein synthesis and arresting mitosis in G(1)phase. | NA | NA | NA | NA | NA | Enzyme Inhibitors | NA | NA | NA | NA | DNA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11893 | Th1265 | Ranpirnase | NA | NA | NA | NA | NA | NA | NA | Ranpirnase is a ribonuclease enzyme found in Rana pipiens oocytes. It is being studied in the treatment of cancer. It is manufactured by Alfacell Corporation. It is the first ribonuclease to enter cancer clinical trials. | For the treatment of various forms of cancer. | NA | Ranpirnase controls tumour growth by degrading RNA within cancer cells, resulting in inhibition of protein synthesis and arresting mitosis in G(1)phase. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | DNA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11894 | Th1265 | Ranpirnase | NA | NA | NA | NA | NA | NA | NA | Ranpirnase is a ribonuclease enzyme found in Rana pipiens oocytes. It is being studied in the treatment of cancer. It is manufactured by Alfacell Corporation. It is the first ribonuclease to enter cancer clinical trials. | For the treatment of various forms of cancer. | NA | Ranpirnase controls tumour growth by degrading RNA within cancer cells, resulting in inhibition of protein synthesis and arresting mitosis in G(1)phase. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | DNA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12064 | Th1283 | Fibrinolysin | >Th1283_Fibrinolysin DLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGR | 88411.4 | C3848H5912N1096O1185S60 | NA | NA | NA | Almost completely inactivated after 24 hours. | Fibrinolysin consists of two polypeptide chains, one light and one heavy, linked by a disulfide bond. The light chain has a molecular weight of approximately 27,000 Da and contains the active center of Fibrinolysin; the heavy chain has a molecular weight of approximately 57,000 Da. Fibrinolysin is used as a local healing ointment when combined together with the enzyme deoxyribonuclease I (extracted from bovine pancreas). Fibrinolysin and deoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) Fibrinolysin and 666 BUs desoxyribonuclease per gram. The ointment is marketed by Pfizer under the brand name Fibrolan in a variety of countries (e.g. Switzerland). It is currently not approved in the USA. | Fibrinolysin assists with the healing of minor burns, superficial wounds, ulcers, surgical wounds, and superficial hematomas. | NA | Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living tissue. | NA | local inactivation | NA | NA | NA | Enzymes | NA | NA | NA | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12065 | Th1283 | Fibrinolysin | >Th1283_Fibrinolysin DLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGR | 88411.4 | C3848H5912N1096O1185S60 | NA | NA | NA | Almost completely inactivated after 24 hours. | Fibrinolysin consists of two polypeptide chains, one light and one heavy, linked by a disulfide bond. The light chain has a molecular weight of approximately 27,000 Da and contains the active center of Fibrinolysin; the heavy chain has a molecular weight of approximately 57,000 Da. Fibrinolysin is used as a local healing ointment when combined together with the enzyme deoxyribonuclease I (extracted from bovine pancreas). Fibrinolysin and deoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) Fibrinolysin and 666 BUs desoxyribonuclease per gram. The ointment is marketed by Pfizer under the brand name Fibrolan in a variety of countries (e.g. Switzerland). It is currently not approved in the USA. | Fibrinolysin assists with the healing of minor burns, superficial wounds, ulcers, surgical wounds, and superficial hematomas. | NA | Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living tissue. | NA | local inactivation | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12080 | Th1284 | Interferon alfa | >Th1284_Interferon_alfa CDLPETHSLDNRRTLMLLAQMSRISPSSCLMDRHDFGFPQEEFDGNQFQKAPAISVLHELIQQIFNLFTTKDSSAAWDEDLLDKFCTELYQQLNDLEACVMQEERVGETPLMNADSILAVKKYFRRITLYLTEKKYSPCAWEVVRAEIMRSLSLSTNLQERLRRKE | 20700 | NA | NA | NA | NA | NA | Natural interferon alpha or Multiferon is obtained from the leukocyte fraction of human blood following induction with Sendai virus. Interferon alfa contains several naturally occurring IFN-a subtypes and is purified by affinity chromatography. Interferon alpha proteins are mainly involved in innate immune response against viral infection. They come in 13 subtypes that are called IFNA1, IFNA2, IFNA4, IFNA5, IFNA6, IFNA7, IFNA8, IFNA10, IFNA13, IFNA14, IFNA16, IFNA17, IFNA21. Multiferon consists of the 6 major subtypes are IFN-a1, IFN-a2, IFN-a8, IFN-a10, IFN-a14 and IFN-a21. Of these, IFN-a2 and IFN-a14 are glycosylated. | Investigated for use/treatment in hepatitis (viral, C), leukemia (lymphoid), leukemia (myeloid), leukemia (unspecified), and melanoma. | NA | Natural alpha interferon offers multiple subtypes of interferon which may work together as a 'cocktail-in-one', while recombinant versions only exhibit a single subtype." Viragen offers MultiferonT at a cost which is competitive with recombinant interferon regimens. Natural alpha interferon contains the multiple subtype composition that is characteristic of interferon produced by the human body. It is believed that this results in a broader spectrum of specific anti-viral and immunoregulatory activity with the subtypes acting synergistically to give a wide-ranging response. | NA | Proteolyzed by endogenous proteases. | NA | NA | NA | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | Interferon alpha/beta receptor 1 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12159 | Th1292 | PEG-uricase | NA | NA | NA | NA | NA | NA | NA | PEG-uricase, a polyethylene glycol ("PEG") conjugate of recombinant porcine uricase (urate oxidase), which breaks down the uric acid deposits is being studied in Phase III clinical trials for the treatment of severe, treatment-refractory gout in the United States in 2006. | Investigated for use/treatment in hyperuricemia. | NA | PEG-uricase is a recombinant, PEGylated formulation of a modified porcine urate oxidase intended to dramatically lower the blood level of uric acid safely and continuously in patients who have not benefited from conventional therapeutic approaches. Urate oxidase is a hepatic enzyme present in almost all mammals – but not in humans – that lowers uric acid levels in the blood by converting uric acid into allantoin, a benign substance which is then easily excreted in the urine. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | Uric acid degradation bifunctional protein | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12160 | Th1292 | PEG-uricase | NA | NA | NA | NA | NA | NA | NA | PEG-uricase, a polyethylene glycol ("PEG") conjugate of recombinant porcine uricase (urate oxidase), which breaks down the uric acid deposits is being studied in Phase III clinical trials for the treatment of severe, treatment-refractory gout in the United States in 2006. | Investigated for use/treatment in hyperuricemia. | NA | PEG-uricase is a recombinant, PEGylated formulation of a modified porcine urate oxidase intended to dramatically lower the blood level of uric acid safely and continuously in patients who have not benefited from conventional therapeutic approaches. Urate oxidase is a hepatic enzyme present in almost all mammals – but not in humans – that lowers uric acid levels in the blood by converting uric acid into allantoin, a benign substance which is then easily excreted in the urine. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Uric acid degradation bifunctional protein | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12161 | Th1292 | PEG-uricase | NA | NA | NA | NA | NA | NA | NA | PEG-uricase, a polyethylene glycol ("PEG") conjugate of recombinant porcine uricase (urate oxidase), which breaks down the uric acid deposits is being studied in Phase III clinical trials for the treatment of severe, treatment-refractory gout in the United States in 2006. | Investigated for use/treatment in hyperuricemia. | NA | PEG-uricase is a recombinant, PEGylated formulation of a modified porcine urate oxidase intended to dramatically lower the blood level of uric acid safely and continuously in patients who have not benefited from conventional therapeutic approaches. Urate oxidase is a hepatic enzyme present in almost all mammals – but not in humans – that lowers uric acid levels in the blood by converting uric acid into allantoin, a benign substance which is then easily excreted in the urine. | NA | NA | NA | NA | NA | Enzymes, Immobilized | NA | NA | NA | NA | Uric acid degradation bifunctional protein | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12176 | Th1295 | ALTU-135 | NA | NA | NA | NA | NA | NA | NA | ALTU-135, the Company's orally administered enzyme replacement therapy for patients with pancreatic insufficiency, is manufactured by blending three drug substance enzymes: lipase, protease and amylase. This consistent and pure enzyme combination is designed to improve fat, protein and carbohydrate absorption in pancreatic insufficient individuals. ALTU-135 has been granted orphan drug and fast-track designation as well as CMA Pilot 2 program status by the Food and Drug Administration (FDA). | Investigated for use/treatment in cystic fibrosis and pancreatic disorders. | NA | As ALTU-135 consists of three enzymes, lipase, protease and amylase that are delivered in a consistent ratio and is designed to improve fat, protein, and carbohydrate absorption in pancreatic insufficient individuals. ALTU-135 is designed to be highly concentrated, stable and pure and to allow patients to take a single capsule per meal or snack, whereas current products are derived from pig pancreases and require a significantly higher pill burden. This reduced pill burden for ALTU-135 is expected to provide greater convenience for the patient and result in improved compliance and therefore effectiveness. ALTU-135 has been granted Orphan Drug designation in the United States and Europe. ALTU-135 was also granted fast track designation by the U.S. Food and Drug Administration (FDA) in November 2003, and was accepted into the FDA’s Continuous Marketing Application Pilot 2 Program in February 2004. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12177 | Th1295 | ALTU-135 | NA | NA | NA | NA | NA | NA | NA | ALTU-135, the Company's orally administered enzyme replacement therapy for patients with pancreatic insufficiency, is manufactured by blending three drug substance enzymes: lipase, protease and amylase. This consistent and pure enzyme combination is designed to improve fat, protein and carbohydrate absorption in pancreatic insufficient individuals. ALTU-135 has been granted orphan drug and fast-track designation as well as CMA Pilot 2 program status by the Food and Drug Administration (FDA). | Investigated for use/treatment in cystic fibrosis and pancreatic disorders. | NA | As ALTU-135 consists of three enzymes, lipase, protease and amylase that are delivered in a consistent ratio and is designed to improve fat, protein, and carbohydrate absorption in pancreatic insufficient individuals. ALTU-135 is designed to be highly concentrated, stable and pure and to allow patients to take a single capsule per meal or snack, whereas current products are derived from pig pancreases and require a significantly higher pill burden. This reduced pill burden for ALTU-135 is expected to provide greater convenience for the patient and result in improved compliance and therefore effectiveness. ALTU-135 has been granted Orphan Drug designation in the United States and Europe. ALTU-135 was also granted fast track designation by the U.S. Food and Drug Administration (FDA) in November 2003, and was accepted into the FDA’s Continuous Marketing Application Pilot 2 Program in February 2004. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12207 | Th1298 | Albinterferon Alfa-2B | >Th1298_Albinterferon_Alfa-2B DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGLCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 85700 | C3796H5937N1015O1143S50 | NA | NA | NA | NA | Albumin-interferon alpha (Albuferon) is a novel, long-acting form of interferon alpha. Recombinant interferon alpha is approved for the treatment of hepatitis C, hepatitis B, and a broad range of cancers. Human Genome Sciences modified interferon alpha to improve its pharmacological properties by using the company's proprietary albumin fusion technology. Human Genome Sciences is developing Albuferon as a potential treatment for chronic hepatitis C. The drug was under investigation as an alternative to pegylated IFN-a-2a for the treatment of hepatitis C. In response to an FDA ruling, Novartis and Human Genome Sciences announced on October 5, 2010 that they ceased development of the drug. | Investigated for use/treatment in hepatitis (viral, C). | NA | Interferons belong to a family of proteins known as cytokines that occur naturally in the human body. Cytokines control cellular processes, such as cell growth, activation, migration and aging. While the precise mechanism of action for interferon alpha is not known, research has demonstrated direct antiviral activity in patients with diseases like hepatitis C, as well as immune-modulating and direct antitumor effects in certain types of cancer. | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12299 | Th1311 | Praconase | NA | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in spinal cord injuries. | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12300 | Th1311 | Praconase | NA | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in spinal cord injuries. | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12640 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12641 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12690 | Th1345 | AVE9633 | NA | NA | NA | NA | NA | NA | NA | AVE9633 is an anti-CD33 monoclonal antibody-DM4 conjugate. | Investigated for use/treatment in leukemia (myeloid). | An immunoconjugate consisting of the humanized monoclonal antibody huMy9-6 conjugated to the cytotoxic maytansinoid derivative DM4 with potential antineoplastic activity. The monoclonal antibody portion of anti-CD33 monoclonal antibody-DM4 conjugate AVE9633 specifically binds to the cell surface antigen CD33 expressed on myeloid leukemia cells; upon internalization, the DM4 moiety is released, binds tubulin, and disrupts microtubule assembly/disassembly dynamics, resulting in the inhibition of cell division and cell growth in myeloid leukemia cells that express CD33. CD33 is expressed on normal non-pluripotent hematopoietic stem cells as well as on myeloid leukemia cells. [National Cancer Institute Drug Dictionary] | NA | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | Myeloid cell surface antigen CD33 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12723 | Th1349 | Latiglutenase | NA | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in gastrointestinal diseases and disorders (miscellaneous) and autoimmune diseases such as celiac disease. | NA | ALV003 is an orally administered combination of two proteases engineered to digest gluten. It targets the glutamine and proline residues that are common in gluten. ALV003 consists of a glutamine-specific cysteine protease (EP-B2) and a proline specific prolyl endopeptidase (PEP). The proposed mechanism of action of ALV003 is to digest gluten into non-immunotoxic fragments. [Alvine Pharmaceuticals Press Release] | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12724 | Th1349 | Latiglutenase | NA | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in gastrointestinal diseases and disorders (miscellaneous) and autoimmune diseases such as celiac disease. | NA | ALV003 is an orally administered combination of two proteases engineered to digest gluten. It targets the glutamine and proline residues that are common in gluten. ALV003 consists of a glutamine-specific cysteine protease (EP-B2) and a proline specific prolyl endopeptidase (PEP). The proposed mechanism of action of ALV003 is to digest gluten into non-immunotoxic fragments. [Alvine Pharmaceuticals Press Release] | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12735 | Th1350 | Coltuximab ravtansine | NA | NA | NA | NA | NA | NA | NA | Coltuximab ravtansine (SAR3419) targets CD19 and is being investigated for the treatment of acute lymphoblastic leukemia (ALL). | Investigated for use/treatment in lymphoma (non-hodgkin's). | NA | SAR3419 is an anti-CD19-DM4 immunoconjugate consisting of an anti-CD19 monoclonal antibody conjugated to the maytansinoid DM4, a derivative of the cytotoxic agent maytansine (DM1), with potential antineoplastic activity. SAR3419 targets the cell surface antigen CD19, found on a number of B-cell-derived cancers. Upon antibody/antigen binding and internalization, the immunoconjugate releases DM4, which binds to tubulin and disrupts microtubule assembly/disassembly dynamics, resulting in inhibition of cell division and cell growth of CD19-expressing tumor cells. [National Cancer Institute Drug Dictionary] | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | B-lymphocyte antigen CD19 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12789 | Th1355 | Human C1-esterase inhibitor | >Th1355_Human_C1-esterase_inhibitor MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA | 68000 | NA | NA | NA | NA | The half life of a 50 IU/kg dose is 2.4 ± 0.6 h, while the half life of a 100 IU/kg dose is 2.7 ± 0.3 h.[L16591] Subcutaneous administration produces a half life of 199.6 hours.[A19661] | C1 Esterase Inhibitor (Human) is composed of purified endogenous complement component-1 esterase inhibitor (hC1INH) isolated from human plasma.[L16586,L16591,L16606] The primary function of endogenous C1INH is to regulate the activation of the complement and contact system pathways.[L16586,L16591,L16606] This drug is indicated for prophylaxis and treatment of Hereditary Angioedema (HAE), a human genetic disorder caused by a shortage of C1 inhibitor activity that results in an overreaction of the immune system.[L16586,L16591,L16606] The disease is characterized by acute attacks of painful and in some cases fatal swelling of several soft tissues (edema), which may last up to five days when untreated.[L16586,L16591,L16606] | C1 esterase inhibitors are indicated for the prophylaxis and treatment of acute attacks of hereditary angioedema in patients at least 6 years old.[L16586,L16591,L16596] | The C1 esterase inhibitor treats and prevents attacks of hereditary angioedema.[L16591] It has a long duration of action as it is given every 3-4 days prophylactically.[L16586] Patients should be counselled regarding the risk of hypersensitivity reactions as well as arterial and venous thromboemboli.[L16586,L16591] | The C1 esterase inhibitor binds to proteins such as C1s, kallikrein, factor XIIa, and XIa and irreversibly inactivates them.[L16586,L16591] Patients with hereditary angioedema have low levels of C1 esterase inhibitors.[L16586,L16591] By providing patients with C1 esterase inhibitors, this may prevent contact system activation, which prevents increases in vascular permeability.[L16586,L16591] Manifestations of hereditary angioedema may be prevented by preventing increases in vascular permeability.[L16586,L16591] | Data regarding overdoses in humans are not readily available.[L16591] A study in monkeys showed doses above the recommended human dose resulted in temporarily increased liver enzymes such as AST and ALP.[L16591] | Protein drugs are expected to be degraded by proteases and other catalytic enzymes to smaller peptides and amino acids.[A182009] | A 50 IU/kg dose reaches a Cmax of 1.2 ± 0.2 IU/mL, with a Tmax of 0.31 ± 0.10 hours, and an AUC of 3.3 ± 1.0 IU | The volume of distribution at steady state of a 50 IU/kg dose is 3.0 ± 0.9 L.[L16591] | The clearance of a 50 IU/kg dose is 1207 ± 414 mL/h, while the clearance of a 100 IU/kg dose is 781 ± 147 mL/h.[L16591] | Enzyme Inhibitors | NA | NA | NA | NA | Complement C1r subcomponent,Complement C1s subcomponent,Plasma kallikrein,Coagulation factor XII,Prothrombin,Coagulation factor XI,Tissue-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12975 | Th1373 | Chymopapain | >Th1373_Chymopapain MATMSSISKIIFLATCLIIHMGLSSADFYTVGYSQDDLTSIERLIQLFDSWMLKHNKIYESIDEKIYRFEIFRDNLMYIDETNKKNNSYWLGLNGFADLSNDEFKKKYVGFVAEDFTGLEHFDNEDFTYKHVTNYPQSIDWRAKGAVTPVKNQGACGSCWAFSTIATVEGINKIVTGNLLELSEQELVDCDKHSYGCKGGYQTTSLQYVANNGVHTSKVYPYQAKQYKCRATDKPGPKVKITGYKRVPSNCETSFLGALANQPLSVLVEAGGKPFQLYKSGVFDGPCGTKLDHAVTAVGYGTSDGKNYIIIKNSWGPNWGEKGYMRLKRQSGNSQGTCGVYKSSYYPFKGFA | 27000 | NA | 10.2-10.6 | NA | 137-182 ºC | Following intra-discal injection, the level of chymopapain decreases gradually and presents a half-life of 2-3 days. The half-life for urinary excretion is reported to be of about 3 days.[A32704] | Chymopapain was first isolated in 1941 from the crude latex derived from the fruit of Carica papaya by squeezing the green papaya while on the plant prior to harvest.[L2482]It is an extracellular plant cysteine proteinase similar to papain in specificity.[A32688] Chymopapain was developed by Chart Medcl and FDA approved on November 10, 1982. It is currently discontinued.[L2487] | Chymopapain is indicated for the development of chemonucleolysis which is used for the digestion of the nucleus pulposus in patients with disc herniation confirmed by myelography.[A32687] A disc herniation occurs when the outer portion of the spinal disc breaks down and the inner portion (nucleus pulposus) leaks out pressing surrounding nerves and leading to irradiating pain.[L2496] The chemonucleolysis is a non-surgical treatment that involves the injection of an enzyme to dissolve the nucleus pulposus.[L2482] | The first studies showed that after intradiscal injection of chymopapain the effect involved the removal of the nucleus pulposus leaving the annulus intact.[L2482] The clinical reports indicated a spontaneous remission of symptoms after the administration of chymopapain. It is also highly documented an increased urinary excretion of glycosaminoglycans.[A32701] | Chymopapain is thought to degrade proteoglycan content of the intervertebral disc causing loss of glycosaminoglycan and water. This effect will cause the shrinkage of the disc and a reduction of the pressure on the nerve root.[A32701] | The median lethal dose of chymopapain in mice is registered to be 82 mg/kg and the toxicity mechanism was caused by hemorrhage due to the destruction of the cement substance in the blood vessels. When administered in an overdosage, chymopapain was able to nearly completely dissolve the nucleus pulposus and cause the disruption of the annulus fibrosus.[A32706] | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | Bone marrow proteoglycan | NA | NA | NA | NA | NA | NA | NA | NA | NA | disodium;4,5-dihydroxybenzene-1,3-disulfonate | NA | Link | NA | NA |
| 12976 | Th1373 | Chymopapain | >Th1373_Chymopapain MATMSSISKIIFLATCLIIHMGLSSADFYTVGYSQDDLTSIERLIQLFDSWMLKHNKIYESIDEKIYRFEIFRDNLMYIDETNKKNNSYWLGLNGFADLSNDEFKKKYVGFVAEDFTGLEHFDNEDFTYKHVTNYPQSIDWRAKGAVTPVKNQGACGSCWAFSTIATVEGINKIVTGNLLELSEQELVDCDKHSYGCKGGYQTTSLQYVANNGVHTSKVYPYQAKQYKCRATDKPGPKVKITGYKRVPSNCETSFLGALANQPLSVLVEAGGKPFQLYKSGVFDGPCGTKLDHAVTAVGYGTSDGKNYIIIKNSWGPNWGEKGYMRLKRQSGNSQGTCGVYKSSYYPFKGFA | 27000 | NA | 10.2-10.6 | NA | 137-182 ºC | Following intra-discal injection, the level of chymopapain decreases gradually and presents a half-life of 2-3 days. The half-life for urinary excretion is reported to be of about 3 days.[A32704] | Chymopapain was first isolated in 1941 from the crude latex derived from the fruit of Carica papaya by squeezing the green papaya while on the plant prior to harvest.[L2482]It is an extracellular plant cysteine proteinase similar to papain in specificity.[A32688] Chymopapain was developed by Chart Medcl and FDA approved on November 10, 1982. It is currently discontinued.[L2487] | Chymopapain is indicated for the development of chemonucleolysis which is used for the digestion of the nucleus pulposus in patients with disc herniation confirmed by myelography.[A32687] A disc herniation occurs when the outer portion of the spinal disc breaks down and the inner portion (nucleus pulposus) leaks out pressing surrounding nerves and leading to irradiating pain.[L2496] The chemonucleolysis is a non-surgical treatment that involves the injection of an enzyme to dissolve the nucleus pulposus.[L2482] | The first studies showed that after intradiscal injection of chymopapain the effect involved the removal of the nucleus pulposus leaving the annulus intact.[L2482] The clinical reports indicated a spontaneous remission of symptoms after the administration of chymopapain. It is also highly documented an increased urinary excretion of glycosaminoglycans.[A32701] | Chymopapain is thought to degrade proteoglycan content of the intervertebral disc causing loss of glycosaminoglycan and water. This effect will cause the shrinkage of the disc and a reduction of the pressure on the nerve root.[A32701] | The median lethal dose of chymopapain in mice is registered to be 82 mg/kg and the toxicity mechanism was caused by hemorrhage due to the destruction of the cement substance in the blood vessels. When administered in an overdosage, chymopapain was able to nearly completely dissolve the nucleus pulposus and cause the disruption of the annulus fibrosus.[A32706] | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Bone marrow proteoglycan | NA | NA | NA | NA | NA | NA | NA | NA | NA | disodium;4,5-dihydroxybenzene-1,3-disulfonate | NA | Link | NA | NA |
| 13122 | Th1382 | Sutilain | NA | NA | NA | NA | NA | NA | This pharmacokinetic parameter is not relevant. | Sutilain is a member of the keratase family which includes agents such as papain. It is able to dissolve the intercellular matrix which helps with desquamation. Sutilain contains proteolytic enzymes derived from _Bacillus subtilis_ and it is available as a cream-colored odorless powder. One gram of sutilain powder contains 250,000 casein units of proteolytic activity.[T169] Sutilain was developed by Abbott and FDA approved on June 12, 1969. It is currently discontinued.[L2368] | Sutilain was indicated, in the form of an ointment, as a biochemical debridement of second and third-degree burns, incisional traumatic and pyrogenic wounds and ulcers occurring due to peripheral vascular diseases.[T169] | Reports indicated that sutilain exhibited a rapid and effective debridement when used for the treatment of burns, decubiti and traumatic wounds. In the case of peripheral vascular ulcerations, it did not respond in a predictable manner.[A32601] When used, sutilain caused a rapid dissolution of the surface of the treated skin zone. However, a graftable wound bed as achieved no more rapidly than if saline soaks had been used since the enzyme appears to be ineffective in removing deep dermal elements and necrotic fat.[L2383] | Sutilain is a proteolytic enzyme that dissolves necrotic tissue and hyaluronidase.[T170] | The toxicity has not been determined. | This pharmacokinetic parameter is not relevant. | Sutilain is not absorbed. | This pharmacokinetic parameter is not relevant. | This pharmacokinetic parameter is not relevant. | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13123 | Th1382 | Sutilain | NA | NA | NA | NA | NA | NA | This pharmacokinetic parameter is not relevant. | Sutilain is a member of the keratase family which includes agents such as papain. It is able to dissolve the intercellular matrix which helps with desquamation. Sutilain contains proteolytic enzymes derived from _Bacillus subtilis_ and it is available as a cream-colored odorless powder. One gram of sutilain powder contains 250,000 casein units of proteolytic activity.[T169] Sutilain was developed by Abbott and FDA approved on June 12, 1969. It is currently discontinued.[L2368] | Sutilain was indicated, in the form of an ointment, as a biochemical debridement of second and third-degree burns, incisional traumatic and pyrogenic wounds and ulcers occurring due to peripheral vascular diseases.[T169] | Reports indicated that sutilain exhibited a rapid and effective debridement when used for the treatment of burns, decubiti and traumatic wounds. In the case of peripheral vascular ulcerations, it did not respond in a predictable manner.[A32601] When used, sutilain caused a rapid dissolution of the surface of the treated skin zone. However, a graftable wound bed as achieved no more rapidly than if saline soaks had been used since the enzyme appears to be ineffective in removing deep dermal elements and necrotic fat.[L2383] | Sutilain is a proteolytic enzyme that dissolves necrotic tissue and hyaluronidase.[T170] | The toxicity has not been determined. | This pharmacokinetic parameter is not relevant. | Sutilain is not absorbed. | This pharmacokinetic parameter is not relevant. | This pharmacokinetic parameter is not relevant. | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13165 | Th1390 | Pancrelipase amylase | >Th1390_Pancrelipase_amylase MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL | 57086 | NA | 5.25-5.95 | NA | NA | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the elimination half-life is not relevant.10 | Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.[L2509] The amylases are enzymes that help in the chemical process of digestion by hydrolizing starch into more available saccharide forms.[T177] The pancrelipase amylase is a single polypeptide chain containing two SH groups and four disulfide bridges.[L2512] The pancrelipase mixture, including pancrelipase amylase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.[L2510] | The use of pancrelipase amylase is part of the pancreatic enzyme replacement therapy. This therapy is indicated for the treatment of pancreatic insufficiency attributed to cystic fibrosis, chronic pancreatitis or any other medically defined pancreatic disease that might require it. Pancreatic diseases are associated with the deterioration of pancreatic parenchyma and of the dual physiological functions of the pancreas. Once established, pancreatic insufficiency results in malnutrition, weight loss, and steatorrhea. | The major maldigestion/malabsorption problems arise from incomplete fat digestion. In clinical trials, the administration of pancrelipase as a mixture of amylase, lipase, and protease demonstrated a significant improvement in the coefficient of fat absorption and nitrogen absorption. These effects are accompanied by increased in body weight and body mass index. | The pancrelipase amylase acts by replacing the lack of physiological amylase. The amylase activity is done by the hydrolyzation of the alpha 1-4 linkages in the polysaccharides of three or more linked glucose units. The linkages alpha 1-6 are not hydrolyzed and thus, the starch is only reduced to lower molecule compounds.[L2512] | The studies of the toxicology of pancrelipase are not needed as this drug has been used clinically for a long time. Clinical overdose studies proved no effect on lungs, pancreas, liver and kidneys but it can produce symptoms such as diarrhea or stomach upset. Carcinogenicity studies have not shown any increased incidence with the use of pancrelipase. As pancrelipase is not absorbed, the effect on fetal development or reproduction is not expected. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the metabolism is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the volume of distribution is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the clearance rate is not relevant. | Enzymes | 8562981 | 22-10-2013 | 20-02-2028 | NA | Dietary starch | Cotazym Ecs 20 | Organon Canada Inc. | Organon Canada Inc. | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13166 | Th1390 | Pancrelipase amylase | >Th1390_Pancrelipase_amylase MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL | 57086 | NA | 5.25-5.95 | NA | NA | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the elimination half-life is not relevant.11 | Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.[L2509] The amylases are enzymes that help in the chemical process of digestion by hydrolizing starch into more available saccharide forms.[T177] The pancrelipase amylase is a single polypeptide chain containing two SH groups and four disulfide bridges.[L2512] The pancrelipase mixture, including pancrelipase amylase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.[L2510] | The use of pancrelipase amylase is part of the pancreatic enzyme replacement therapy. This therapy is indicated for the treatment of pancreatic insufficiency attributed to cystic fibrosis, chronic pancreatitis or any other medically defined pancreatic disease that might require it. Pancreatic diseases are associated with the deterioration of pancreatic parenchyma and of the dual physiological functions of the pancreas. Once established, pancreatic insufficiency results in malnutrition, weight loss, and steatorrhea. | The major maldigestion/malabsorption problems arise from incomplete fat digestion. In clinical trials, the administration of pancrelipase as a mixture of amylase, lipase, and protease demonstrated a significant improvement in the coefficient of fat absorption and nitrogen absorption. These effects are accompanied by increased in body weight and body mass index. | The pancrelipase amylase acts by replacing the lack of physiological amylase. The amylase activity is done by the hydrolyzation of the alpha 1-4 linkages in the polysaccharides of three or more linked glucose units. The linkages alpha 1-6 are not hydrolyzed and thus, the starch is only reduced to lower molecule compounds.[L2512] | The studies of the toxicology of pancrelipase are not needed as this drug has been used clinically for a long time. Clinical overdose studies proved no effect on lungs, pancreas, liver and kidneys but it can produce symptoms such as diarrhea or stomach upset. Carcinogenicity studies have not shown any increased incidence with the use of pancrelipase. As pancrelipase is not absorbed, the effect on fetal development or reproduction is not expected. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the metabolism is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the volume of distribution is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the clearance rate is not relevant. | Enzymes and Coenzymes | 8221747 | 17-07-2012 | 20-02-2028 | NA | Dietary starch | Cotazym Ecs 4 | Merck Ltd. | Merck Ltd. | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13213 | Th1391 | Pancrelipase protease | >Th1391_Pancrelipase_protease FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN | NA | NA | NA | NA | NA | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the elimination half-life is not relevant.58 | Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.[L2509] The amylases are enzymes that help in the chemical process of digestion by hydrolizing starch into more available saccharide forms.[T177] The pancrelipase amylase is a single polypeptide chain containing two SH groups and four disulfide bridges.[L2512] The pancrelipase mixture, including pancrelipase amylase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.[L2510] | The use of pancrelipase amylase is part of the pancreatic enzyme replacement therapy. This therapy is indicated for the treatment of pancreatic insufficiency attributed to cystic fibrosis, chronic pancreatitis or any other medically defined pancreatic disease that might require it. Pancreatic diseases are associated with the deterioration of pancreatic parenchyma and of the dual physiological functions of the pancreas. Once established, pancreatic insufficiency results in malnutrition, weight loss, and steatorrhea. | The major maldigestion/malabsorption problems arise from incomplete fat digestion. In clinical trials, the administration of pancrelipase as a mixture of amylase, lipase, and protease demonstrated a significant improvement in the coefficient of fat absorption and nitrogen absorption. These effects are accompanied by increased in body weight and body mass index. | The pancrelipase amylase acts by replacing the lack of physiological amylase. The amylase activity is done by the hydrolyzation of the alpha 1-4 linkages in the polysaccharides of three or more linked glucose units. The linkages alpha 1-6 are not hydrolyzed and thus, the starch is only reduced to lower molecule compounds.[L2512] | The studies of the toxicology of pancrelipase are not needed as this drug has been used clinically for a long time. Clinical overdose studies proved no effect on lungs, pancreas, liver and kidneys but it can produce symptoms such as diarrhea or stomach upset. Carcinogenicity studies have not shown any increased incidence with the use of pancrelipase. As pancrelipase is not absorbed, the effect on fetal development or reproduction is not expected. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the metabolism is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the volume of distribution is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the clearance rate is not relevant. | Enzymes | 9198871 | 01-12-2015 | 07-02-2030 | NA | Dietary protein | Bevitrol | Misemer Pharmaceutical | Misemer Pharmaceutical | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13214 | Th1391 | Pancrelipase protease | >Th1391_Pancrelipase_protease FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN | NA | NA | NA | NA | NA | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the elimination half-life is not relevant.59 | Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.[L2509] The amylases are enzymes that help in the chemical process of digestion by hydrolizing starch into more available saccharide forms.[T177] The pancrelipase amylase is a single polypeptide chain containing two SH groups and four disulfide bridges.[L2512] The pancrelipase mixture, including pancrelipase amylase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.[L2510] | The use of pancrelipase amylase is part of the pancreatic enzyme replacement therapy. This therapy is indicated for the treatment of pancreatic insufficiency attributed to cystic fibrosis, chronic pancreatitis or any other medically defined pancreatic disease that might require it. Pancreatic diseases are associated with the deterioration of pancreatic parenchyma and of the dual physiological functions of the pancreas. Once established, pancreatic insufficiency results in malnutrition, weight loss, and steatorrhea. | The major maldigestion/malabsorption problems arise from incomplete fat digestion. In clinical trials, the administration of pancrelipase as a mixture of amylase, lipase, and protease demonstrated a significant improvement in the coefficient of fat absorption and nitrogen absorption. These effects are accompanied by increased in body weight and body mass index. | The pancrelipase amylase acts by replacing the lack of physiological amylase. The amylase activity is done by the hydrolyzation of the alpha 1-4 linkages in the polysaccharides of three or more linked glucose units. The linkages alpha 1-6 are not hydrolyzed and thus, the starch is only reduced to lower molecule compounds.[L2512] | The studies of the toxicology of pancrelipase are not needed as this drug has been used clinically for a long time. Clinical overdose studies proved no effect on lungs, pancreas, liver and kidneys but it can produce symptoms such as diarrhea or stomach upset. Carcinogenicity studies have not shown any increased incidence with the use of pancrelipase. As pancrelipase is not absorbed, the effect on fetal development or reproduction is not expected. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the metabolism is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the volume of distribution is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the clearance rate is not relevant. | Enzymes and Coenzymes | 8562979 | 22-10-2013 | 20-02-2028 | NA | Dietary protein | Cotazym | Organon Canada Inc. | Organon Canada Inc. | Oral | NA | NA | Abnormal feces anxiety bloated feeling chills cold sweats confusion cool, pale skin depression excess air or gas in the stomach or intestines feeling of fullness fever frequent bowel movements loss of consciousness muscle aches nightmares passing gas runny nose seizures shakiness slurred speech sore throat | NA | NA | NA | NA | Link | Link | NA |
| 13268 | Th1392 | Thrombin | >Th1392_Thrombin MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS | NA | NA | NA | NA | NA | Unfortunately, little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155]. | Also known as coagulation factor II, thrombin is a serine protease that plays a physiological role in regulating hemostasis and maintaining blood coagulation. Once converted from prothrombin, thrombin converts fibrinogen to fibrin, which, in combination with platelets from the blood, forms a clot. Medical thrombin is a protein substance produced through a conversion reaction in which prothrombin of bovine origin is activated by tissue thromboplastin in the presence of calcium chloride. Thrombin requires no intermediate physiological agent for its action. It clots the fibrinogen of the blood directly. Failure to clot blood occurs in the rare case where the primary clotting defect is the absence of fibrinogen itself. Bovine thrombin however, is capable of causing fatal severe bleeding or thrombosis [FDA Label]. This thrombosis may result from the development of antibodies against bovine thrombin [FDA Label]. Bleeding may result from the development of antibodies against bovine factor V [FDA Label]. These antibodies may subsequently cross-react with endogenous human factor V and lead to its deficiency [FDA Label]. Patients who are know or suspected to have antibodies to bovine thrombin and/or bovine factor V should not be re-exposed to the product [FDA Label]. Patients who are administered bovine thrombin should be monitored for abnormal coagulation laboratory values, bleeding, or indeed, thrombosis [FDA Label]. A variety of human thrombin and recombinant thrombin (ie. thrombin alfa) products are available as alternatives to using bovine thrombin. | Bovine thrombin is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (like suture, ligature, or cautery) is ineffective or impractical [FDA Label]. Additionally, topical bovine thrombin can also be used in combination with an absorbable gelatin sponge, USP [FDA Label]. | Little has been reported about the systemic pharmacodynamics and pharmacokinetics of bovine thrombin preparations [T155], but it is expected that bovine thrombin elicits similar activities as endogenous thrombin. Subsequently, it is believed that bovine thrombin, like endogenous thrombin, functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, factor XIIIa catalyzes covalent bonds between lysine and glutamine residues that are found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Bovine thrombin requires no intermediate physiological agent for its action [FDA Label]. It activates platelets and catalyzes the conversion of fibrinogen to fibrin, which are essential steps for clot formation [FDA Label]. Failure to clot blood occurs in the case where the primary clotting defect is the absence of fibrinogen itself [FDA Label]. The speed with which the bovine thrombin clots blood is dependent upon the concentration of both the bovine thrombin and the fibrinogen present [FDA Label]. | With regards to bovine thrombin, no cases of overdose have been reported so far [T155]. Bovine thrombin however, is capable of causing fatal severe bleeding or thrombosis [FDA Label]. This thrombosis may result from the development of antibodies against bovine thrombin [FDA Label]. Bleeding may result from the development of antibodies against bovine factor V [FDA Label]. These antibodies may subsequently cross-react with endogenous human factor V and lead to its deficiency [FDA Label]. Patients who are know or suspected to have antibodies to bovine thrombin and/or bovine factor V should not be re-exposed to the product [FDA Label]. Patients who are administered bovine thrombin should be monitored for abnormal coagulation laboratory values, bleeding, or indeed, thrombosis [FDA Label]. LD50 values are available for rat and mouse models where rat subcutaneous LD50 > 40mg/kg, rat IP LD50 > 40mg/kg, and mouse subcutaneous LD50 > 50 mg/kg (in which the greater than symbol indicates that the toxicity endpoint being tested was not achievable at the highest dose used in the test) [MSDS]. Regardless, the most common adverse reactions following administration of bovine thrombin include hypersensitivity, bleeding, anemia, post-operative wound infection, thromboembolic events, hypotension, pyrexia, tachycardia, and/or thrombocytopenia [FDA Label]. | Although little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], such products are expected to be metabolized in the same way as endogenous thrombin is. Endogenous thrombin does not circulate in the blood as a free, active molecule for very long [L2079]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [L2079]. | Little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], but owing to its topical mode of administration, it is expected that any kind of systemic absorption would be minimal. | Little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], but owing to its topical mode of application, systemic exposure or distribution to other organs and tissues is not expected. | Although little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], it is expected that they are generally rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Enzymes | NA | NA | NA | NA | Proteinase-activated receptor 1,Proteinase-activated receptor 4,Coagulation factor XI,Coagulation factor XIII A chain,Coagulation factor XIII B chain,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain,Coagulation factor V,Coagulation factor VIII | NA | NA | NA | NA | NA | NA | NA | NA | NA | 7-iminophenothiazin-3-amine;hydrochloride | NA | Link | NA | NA |
| 13269 | Th1392 | Thrombin | >Th1392_Thrombin MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS | NA | NA | NA | NA | NA | Unfortunately, little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155]. | Also known as coagulation factor II, thrombin is a serine protease that plays a physiological role in regulating hemostasis and maintaining blood coagulation. Once converted from prothrombin, thrombin converts fibrinogen to fibrin, which, in combination with platelets from the blood, forms a clot. Medical thrombin is a protein substance produced through a conversion reaction in which prothrombin of bovine origin is activated by tissue thromboplastin in the presence of calcium chloride. Thrombin requires no intermediate physiological agent for its action. It clots the fibrinogen of the blood directly. Failure to clot blood occurs in the rare case where the primary clotting defect is the absence of fibrinogen itself. Bovine thrombin however, is capable of causing fatal severe bleeding or thrombosis [FDA Label]. This thrombosis may result from the development of antibodies against bovine thrombin [FDA Label]. Bleeding may result from the development of antibodies against bovine factor V [FDA Label]. These antibodies may subsequently cross-react with endogenous human factor V and lead to its deficiency [FDA Label]. Patients who are know or suspected to have antibodies to bovine thrombin and/or bovine factor V should not be re-exposed to the product [FDA Label]. Patients who are administered bovine thrombin should be monitored for abnormal coagulation laboratory values, bleeding, or indeed, thrombosis [FDA Label]. A variety of human thrombin and recombinant thrombin (ie. thrombin alfa) products are available as alternatives to using bovine thrombin. | Bovine thrombin is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (like suture, ligature, or cautery) is ineffective or impractical [FDA Label]. Additionally, topical bovine thrombin can also be used in combination with an absorbable gelatin sponge, USP [FDA Label]. | Little has been reported about the systemic pharmacodynamics and pharmacokinetics of bovine thrombin preparations [T155], but it is expected that bovine thrombin elicits similar activities as endogenous thrombin. Subsequently, it is believed that bovine thrombin, like endogenous thrombin, functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, factor XIIIa catalyzes covalent bonds between lysine and glutamine residues that are found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Bovine thrombin requires no intermediate physiological agent for its action [FDA Label]. It activates platelets and catalyzes the conversion of fibrinogen to fibrin, which are essential steps for clot formation [FDA Label]. Failure to clot blood occurs in the case where the primary clotting defect is the absence of fibrinogen itself [FDA Label]. The speed with which the bovine thrombin clots blood is dependent upon the concentration of both the bovine thrombin and the fibrinogen present [FDA Label]. | With regards to bovine thrombin, no cases of overdose have been reported so far [T155]. Bovine thrombin however, is capable of causing fatal severe bleeding or thrombosis [FDA Label]. This thrombosis may result from the development of antibodies against bovine thrombin [FDA Label]. Bleeding may result from the development of antibodies against bovine factor V [FDA Label]. These antibodies may subsequently cross-react with endogenous human factor V and lead to its deficiency [FDA Label]. Patients who are know or suspected to have antibodies to bovine thrombin and/or bovine factor V should not be re-exposed to the product [FDA Label]. Patients who are administered bovine thrombin should be monitored for abnormal coagulation laboratory values, bleeding, or indeed, thrombosis [FDA Label]. LD50 values are available for rat and mouse models where rat subcutaneous LD50 > 40mg/kg, rat IP LD50 > 40mg/kg, and mouse subcutaneous LD50 > 50 mg/kg (in which the greater than symbol indicates that the toxicity endpoint being tested was not achievable at the highest dose used in the test) [MSDS]. Regardless, the most common adverse reactions following administration of bovine thrombin include hypersensitivity, bleeding, anemia, post-operative wound infection, thromboembolic events, hypotension, pyrexia, tachycardia, and/or thrombocytopenia [FDA Label]. | Although little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], such products are expected to be metabolized in the same way as endogenous thrombin is. Endogenous thrombin does not circulate in the blood as a free, active molecule for very long [L2079]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [L2079]. | Little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], but owing to its topical mode of administration, it is expected that any kind of systemic absorption would be minimal. | Little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], but owing to its topical mode of application, systemic exposure or distribution to other organs and tissues is not expected. | Although little has been reported about the systemic pharmacokinetics of bovine thrombin preparations [T155], it is expected that they are generally rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Enzymes and Coenzymes | NA | NA | NA | NA | Proteinase-activated receptor 1,Proteinase-activated receptor 4,Coagulation factor XI,Coagulation factor XIII A chain,Coagulation factor XIII B chain,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain,Coagulation factor V,Coagulation factor VIII | NA | NA | NA | NA | NA | NA | NA | NA | NA | 7-iminophenothiazin-3-amine;hydrochloride | NA | Link | NA | NA |
| 13285 | Th1393 | Prothrombin | >Th1393_Prothrombin MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Approximately 60h [A19411]. | Prothrombin Complex Concentrate (Human), is indicated for the urgent reversal of acquired coagulation factor deficiency induced by Vitamin K antagonist (VKA, e.g., warfarin) therapy in adult patients with acute major bleeding. | For use in the emergency reversal of coagulation factor deficiency in patients receiving vitamin K antagonist therapy. Prothrombin is administered as part of a cocktail containing several coagulation factors. | NA | NA | NA | NA | NA | NA | NA | Enzyme Precursors | NA | NA | NA | NA | Fibrinogen alpha chain,Fibrinogen beta chain,Coagulation factor XIII A chain,Carboxypeptidase B2 | Octaplex | Octapharma Pharmazeutika Produktionsges M B H | Octapharma Pharmazeutika Produktionsges M B H | Intravenous | NA | NA | Immune system disorders; General disorders and administration site conditions; Vascular disorders; Nervous system disorders; | NA | NA | NA | NA | Link | Link | NA |
| 13286 | Th1393 | Prothrombin | >Th1393_Prothrombin MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Approximately 60h [A19411]. | Prothrombin Complex Concentrate (Human), is indicated for the urgent reversal of acquired coagulation factor deficiency induced by Vitamin K antagonist (VKA, e.g., warfarin) therapy in adult patients with acute major bleeding. | For use in the emergency reversal of coagulation factor deficiency in patients receiving vitamin K antagonist therapy. Prothrombin is administered as part of a cocktail containing several coagulation factors. | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Fibrinogen alpha chain,Fibrinogen beta chain,Coagulation factor XIII A chain,Carboxypeptidase B2 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13298 | Th1394 | Protein C | NA | NA | NA | NA | NA | NA | Initial half life = 7.8 hr, Terminal half life = 9.9 hr | Protein C is an endogenously occurring plasma protein that plays a key role within the coagulation cascade. Protein C is a zymogen, or enzyme precursor, of a vitamin K-dependent anticoagulant glycoprotein (serine protease) that is synthesized in the liver. It is converted by the thrombin/thrombomodulin-complex on the endothelial cell surface to Activated Protein C (APC). Once in its activated form, APC functions as a serine protease with potent anticoagulant effects, especially in the presence of its cofactor protein S. APC exerts its effect by inactivating essential components of the coagulation cascade (specifically factors V and VIII), which leads to a decrease in thrombin formation, and therefore a reduction in clot formation. The Protein C pathway provides a natural mechanism for control of the coagulation system and prevention of excessive procoagulant responses to activating stimuli. A lack of protein C in the body would lead to unchecked coagulation activation, resulting in thrombin generation and intravascular clot formation. Protein C is available in concentrated form as the product Ceprotin, which is indicated for use in pediatric and adult patients with severe congenital protein C deficiency for the prevention and treatment of venous thrombosis and purpura fulminans. | Protein C concentrate is indicated for pediatric and adult patients with severe congenital protein C deficiency for the prevention and treatment of venous thrombosis and purpura fulminans.[L12831] It is also found as a component of some prothrombin complex concentrate (i.e. [Factor IX Complex (Human)]) formulations, such as Kcentra.[L12834] | In clinical studies, the intravenous administration of Protein C Concentrate demonstrated a temporary increase, within approximately half an hour of administration, in plasma levels of APC. Replacement of protein C in protein C-deficient patients is expected to control or, if given prophylactically, to prevent thrombotic complications.[L12831] | Protein C is an endogenously occurring plasma protein that plays a key role within the coagulation cascade. Also known as blood coagulation factor XIV, Protein C is a zymogen, or enzyme precursor, of a vitamin K-dependent anticoagulant glycoprotein (serine protease) that is synthesized in the liver. It is converted by the thrombin/thrombomodulin-complex on the endothelial cell surface to Activated Protein C (APC). Once in its activated form, APC functions as a serine protease with potent anticoagulant effects, especially in the presence of its cofactor protein S. APC exerts its effect by inactivating essential components of the coagulation cascade (specifically factors V and VIII), which leads to a decrease in thrombin formation, and therefore a reduction in clot formation. | NA | NA | Cmax = 110 IU/dL Tmax = 0.50 hr | Volume of distribution at steady state = 0.74 dL/kg | CL = 0.0533 dL/kg/h | Enzyme Precursors | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII | Octaplex | Octapharma Pharmazeutika Produktionsges M B H | Octapharma Pharmazeutika Produktionsges M B H | Intravenous | NA | NA | Immune system disorders; General disorders and administration site conditions; Vascular disorders; Nervous system disorders; | NA | NA | NA | NA | Link | Link | NA |
| 13299 | Th1394 | Protein C | NA | NA | NA | NA | NA | NA | Initial half life = 7.8 hr, Terminal half life = 9.9 hr | Protein C is an endogenously occurring plasma protein that plays a key role within the coagulation cascade. Protein C is a zymogen, or enzyme precursor, of a vitamin K-dependent anticoagulant glycoprotein (serine protease) that is synthesized in the liver. It is converted by the thrombin/thrombomodulin-complex on the endothelial cell surface to Activated Protein C (APC). Once in its activated form, APC functions as a serine protease with potent anticoagulant effects, especially in the presence of its cofactor protein S. APC exerts its effect by inactivating essential components of the coagulation cascade (specifically factors V and VIII), which leads to a decrease in thrombin formation, and therefore a reduction in clot formation. The Protein C pathway provides a natural mechanism for control of the coagulation system and prevention of excessive procoagulant responses to activating stimuli. A lack of protein C in the body would lead to unchecked coagulation activation, resulting in thrombin generation and intravascular clot formation. Protein C is available in concentrated form as the product Ceprotin, which is indicated for use in pediatric and adult patients with severe congenital protein C deficiency for the prevention and treatment of venous thrombosis and purpura fulminans. | Protein C concentrate is indicated for pediatric and adult patients with severe congenital protein C deficiency for the prevention and treatment of venous thrombosis and purpura fulminans.[L12831] It is also found as a component of some prothrombin complex concentrate (i.e. [Factor IX Complex (Human)]) formulations, such as Kcentra.[L12834] | In clinical studies, the intravenous administration of Protein C Concentrate demonstrated a temporary increase, within approximately half an hour of administration, in plasma levels of APC. Replacement of protein C in protein C-deficient patients is expected to control or, if given prophylactically, to prevent thrombotic complications.[L12831] | Protein C is an endogenously occurring plasma protein that plays a key role within the coagulation cascade. Also known as blood coagulation factor XIV, Protein C is a zymogen, or enzyme precursor, of a vitamin K-dependent anticoagulant glycoprotein (serine protease) that is synthesized in the liver. It is converted by the thrombin/thrombomodulin-complex on the endothelial cell surface to Activated Protein C (APC). Once in its activated form, APC functions as a serine protease with potent anticoagulant effects, especially in the presence of its cofactor protein S. APC exerts its effect by inactivating essential components of the coagulation cascade (specifically factors V and VIII), which leads to a decrease in thrombin formation, and therefore a reduction in clot formation. | NA | NA | Cmax = 110 IU/dL Tmax = 0.50 hr | Volume of distribution at steady state = 0.74 dL/kg | CL = 0.0533 dL/kg/h | Enzymes | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13300 | Th1394 | Protein C | NA | NA | NA | NA | NA | NA | Initial half life = 7.8 hr, Terminal half life = 9.9 hr | Protein C is an endogenously occurring plasma protein that plays a key role within the coagulation cascade. Protein C is a zymogen, or enzyme precursor, of a vitamin K-dependent anticoagulant glycoprotein (serine protease) that is synthesized in the liver. It is converted by the thrombin/thrombomodulin-complex on the endothelial cell surface to Activated Protein C (APC). Once in its activated form, APC functions as a serine protease with potent anticoagulant effects, especially in the presence of its cofactor protein S. APC exerts its effect by inactivating essential components of the coagulation cascade (specifically factors V and VIII), which leads to a decrease in thrombin formation, and therefore a reduction in clot formation. The Protein C pathway provides a natural mechanism for control of the coagulation system and prevention of excessive procoagulant responses to activating stimuli. A lack of protein C in the body would lead to unchecked coagulation activation, resulting in thrombin generation and intravascular clot formation. Protein C is available in concentrated form as the product Ceprotin, which is indicated for use in pediatric and adult patients with severe congenital protein C deficiency for the prevention and treatment of venous thrombosis and purpura fulminans. | Protein C concentrate is indicated for pediatric and adult patients with severe congenital protein C deficiency for the prevention and treatment of venous thrombosis and purpura fulminans.[L12831] It is also found as a component of some prothrombin complex concentrate (i.e. [Factor IX Complex (Human)]) formulations, such as Kcentra.[L12834] | In clinical studies, the intravenous administration of Protein C Concentrate demonstrated a temporary increase, within approximately half an hour of administration, in plasma levels of APC. Replacement of protein C in protein C-deficient patients is expected to control or, if given prophylactically, to prevent thrombotic complications.[L12831] | Protein C is an endogenously occurring plasma protein that plays a key role within the coagulation cascade. Also known as blood coagulation factor XIV, Protein C is a zymogen, or enzyme precursor, of a vitamin K-dependent anticoagulant glycoprotein (serine protease) that is synthesized in the liver. It is converted by the thrombin/thrombomodulin-complex on the endothelial cell surface to Activated Protein C (APC). Once in its activated form, APC functions as a serine protease with potent anticoagulant effects, especially in the presence of its cofactor protein S. APC exerts its effect by inactivating essential components of the coagulation cascade (specifically factors V and VIII), which leads to a decrease in thrombin formation, and therefore a reduction in clot formation. | NA | NA | Cmax = 110 IU/dL Tmax = 0.50 hr | Volume of distribution at steady state = 0.74 dL/kg | CL = 0.0533 dL/kg/h | Enzymes and Coenzymes | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13313 | Th1395 | Insulin peglispro | NA | NA | NA | NA | NA | NA | NA | 0 | NA | NA | NA | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inducers | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13329 | Th1396 | Insulin tregopil | NA | NA | NA | NA | NA | NA | NA | 0 | `code text here` | NA | NA | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inducers | NA | NA | NA | NA | Insulin receptor,Insulin-like growth factor 1 receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | (4S)-4-[[2-[[(1R,6R,12S,15S,18S,21S,24S,27S,30S,33S,36S,39S,42R,47R,50S,53S,56S,59S,62S,65S,68S,71S,74R,77S,80S,83S,88R)-88-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[(2-aminoacetyl)amino]-3-methylpentanoyl]amino]-3-methylbutanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]-6-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]-4-oxobutanoyl]amino]-5-oxopentanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-4-methylpentanoyl]amino]-47-[[(1S)-3-amino-1-carboxy-3-oxopropyl]carbamoyl]-53-(2-amino-2-oxoethyl)-62-(3-amino-3-oxopropyl)-77-[(2S)-butan-2-yl]-24,56-bis(2-carboxyethyl)-83-[(1R)-1-hydroxyethyl]-12,71,80-tris(hydroxymethyl)-33,50,65-tris[(4-hydroxyphenyl)methyl]-15-(1H-imidazol-4-ylmethyl)-27-methyl-18,30,36,59,68-pentakis(2-methylpropyl)-7,10,13,16,19,22,25,28,31,34,37,40,49,52,55,58,61,64,67,70,73,76,79,82,85,87-hexacosaoxo-21,39-di(propan-2-yl)-3,4,44,45,90,91-hexathia-8,11,14,17,20,23,26,29,32,35,38,41,48,51,54,57,60,63,66,69,72,75,78,81,84,86-hexacosazabicyclo[72.11.7]dononacontane-42-carbonyl]amino]acetyl]amino]-5-[[(2S)-5-carbamimidamido-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[(2S)-2-[[(2S)-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-6-[3-[2-[2-(2-methoxyethoxy)ethoxy]ethoxy]propanoylamino]-1-oxohexan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]amino]-1-oxopentan-2-yl]amino]-5-oxopentanoic acid | NA | Link | NA | NA |
| 13366 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Enzymes | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | Baxter Laboratories | Baxter Laboratories | Topical | 6000 unit / vial | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |
| 13367 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Enzymes and Coenzymes | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13417 | Th1402 | Eftrenonacog alfa | NA | 98000 | NA | NA | NA | NA | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean terminal half life (t1/2) was 77.6 hours [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, the mean t1/2 ranged from 66.49 to 82.22 hours [FDA Label]. | Eftrenonacog alfa is a long-acting recombinant fusion protein used in the treatment of hemophilia B. It is comprised of a single molecule of human factor IX (FIX) covalently linked to the constant region (Fc) domain of human IgG1 via recombinant DNA technology in a human embryonic kidney cell line (HEK293H) [A31556]. The presence of the Fc domain extends the terminal half-life which confers clinical benefits of prolonged therapeutic efficacy, less frequent intravenous injections for patient convenience and improved adherence to prophylaxis. Hemophilia B is a blood disorder with an incidence of approximately once every 30,000 male births in all populations and ethnic groups [A31557]. It is an X-linked genetic disease caused by mutation of the gene for coagulation protein factor IX (FIX), leading to decreased levels of endogenous factor IX and increased susceptibility to recurrent bleeding episodes caused spontaneously or as a result of accidental or surgical trauma [FDA Label]. When untreated, most patients die from bleeding complications before 25 years of age [A31557]. Eftrenonacog alfa acts as a replacement therapy to restore the levels of factor IX and allow normal hemostasis. Eftrenonacog alfa was developed and marketed as Alprolix for intravenous injection by Biogen. It was first approved by the FDA in March 2014 and later approved by the EMA in May 2016. Eftrenonacog alfa treatment demonstrated good tolerability with no reports of inhibitor development in clinical studies [A31556]. | Indicated for the treatment and prophylaxis of bleeding in patients of all age with haemophilia B (congenital factor IX deficiency). | In two multinational, phase III studies in previously treated children, adolescents and adults with severe haemophilia B, eftrenonacog alfa prophylaxis resulted in low median annualized bleeding rates (ABRs), and was associated with reductions in median weekly factor consumption and dosing frequency compared with pre-study FIX regimens. The extension of those studies demonstrated effectiveness in the treatment of bleeding episodes and when used in the perioperative setting in all age groups [A31556]. In animal models, a single intravenous dose of eftrenonacog alfa displayed half values approximately three- to four-fold longer than those seen with recombinant FIX [A31556]. | The coagulation protein factor IX (FIX) is a vitamin K-dependent coagulation factor and one of the critical serine proteases involved in the coagulation cascade. Upon activation by factor XIa in the intrinsic coagulation pathway and by the factor VII/tissue factor complex in the extrinsic pathway, factor IX, in combination with factor VIII, activates factor X. Activated factor X mediates the conversion of prothrombin to thrombin which sequentially leads to thrombin converting fibrinogen into fibrin. A blood clot is then formed [FDA Label]. With a mutation in the gene encoding the coagulation protein factor IX (FIX), patients with hemophilia B have factor IX deficiency and are at high risk for recurrent bleeding episodes. Eftrenonacog alfa is composed of a single molecule of recombinant FIX (rFIX) covalently fused to the dimeric Fc domain of immunoglobulin (Ig) G1 (rFIXFc). It serves as a replacement therapy to increase the plasma levels of factor IX thereby enabling a temporary correction of the factor deficiency and correction of the bleeding tendencies [FDA Label]. The Fc region of human immunoglobulin G1 binds with the neonatal Fc receptor which is expressed throughout life as part of a naturally occurring pathway that protects immunoglobulins from lysosomal degradation by cycling these proteins back into circulation, resulting in their long plasma half-life. The binding of eftrenonacog alfa to the neonatal Fc receptor delays degradation and recycles the fusion protein back into circulation for increased plasma half life and prolonged therapeutic action [FDA Label, A31557]. | Based on findings from a rabbit thrombogenicity test and rat or monkey repeated-dose toxicity studies, eftrenonacog alfa displays no special hazards for humans. Studies to investigate the genotoxicity, carcinogenicity, toxicity to reproduction or embryo-foetal development have not been conducted. Eftrenonacog alfa has shown to cross the placenta in small amounts according to a mouse placental transfer study [FDA Label]. | The Fc domain of eftrenonacog alfa is expected to undergo lysosomal degradation while the remaining recombinant FIX (rFIX) portion is expected to be metabolized by the same pathway as endogenous factor IX. | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean peak plasma concentration (Cmax) was 46.10 IU/dL [FDA Label]. The mean area under the FIX activity time curve (AUC) was 31.58 Uxh/dL per IU/kg [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, the mean AUC ranged from 22.71 to 29.50 Uxh/dL per IU/kg [FDA Label]. | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean volume of distribution at steady-state (Vss) was 303.4 mL/kg [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, the mean Vss ranged from 289 to 365.1 mL/kg [FDA Label]. | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean clearance (CL) was 3.17 mL/h/kg [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, mean CL ranged from 3.390 to 4.365 mL/h/kg [FDA Label]. | Enzyme Precursors | NA | NA | NA | NA | NA | Alprolix | Bioverativ Therapeutics Inc. | Bioverativ Therapeutics Inc. | Intravenous | 250 [iU]/5mL | ALPROLIX™ is contraindicated in individuals who have a known history of hypersensitivity reactions, including anaphylaxis, to the product or its excipients | headache, numbness and tingling sensation in the mouth, dizziness, changes in the sense of taste, breath odor, fatigue, injection site pain, heart palpitations, difficulty urinating, and low blood pressure (hypotension). | Alprolix is an injectable medicine that is used to help control and prevent bleeding in people with hemophilia B. Hemophilia B is also called congenital Factor IX deficiency. Your healthcare provider may give you Alprolix when you have surgery. | Alprolix [Coagulation Factor IX (Recombinant), Fc Fusion Protein] is a recombinant DNA derived, coagulation Factor IX concentrate indicated in adults and children with hemophilia B (congenital Factor IX deficiency) to control and prevent bleeding episodes, for perioperative management, and for routine prophylaxis to prevent or reduce the frequency of bleeding episodes. Alprolix is not indicated for induction of immune tolerance in patients with hemophilia B. | NA | NA | Link | Link | NA |
| 13418 | Th1402 | Eftrenonacog alfa | NA | 98000 | NA | NA | NA | NA | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean terminal half life (t1/2) was 77.6 hours [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, the mean t1/2 ranged from 66.49 to 82.22 hours [FDA Label]. | Eftrenonacog alfa is a long-acting recombinant fusion protein used in the treatment of hemophilia B. It is comprised of a single molecule of human factor IX (FIX) covalently linked to the constant region (Fc) domain of human IgG1 via recombinant DNA technology in a human embryonic kidney cell line (HEK293H) [A31556]. The presence of the Fc domain extends the terminal half-life which confers clinical benefits of prolonged therapeutic efficacy, less frequent intravenous injections for patient convenience and improved adherence to prophylaxis. Hemophilia B is a blood disorder with an incidence of approximately once every 30,000 male births in all populations and ethnic groups [A31557]. It is an X-linked genetic disease caused by mutation of the gene for coagulation protein factor IX (FIX), leading to decreased levels of endogenous factor IX and increased susceptibility to recurrent bleeding episodes caused spontaneously or as a result of accidental or surgical trauma [FDA Label]. When untreated, most patients die from bleeding complications before 25 years of age [A31557]. Eftrenonacog alfa acts as a replacement therapy to restore the levels of factor IX and allow normal hemostasis. Eftrenonacog alfa was developed and marketed as Alprolix for intravenous injection by Biogen. It was first approved by the FDA in March 2014 and later approved by the EMA in May 2016. Eftrenonacog alfa treatment demonstrated good tolerability with no reports of inhibitor development in clinical studies [A31556]. | Indicated for the treatment and prophylaxis of bleeding in patients of all age with haemophilia B (congenital factor IX deficiency). | In two multinational, phase III studies in previously treated children, adolescents and adults with severe haemophilia B, eftrenonacog alfa prophylaxis resulted in low median annualized bleeding rates (ABRs), and was associated with reductions in median weekly factor consumption and dosing frequency compared with pre-study FIX regimens. The extension of those studies demonstrated effectiveness in the treatment of bleeding episodes and when used in the perioperative setting in all age groups [A31556]. In animal models, a single intravenous dose of eftrenonacog alfa displayed half values approximately three- to four-fold longer than those seen with recombinant FIX [A31556]. | The coagulation protein factor IX (FIX) is a vitamin K-dependent coagulation factor and one of the critical serine proteases involved in the coagulation cascade. Upon activation by factor XIa in the intrinsic coagulation pathway and by the factor VII/tissue factor complex in the extrinsic pathway, factor IX, in combination with factor VIII, activates factor X. Activated factor X mediates the conversion of prothrombin to thrombin which sequentially leads to thrombin converting fibrinogen into fibrin. A blood clot is then formed [FDA Label]. With a mutation in the gene encoding the coagulation protein factor IX (FIX), patients with hemophilia B have factor IX deficiency and are at high risk for recurrent bleeding episodes. Eftrenonacog alfa is composed of a single molecule of recombinant FIX (rFIX) covalently fused to the dimeric Fc domain of immunoglobulin (Ig) G1 (rFIXFc). It serves as a replacement therapy to increase the plasma levels of factor IX thereby enabling a temporary correction of the factor deficiency and correction of the bleeding tendencies [FDA Label]. The Fc region of human immunoglobulin G1 binds with the neonatal Fc receptor which is expressed throughout life as part of a naturally occurring pathway that protects immunoglobulins from lysosomal degradation by cycling these proteins back into circulation, resulting in their long plasma half-life. The binding of eftrenonacog alfa to the neonatal Fc receptor delays degradation and recycles the fusion protein back into circulation for increased plasma half life and prolonged therapeutic action [FDA Label, A31557]. | Based on findings from a rabbit thrombogenicity test and rat or monkey repeated-dose toxicity studies, eftrenonacog alfa displays no special hazards for humans. Studies to investigate the genotoxicity, carcinogenicity, toxicity to reproduction or embryo-foetal development have not been conducted. Eftrenonacog alfa has shown to cross the placenta in small amounts according to a mouse placental transfer study [FDA Label]. | The Fc domain of eftrenonacog alfa is expected to undergo lysosomal degradation while the remaining recombinant FIX (rFIX) portion is expected to be metabolized by the same pathway as endogenous factor IX. | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean peak plasma concentration (Cmax) was 46.10 IU/dL [FDA Label]. The mean area under the FIX activity time curve (AUC) was 31.58 Uxh/dL per IU/kg [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, the mean AUC ranged from 22.71 to 29.50 Uxh/dL per IU/kg [FDA Label]. | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean volume of distribution at steady-state (Vss) was 303.4 mL/kg [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, the mean Vss ranged from 289 to 365.1 mL/kg [FDA Label]. | Following administration of a single intravenous dose of 50 IU/kg of eftrenonacog alfa in patients =19 years of age with hemophilia B, the mean clearance (CL) was 3.17 mL/h/kg [FDA Label]. In pediatric and adolescent patients (< 18 years of age) receiving the same dose, mean CL ranged from 3.390 to 4.365 mL/h/kg [FDA Label]. | Enzymes and Coenzymes | NA | NA | NA | NA | NA | Alprolix | Bioverativ Therapeutics Inc. | Bioverativ Therapeutics Inc. | Intravenous | 4000 [iU]/5mL | ALPROLIX™ is contraindicated in individuals who have a known history of hypersensitivity reactions, including anaphylaxis, to the product or its excipients | headache, numbness and tingling sensation in the mouth, dizziness, changes in the sense of taste, breath odor, fatigue, injection site pain, heart palpitations, difficulty urinating, and low blood pressure (hypotension). | Alprolix is an injectable medicine that is used to help control and prevent bleeding in people with hemophilia B. Hemophilia B is also called congenital Factor IX deficiency. Your healthcare provider may give you Alprolix when you have surgery. | Alprolix [Coagulation Factor IX (Recombinant), Fc Fusion Protein] is a recombinant DNA derived, coagulation Factor IX concentrate indicated in adults and children with hemophilia B (congenital Factor IX deficiency) to control and prevent bleeding episodes, for perioperative management, and for routine prophylaxis to prevent or reduce the frequency of bleeding episodes. Alprolix is not indicated for induction of immune tolerance in patients with hemophilia B. | NA | NA | Link | Link | NA |
| 13476 | Th1407 | Recombinant Cholera Toxin B Subunit | >Th1407_Recombinant_Cholera_Toxin_B_Subunit MIKLKFGVFFTVLLSSAYAHGTPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN | NA | NA | NA | NA | NA | NA | Recombinant Cholera Toxin B Subunit is an ingredient in the EMA-authorised product Dukoral. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13477 | Th1407 | Recombinant Cholera Toxin B Subunit | >Th1407_Recombinant_Cholera_Toxin_B_Subunit MIKLKFGVFFTVLLSSAYAHGTPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN | NA | NA | NA | NA | NA | NA | Recombinant Cholera Toxin B Subunit is an ingredient in the EMA-authorised product Dukoral. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13511 | Th1411 | Rusalatide acetate | NA | NA | NA | NA | NA | NA | NA | Chrysalin has been used in trials studying the treatment of Radius Fracture. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | acetic acid;(4S)-5-[[2-[[(2S)-6-amino-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2R)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[2-[[2-[(2S)-2-[[(2S)-1-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-oxoethyl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-2-oxoethyl]amino]-4-[[(2S)-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[2-[[(2S)-2-aminopropanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-3-carboxypropanoyl]amino]-5-oxopentanoic acid | NA | Link | NA | NA |
| 13512 | Th1411 | Rusalatide acetate | NA | NA | NA | NA | NA | NA | NA | Chrysalin has been used in trials studying the treatment of Radius Fracture. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | acetic acid;(4S)-5-[[2-[[(2S)-6-amino-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2R)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[2-[[2-[(2S)-2-[[(2S)-1-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-oxoethyl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-2-oxoethyl]amino]-4-[[(2S)-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[2-[[(2S)-2-aminopropanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-3-carboxypropanoyl]amino]-5-oxopentanoic acid | NA | Link | NA | NA |
| 13540 | Th1414 | Vonapanitase | NA | NA | NA | NA | NA | NA | NA | Vonapanitase is under investigation for the treatment of Chronic Kidney Disease. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13541 | Th1414 | Vonapanitase | NA | NA | NA | NA | NA | NA | NA | Vonapanitase is under investigation for the treatment of Chronic Kidney Disease. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13633 | Th1420 | Sarilumab | >Th1420_Sarilumab EVQLVESGGGLVQPGRSLRLSCAASRFTFDDYAMHWVRQAPGKGLEWVSGISWNSGRIGYADSVKGRFTISRDNAENSLFLQMNGLRAEDTALYYCAKGRDSFDIWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK | 150000 | C6388H9918N1718O1998S44 | 6.6 - 7.2 | NA | 69 °C (midpoint transition), 80 °C (whole IgG1) | The half life will depend on the administered concentration. At 200 mg every 2 weeks, half-life is up to 10 days in patients with RA at steady state. At 150 mg every 2 weeks, half-life is up to 8 days in patients with RA at steady state. After the last steady state dose of 150 mg and 200 mg, the time to reach nondetectable concentration is 28 and 43 days, respectively [L1000]. | Sarilumab is a fully human anti-IL-6R monoclonal IgG1 antibody that binds to both membrane bound and soluble interleukin 6 (IL-6) receptor forms, thus blocking the cis- and trans-inflammatory signalling cascades of IL-6 [A27262]. Sarilumab was developped by Sanofi and Regeneron Pharmaceuticals, Inc; it was US FDA-approved in May 2017 and followed by EU approval in June 2017 for the treatment of moderate to severe Rheumatoid Arthritis (RA) in combination with methotrexate [A27265]. RA is a chronic inflammatory disease characterized by polyarthritis and its treatment has been challenged by the different response in every patient [A27264]. Subcutaneous administration of Sarilumab has been shown to decrease acute-phase reactant levels and improve in clinical RA symptoms [A27263]. | Indicated for modere to severe reactive RA in adult patients who are irresponsive, respond inadequately or present intolerance to disease-modifying anti-rheumatic drugs (DMARDs) or tumor necrosis factor (TNF) antagonists. It is indicated to be used in combination with methotrexate (MTX) or as a monotherapy when there is intolerance to MTX or MTX administration is inappropriate. | Single-dose subcutaneous administration of Sarilumab produced a rapid reduction of CRP levels, leading to normal levels after two weeks of treatment. Peak reduction in the absolute neutrophile count was observed after 3 to 4 days of treatment followed by a recovery to baseline levels. It is observed a decrease in fibrinogen and serum amyloid A as well as an increase in hemoglobin and serum albumin. | Sarilumab is a human recombinant IgG1 antibody that binds to both forms of interleukin 6 receptors (IL-6R), thus inhibiting the IL-6-mediated signaling. IL-6 is known to be a pleiotropic cytokine that activates immune cells (T and B cells), as well as hepatocytes for the release of acute phase proteins like CRP, serum amyloid A and fibrinogen which are biomarkers of RA activity. IL-6 is also found in synovial fluid and plays a major role in the pathological inflammation and joint destruction features of RA. Thus, it is used for the treatment of RA due to its ability to inhibit intra-articular and systemic IL-6 signaling [L1000, L1001, FDA file]. | Repeat dose exposure has been shown to produce a partially reversible decrease in neutophil count and a reversible decrease in fibrinogen [L1000]. | The metabolism of Sarilumab has not been characterized. As it is a monoclonal antibody, It is thought to be degraded into small peptides and amino acids [FDA file]. | Sarilumab is shown to be well absorbed in RA patients after single SC administration with a maximum of serum concentration presented after 2 to 4 days. For the 150 mg every two weeks dose regimen, the AUC, Cmin and Cmax of sarilumab were 202 ± 120 mg.day/L, 6.35 ± 7.54 mg/L, and 20.0 ± 9.20 mg/L, respectively. For the 200 mg every two weeks dose regimen, the AUC, Cmin and Cmax of sarilumab were 395 ± 207 mg.day/L, 16.5 ± 14.1 mg/L, and 35.6 ± 15.2 mg/L, respectively [L1001, FDA file]. | In patients with RA, the apparent volume of distribution at steady state was 7.3 L [L1001, FDA file]. | Sarilumab is not eliminated via renal or hepatic pathways. RA patients have shown a trend toward higher clearance in presence of anti-sarilumab antibodies [FDA file]. | Cytochrome P-450 Enzyme Inducers | NA | NA | NA | NA | Interleukin-6 receptor subunit alpha,High affinity immunoglobulin gamma Fc receptor I,Low affinity immunoglobulin gamma Fc region receptor II-a,Low affinity immunoglobulin gamma Fc region receptor II-b,Low affinity immunoglobulin gamma Fc region receptor III-A,Low affinity immunoglobulin gamma Fc region receptor III-B | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13634 | Th1420 | Sarilumab | >Th1420_Sarilumab EVQLVESGGGLVQPGRSLRLSCAASRFTFDDYAMHWVRQAPGKGLEWVSGISWNSGRIGYADSVKGRFTISRDNAENSLFLQMNGLRAEDTALYYCAKGRDSFDIWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK | 150000 | C6388H9918N1718O1998S44 | 6.6 - 7.2 | NA | 69 °C (midpoint transition), 80 °C (whole IgG1) | The half life will depend on the administered concentration. At 200 mg every 2 weeks, half-life is up to 10 days in patients with RA at steady state. At 150 mg every 2 weeks, half-life is up to 8 days in patients with RA at steady state. After the last steady state dose of 150 mg and 200 mg, the time to reach nondetectable concentration is 28 and 43 days, respectively [L1000]. | Sarilumab is a fully human anti-IL-6R monoclonal IgG1 antibody that binds to both membrane bound and soluble interleukin 6 (IL-6) receptor forms, thus blocking the cis- and trans-inflammatory signalling cascades of IL-6 [A27262]. Sarilumab was developped by Sanofi and Regeneron Pharmaceuticals, Inc; it was US FDA-approved in May 2017 and followed by EU approval in June 2017 for the treatment of moderate to severe Rheumatoid Arthritis (RA) in combination with methotrexate [A27265]. RA is a chronic inflammatory disease characterized by polyarthritis and its treatment has been challenged by the different response in every patient [A27264]. Subcutaneous administration of Sarilumab has been shown to decrease acute-phase reactant levels and improve in clinical RA symptoms [A27263]. | Indicated for modere to severe reactive RA in adult patients who are irresponsive, respond inadequately or present intolerance to disease-modifying anti-rheumatic drugs (DMARDs) or tumor necrosis factor (TNF) antagonists. It is indicated to be used in combination with methotrexate (MTX) or as a monotherapy when there is intolerance to MTX or MTX administration is inappropriate. | Single-dose subcutaneous administration of Sarilumab produced a rapid reduction of CRP levels, leading to normal levels after two weeks of treatment. Peak reduction in the absolute neutrophile count was observed after 3 to 4 days of treatment followed by a recovery to baseline levels. It is observed a decrease in fibrinogen and serum amyloid A as well as an increase in hemoglobin and serum albumin. | Sarilumab is a human recombinant IgG1 antibody that binds to both forms of interleukin 6 receptors (IL-6R), thus inhibiting the IL-6-mediated signaling. IL-6 is known to be a pleiotropic cytokine that activates immune cells (T and B cells), as well as hepatocytes for the release of acute phase proteins like CRP, serum amyloid A and fibrinogen which are biomarkers of RA activity. IL-6 is also found in synovial fluid and plays a major role in the pathological inflammation and joint destruction features of RA. Thus, it is used for the treatment of RA due to its ability to inhibit intra-articular and systemic IL-6 signaling [L1000, L1001, FDA file]. | Repeat dose exposure has been shown to produce a partially reversible decrease in neutophil count and a reversible decrease in fibrinogen [L1000]. | The metabolism of Sarilumab has not been characterized. As it is a monoclonal antibody, It is thought to be degraded into small peptides and amino acids [FDA file]. | Sarilumab is shown to be well absorbed in RA patients after single SC administration with a maximum of serum concentration presented after 2 to 4 days. For the 150 mg every two weeks dose regimen, the AUC, Cmin and Cmax of sarilumab were 202 ± 120 mg.day/L, 6.35 ± 7.54 mg/L, and 20.0 ± 9.20 mg/L, respectively. For the 200 mg every two weeks dose regimen, the AUC, Cmin and Cmax of sarilumab were 395 ± 207 mg.day/L, 16.5 ± 14.1 mg/L, and 35.6 ± 15.2 mg/L, respectively [L1001, FDA file]. | In patients with RA, the apparent volume of distribution at steady state was 7.3 L [L1001, FDA file]. | Sarilumab is not eliminated via renal or hepatic pathways. RA patients have shown a trend toward higher clearance in presence of anti-sarilumab antibodies [FDA file]. | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | Interleukin-6 receptor subunit alpha,High affinity immunoglobulin gamma Fc receptor I,Low affinity immunoglobulin gamma Fc region receptor II-a,Low affinity immunoglobulin gamma Fc region receptor II-b,Low affinity immunoglobulin gamma Fc region receptor III-A,Low affinity immunoglobulin gamma Fc region receptor III-B | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13960 | Th1451 | Ulinastatin | NA | NA | NA | NA | NA | NA | NA | Ulinastatin has been investigated for the prevention of Cardiovascular Disease and Adverse Reaction to Drug. | NA | NA | NA | NA | NA | NA | NA | NA | Enzyme Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14017 | Th1456 | Lorvotuzumab mertansine | >Th1456_Lorvotuzumab_mertansine QVQLVESGGGVVQPGRSLRLSCAASGFTFSSFGMHWVRQAPGKGLEWVAYISSGSFTIYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARMRKGYAMDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK | NA | NA | NA | NA | NA | NA | Lorvotuzumab mertansine has been used in trials studying the treatment of SCLC, Leukemia, Ovarian Cancer, Multiple Myeloma, and Merkel Cell Carcinoma, among others. | NA | NA | NA | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | (2S)-2-amino-6-[4-[[3-[[(2S)-1-[[(1S,2R,3S,5S,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.110,14.03,5]hexacosa-10,12,14(26),16,18-pentaen-6-yl]oxy]-1-oxopropan-2-yl]-methylamino]-3-oxopropyl]disulfanyl]pentanoylamino]hexanoic acid | NA | Link | NA | NA |
| 14221 | Th1476 | Stem bromelain | >Th1476_Stem_bromelain AVPQSIDWRDYGAVTSVKNQNPCGACWAFAAIATVESIYKIKKGILEPLSEQQVLDCAKGYGCKGGWEFRAFEFIISNKGVASGAIYPYKAAKGTCKTDGVPNSAYITGYARVPRNNESSMMYAVSKQPITVAVDANANFQYYKSGVFNGPCGTSLNHAVTAIGYGQDSIIYPKKWGAKWGEAGYIRMARDVSSSSGICGIAIDPLYPTLEE | NA | NA | NA | NA | NA | The estimated plasma half-life of stem bromelain is 6-9 hours [A32644]. | The primary therapeutic use for which stem bromelain is currently and formally indicated is as a burn wound eschar debridement agent that has been approved by the EMA since 2012 and marketed under the brand name Nexobrid [FDA Label]. Bromelain itself belongs to a category of protein-digesting enzymes that are obtained commercially from the fruit or stem of pineapples [A27198]. Although both fruit and stem bromelain are prepared differently and contain different enzymatic compositions, the general term bromelain typically refers to stem bromelain [A27198]. Bromelain is consequently a composite mixture of several different endopeptidases that can facilitate many different reactions with many different substrates. This action allows bromelain to demonstrate a wide range of therapeutic benefits ranging from cardiovascular to anticancer therapy - but the specific mechanisms of action by which it can elicit these effects are currently not properly understood. | The primary medical purpose for which stem bromelain (SB) is currently indicated for is the removal of eschar in adults with deep partial- and full-thickness thermal burns [FDA Label]. Besides this official indication, however, it is also believed that SB may be used as a treatment for several other purposes as well, including cardiovascular health, osteoarthritis, autoimmunity, blood clotting, diarrhea, cancer, surgery, and debridement - although the specific mechanisms of action for these indications remain to be elucidated [A27198]. | Stem bromelain is ultimately a mixture of various different thiol endopeptidases [A27198] that are capable of catalyzing a range of reactions on a number of different substrates, which is perhaps why stem bromelain can evidently be used as some manner of treatment in a range of therapeutic contexts. This notion is facilitated by the fact that various topical and oral administration stem bromelain preparations exist as well, further diversifying the ways in which the medication can be used. Perhaps the most important aspect of stem bromelain, however, is its ability to undergo intestinal absorption undegraded in a functionally intact form, ultimately preserving its proteolytic actions in the plasma [A27198, A32644]. This kind of pharmacodynamic characteristic is another element that perhaps allows stem bromelain to remain active within the body and elicit a number of actions at several major body systems. | Stem bromelain is ultimately a mixture of a number of thiol endopeptidases and other elements including phosphatases, glucosidase, peroxidases, cellulases, glycoproteins, carbohydrates, and various protease inhibitors [A27198]. The many different substrates and reactions that these varied enzymes can catalyze results in a number of different and possible mechanisms of action. Stem bromelain is currently principally used as a topical agent for debridement of necrotic tissue from wounds or second to third-degree burns [FDA Label, A27198]. As bromelain can contain escharase as one of its component enzymes, it is thought that various stem bromelain creams or gels can accelerate the healing process of wounds by facilitating the rapid removal of necrotic layers of dermis while preserving unburned/unharmed tissues [A27198] and/or perhaps by accelerating the recovery of blood perfusion in wound tissue, control the expression of TNF-alpha, and raise the expression of TGT-beta, as demonstrated in the pig animal model [A27198]. This kind of enzymatic debridement is ultimately preferred to surgical debridement as physical, surgical procedures are naturally painful, non-selective, and involve the possibility of repeat or excessive anesthesia and/or bleeding [A27198]. With regards to cardiovascular health, certain studies suggest that stem bromelain is capable of breaking down cholesterol plaques, eliciting a strong fibrinolytic activity, and inhibiting blood platelet aggregation - all of which protect against ischemia/reperfusion injury in skeletal muscle and minimize the risk of arterial thrombosis and embolism [A27198]. Additionally, stem bromelain has also been shown to attenuate allergic airway disease by altering CD4+ and CD8+ T lymphocyte populations - an action that may be beneficial in treating human asthma or hypersensitivity disorders [A27198]. Finally, stem bromelain has also been used to induce cardioprotection against ischemia-reperfusion injury via the Akt/Foxo pathway in rat model myocardium [A27198]. In the treatment of osteoarthritis, it is believed that stem bromelain has analgesic properties which are thought to be the result of direct influence on pain mediators such as bradykinin [A27198]. In addition, various trials suggest that the medication could be useful in reducing swelling, bruising, and pain in women having surgery like episiotomy [A27198]. Moreover, stem bromelain may also be used for treating acute inflammation and sports injuries [A27198]. Furthermore, stem bromelain has also been studied as an adjuvant therapy for chronic inflammatory, malignant, and autoimmune diseases [A27198]. Certain in vitro experiments have demonstrated that stem bromelain can modulate surface adhesion molecules on T cells, macrophages, and natural killer cells and also cause the secretion of IL-1B, IL-6, and Tumor Necrosis Factor-alpha (TNF-alpha) via peripheral blood mononuclear cells [A27198]. The agent has also been able to block the Raf-1/extracellular-regulated-kinase-2 (ERK-2) pathways by preventing T cell signal transduction [A27198]. In particular however, treating cells with stem bromelain decreases the activation of CD4(+) T cells and reduces the expression of CD25 [A27198]. Additionally, there is also evidence to suggest that oral therapy with stem bromelain produces certain analgesic and anti-inflammatory effects in patients with rheumatoid arthritis, which is a particularly common autoimmune disease [A27198]. Stem bromelain also affects blood coagulation by increasing the serum fibrinolytic ability and by preventing the synthesis of fibrin, a protein involved in blood clotting [A27198]. In the rat animal model, the reduction of serum fibrinogen level seems to be dose-dependent when both prothrombin time and activated partial thromboplastin time become markedly prolonged at higher concentrations of administered stem bromelain [A27198]. In vitro and in vivo studies also suggest stem bromelain can act as an effective fibrinolytic agent since it stimulates the conversion of plasminogen to plasmin, causing an increased fibrinolysis by degrading fibrin [A27198]. In terms of potential antimicrobial effects of stem bromelain, there are varying observations regarding its specific mechanism of action [A27198]. When counteracting the effects of some intestinal pathogens like Vibrio cholera or Escherichia coli (whose enterotoxin causes diarrhea in animals), some studies suggest that stem bromelain interacts with intestinal secretory signaling pathways like adenosine 3':5'-cyclic monophosphatase, guanosine 3':5'-cyclic monophosphatase, and/or calcium-dependent signaling cascades [A27198]. Conversely, other studies propose that stem bromelain supplementation can lead to antiadhesion effects which prevent E. coli bacteria from attaching to particular glycoprotein receptors on the intestinal mucosa by proteolytically modifying those receptor attachment sites [A27198]. Additionally, various studies have shown that stem bromelain also possesses anticancer activity. In particular, the agent has been found to increase the expression of p53 and Bax in mouse skin, both of which are well-known apoptosis activators [A27198]. Stem bromelain can also evidently decrease the activity of cell survival regulators like Akt and Erk, therefore inducing apoptotic tumor cell death [A27198]. Finally, stem bromelain has also been observed to downregulate NF-kB and Cox-2 expression in mouse papillomas and in models of skin tumorigenesis [A27198]. It has also demonstrated the capability to inhibit bacterial endotoxin (LPS)-induced NF-kB activity as well as the expression of PGE2 and Cox-2 in human monocytic leukemia and murine microglial cell lines [A27198]. | The human body can seemingly absorb significant amounts of bromelain - about 12 grams/day of bromelain may be consumed without the appearance of any major adverse effects [A27198]. Another study suggests that after giving bromelain (3000 FIP unit/day) to human over a period of ten days discovered no significant changes in blood coagulation parameters [A27198]. Finally, stem bromelain has a relatively low toxicity with an LD50 greater than 10 g/kg in mice, rats, and rabbits [A27198]. | Given its protein structure, it is assumed that stem bromelain, when administered would experience hydrolysis in the gut or eventually in the bloodstream after absorption [A32644]. Regardless, radiolabelled, intact stem bromelain has been found circulating in the plasma after administration [A27198, A32644]. | It appears that stem bromelain can be absorbed from the human gastrointestinal tract to a small but significant extent while remaining undegraded or functionally intact [A27198, A32644]. In a study involving 19 healthy men, daily oral administration of 3g/day of bromelain resulted in a mean plasma concentration of approximately 5000 pg/ml by 48 hours, although the maximum peak blood concentration of bromelain varied between 2000 to 10,000 pg/ml between subjects [A32644]. The average blood concentration of bromelain in the period range of 3 to 51 hours was 10.28 ug [A32644]. | No readily accessible data regarding the volume of distribution of stem bromelain is available. | No readily accessible data regarding the clearance of stem bromelain is available. | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14222 | Th1476 | Stem bromelain | >Th1476_Stem_bromelain AVPQSIDWRDYGAVTSVKNQNPCGACWAFAAIATVESIYKIKKGILEPLSEQQVLDCAKGYGCKGGWEFRAFEFIISNKGVASGAIYPYKAAKGTCKTDGVPNSAYITGYARVPRNNESSMMYAVSKQPITVAVDANANFQYYKSGVFNGPCGTSLNHAVTAIGYGQDSIIYPKKWGAKWGEAGYIRMARDVSSSSGICGIAIDPLYPTLEE | NA | NA | NA | NA | NA | The estimated plasma half-life of stem bromelain is 6-9 hours [A32644]. | The primary therapeutic use for which stem bromelain is currently and formally indicated is as a burn wound eschar debridement agent that has been approved by the EMA since 2012 and marketed under the brand name Nexobrid [FDA Label]. Bromelain itself belongs to a category of protein-digesting enzymes that are obtained commercially from the fruit or stem of pineapples [A27198]. Although both fruit and stem bromelain are prepared differently and contain different enzymatic compositions, the general term bromelain typically refers to stem bromelain [A27198]. Bromelain is consequently a composite mixture of several different endopeptidases that can facilitate many different reactions with many different substrates. This action allows bromelain to demonstrate a wide range of therapeutic benefits ranging from cardiovascular to anticancer therapy - but the specific mechanisms of action by which it can elicit these effects are currently not properly understood. | The primary medical purpose for which stem bromelain (SB) is currently indicated for is the removal of eschar in adults with deep partial- and full-thickness thermal burns [FDA Label]. Besides this official indication, however, it is also believed that SB may be used as a treatment for several other purposes as well, including cardiovascular health, osteoarthritis, autoimmunity, blood clotting, diarrhea, cancer, surgery, and debridement - although the specific mechanisms of action for these indications remain to be elucidated [A27198]. | Stem bromelain is ultimately a mixture of various different thiol endopeptidases [A27198] that are capable of catalyzing a range of reactions on a number of different substrates, which is perhaps why stem bromelain can evidently be used as some manner of treatment in a range of therapeutic contexts. This notion is facilitated by the fact that various topical and oral administration stem bromelain preparations exist as well, further diversifying the ways in which the medication can be used. Perhaps the most important aspect of stem bromelain, however, is its ability to undergo intestinal absorption undegraded in a functionally intact form, ultimately preserving its proteolytic actions in the plasma [A27198, A32644]. This kind of pharmacodynamic characteristic is another element that perhaps allows stem bromelain to remain active within the body and elicit a number of actions at several major body systems. | Stem bromelain is ultimately a mixture of a number of thiol endopeptidases and other elements including phosphatases, glucosidase, peroxidases, cellulases, glycoproteins, carbohydrates, and various protease inhibitors [A27198]. The many different substrates and reactions that these varied enzymes can catalyze results in a number of different and possible mechanisms of action. Stem bromelain is currently principally used as a topical agent for debridement of necrotic tissue from wounds or second to third-degree burns [FDA Label, A27198]. As bromelain can contain escharase as one of its component enzymes, it is thought that various stem bromelain creams or gels can accelerate the healing process of wounds by facilitating the rapid removal of necrotic layers of dermis while preserving unburned/unharmed tissues [A27198] and/or perhaps by accelerating the recovery of blood perfusion in wound tissue, control the expression of TNF-alpha, and raise the expression of TGT-beta, as demonstrated in the pig animal model [A27198]. This kind of enzymatic debridement is ultimately preferred to surgical debridement as physical, surgical procedures are naturally painful, non-selective, and involve the possibility of repeat or excessive anesthesia and/or bleeding [A27198]. With regards to cardiovascular health, certain studies suggest that stem bromelain is capable of breaking down cholesterol plaques, eliciting a strong fibrinolytic activity, and inhibiting blood platelet aggregation - all of which protect against ischemia/reperfusion injury in skeletal muscle and minimize the risk of arterial thrombosis and embolism [A27198]. Additionally, stem bromelain has also been shown to attenuate allergic airway disease by altering CD4+ and CD8+ T lymphocyte populations - an action that may be beneficial in treating human asthma or hypersensitivity disorders [A27198]. Finally, stem bromelain has also been used to induce cardioprotection against ischemia-reperfusion injury via the Akt/Foxo pathway in rat model myocardium [A27198]. In the treatment of osteoarthritis, it is believed that stem bromelain has analgesic properties which are thought to be the result of direct influence on pain mediators such as bradykinin [A27198]. In addition, various trials suggest that the medication could be useful in reducing swelling, bruising, and pain in women having surgery like episiotomy [A27198]. Moreover, stem bromelain may also be used for treating acute inflammation and sports injuries [A27198]. Furthermore, stem bromelain has also been studied as an adjuvant therapy for chronic inflammatory, malignant, and autoimmune diseases [A27198]. Certain in vitro experiments have demonstrated that stem bromelain can modulate surface adhesion molecules on T cells, macrophages, and natural killer cells and also cause the secretion of IL-1B, IL-6, and Tumor Necrosis Factor-alpha (TNF-alpha) via peripheral blood mononuclear cells [A27198]. The agent has also been able to block the Raf-1/extracellular-regulated-kinase-2 (ERK-2) pathways by preventing T cell signal transduction [A27198]. In particular however, treating cells with stem bromelain decreases the activation of CD4(+) T cells and reduces the expression of CD25 [A27198]. Additionally, there is also evidence to suggest that oral therapy with stem bromelain produces certain analgesic and anti-inflammatory effects in patients with rheumatoid arthritis, which is a particularly common autoimmune disease [A27198]. Stem bromelain also affects blood coagulation by increasing the serum fibrinolytic ability and by preventing the synthesis of fibrin, a protein involved in blood clotting [A27198]. In the rat animal model, the reduction of serum fibrinogen level seems to be dose-dependent when both prothrombin time and activated partial thromboplastin time become markedly prolonged at higher concentrations of administered stem bromelain [A27198]. In vitro and in vivo studies also suggest stem bromelain can act as an effective fibrinolytic agent since it stimulates the conversion of plasminogen to plasmin, causing an increased fibrinolysis by degrading fibrin [A27198]. In terms of potential antimicrobial effects of stem bromelain, there are varying observations regarding its specific mechanism of action [A27198]. When counteracting the effects of some intestinal pathogens like Vibrio cholera or Escherichia coli (whose enterotoxin causes diarrhea in animals), some studies suggest that stem bromelain interacts with intestinal secretory signaling pathways like adenosine 3':5'-cyclic monophosphatase, guanosine 3':5'-cyclic monophosphatase, and/or calcium-dependent signaling cascades [A27198]. Conversely, other studies propose that stem bromelain supplementation can lead to antiadhesion effects which prevent E. coli bacteria from attaching to particular glycoprotein receptors on the intestinal mucosa by proteolytically modifying those receptor attachment sites [A27198]. Additionally, various studies have shown that stem bromelain also possesses anticancer activity. In particular, the agent has been found to increase the expression of p53 and Bax in mouse skin, both of which are well-known apoptosis activators [A27198]. Stem bromelain can also evidently decrease the activity of cell survival regulators like Akt and Erk, therefore inducing apoptotic tumor cell death [A27198]. Finally, stem bromelain has also been observed to downregulate NF-kB and Cox-2 expression in mouse papillomas and in models of skin tumorigenesis [A27198]. It has also demonstrated the capability to inhibit bacterial endotoxin (LPS)-induced NF-kB activity as well as the expression of PGE2 and Cox-2 in human monocytic leukemia and murine microglial cell lines [A27198]. | The human body can seemingly absorb significant amounts of bromelain - about 12 grams/day of bromelain may be consumed without the appearance of any major adverse effects [A27198]. Another study suggests that after giving bromelain (3000 FIP unit/day) to human over a period of ten days discovered no significant changes in blood coagulation parameters [A27198]. Finally, stem bromelain has a relatively low toxicity with an LD50 greater than 10 g/kg in mice, rats, and rabbits [A27198]. | Given its protein structure, it is assumed that stem bromelain, when administered would experience hydrolysis in the gut or eventually in the bloodstream after absorption [A32644]. Regardless, radiolabelled, intact stem bromelain has been found circulating in the plasma after administration [A27198, A32644]. | It appears that stem bromelain can be absorbed from the human gastrointestinal tract to a small but significant extent while remaining undegraded or functionally intact [A27198, A32644]. In a study involving 19 healthy men, daily oral administration of 3g/day of bromelain resulted in a mean plasma concentration of approximately 5000 pg/ml by 48 hours, although the maximum peak blood concentration of bromelain varied between 2000 to 10,000 pg/ml between subjects [A32644]. The average blood concentration of bromelain in the period range of 3 to 51 hours was 10.28 ug [A32644]. | No readily accessible data regarding the volume of distribution of stem bromelain is available. | No readily accessible data regarding the clearance of stem bromelain is available. | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14366 | Th1494 | Vestronidase alfa | NA | 72562 | NA | NA | NA | NA | After repeated dosing of 4 mg/kg every other week in MPS VII patients, the mean ± standard deviation of the elimination half-life (t1/2) was 155 ± 37 minutes (range: 51 to 213 minutes) [FDA Label]. | Vestronidase alfa, or vestronidase alfa-vjbk, is a recombinant human lysosomal beta glucuronidase that is a purified enzyme produced by recombinant DNA technology in a Chinese hamster ovary cell line. The enzyme is a homotetramer consisted of 4 monomers with 629 amino acids, and holds the same amino acid sequence as human beta-glucuronidase (GUS) [FDA Label]. Vestronidase alfa is an enzyme replacement therapy for the treatment of mucopolysaccharidosis type VII (MPS VII), also known as Sly syndrome, which is an inherited, rare genetic metabolic condition that targets a small subset of population. MPS VII is a progressive condition that affects most tissues and organs due to the lack of a lysosomal enzyme called beta-glucuronidase, leading to buildup of toxic metabolites. The disorder is initiated with skeletal abnormalities, including short stature, along with other pathological conditions including enlarged liver and spleen, heart valve abnormalities, and narrowed airways which can lead to lung infections and trouble breathing. Last two conditions are leading causes of fatalities in patients with MPS VII. Some affected individuals do not survive infancy, while others may live into adolescence or adulthood and patients may experience developmental delay and progressive intellectual disability [FDA Label]. In clinical trials, vestronidase alfa treatment demonstrated improvement and stabilization in motor symptoms by increasing the patients' ability to walk longer distances in comparison to treatment with placebo . Few patients also experienced improved pulmonary function. Vestronidase alfa was FDA-approved on November 17th, 2017 under the trade name Mepsevii as an intravenous infusion for the treatment of pediatric and adult patients. | Indicated in pediatric and adult patients for the treatment of Mucopolysaccharidosis VII (MPS VII, Sly syndrome). | In all patients evaluated, MEPSEVII treatment resulted in reduction of urinary excretion of GAGs including chondroitin sulfate and dermatan sulfate, which was sustained with continued treatment [FDA Label]. | Beta-glucuronidase (GUS) is a lysosomal enzyme responsible for degradation of glucuronate-containing glycosaminoglycan (GAG) [A31278]. Resulting lysosomal storage and GAG accumulation in cells from incomplete metabolic degradation of macromolecules leads to damage to multiple tissues and organs. Vestronidase alfa serves as an exogenous source of GUS enzyme for uptake into cellular lysosomes, which is facilitated by the presence of mannose-6-phosphate (M6P) residues on the oligosaccharide chains of the recombinant enzyme. The chains allow binding of the enzyme to cell surface receptors to promote cellular uptake, and targets the lysosomes to achieve catabolism of accumulated GAGs in affected tissues [FDA Label]. | Treatment of vestronidase alfa with doses up to 20 mg/kg administered weekly in rats did not result in adverse effect on fertility and reproductive performance of male and female rats. Studies assessing the mutagenic or carcinogenic potential of vestronidase alfa have not been performed [FDA Label]. | Vestronidase alfa is eliminated by nonspecific proteolytic degradation into small peptides and amino acids [FDA Label]. | Serum exposures of vestronidase alfa increases in a dose-proportional manner, from 1 mg/kg (0.25 times the approved recommended dosage) to 2 mg/kg (0.5 times the approved recommended dosage), and 4 mg/kg (the recommended dosage). After repeated dosing of 4 mg/kg every other week in patients with MPS VII, the mean ± standard deviation of maximal concentration (Cmax) was 20.0 ± 8.1 mcg/mL (range: 6.6 to 34.9 mcg/mL). The mean ± standard deviation of area under the concentration-time curve from time zero to the last measurable concentration (AUC0-t) was 3440 ± 1430 mcg x min/mL (range: 1130 to 5820 mcg x min/mL) [FDA Label]. | After repeated dosing of 4 mg/kg every other week in MPS VII patients, the mean ± standard deviation of the total volume of distribution (Vss) was 260 ± 130 mL/kg (range: 97 to 598 mL/kg) [FDA Label]. | After repeated dosing of 4 mg/kg every other week in MPS VII patients, the mean ± standard deviation of the total clearance (CL) was 1.3 ± 0.7 mL/min/kg (range: 0.6 to 3.3 mL/min/kg) [FDA Label]. | Enzymes | NA | NA | NA | NA | NA | Mepsevii | Ultragenyx Pharmaceutical Inc. | Ultragenyx Pharmaceutical Inc. | Intravenous | 2 mg/1mL | None. | infusion site leakage or swelling, diarrhea, rash, severe allergic reaction (anaphylaxis), swelling of the extremities, and itching | Mepsevii contains an enzyme that occurs naturally in the body in healthy people. Some people lack this enzyme because of a genetic disorder. This medicine helps replace this missing enzyme in such people. Mepsevii is used to treat some of the symptoms of a genetic condition called mucopolysaccharidosis... | Mepsevii (vestronidase alfa-vjbk) injection is a recombinant human lysosomal beta glucuronidase indicated in pediatric and adult patients for the treatment of Mucopolysaccharidosis VII (MPS VII, Sly syndrome). | NA | NA | Link | Link | NA |
| 14367 | Th1494 | Vestronidase alfa | NA | 72562 | NA | NA | NA | NA | After repeated dosing of 4 mg/kg every other week in MPS VII patients, the mean ± standard deviation of the elimination half-life (t1/2) was 155 ± 37 minutes (range: 51 to 213 minutes) [FDA Label]. | Vestronidase alfa, or vestronidase alfa-vjbk, is a recombinant human lysosomal beta glucuronidase that is a purified enzyme produced by recombinant DNA technology in a Chinese hamster ovary cell line. The enzyme is a homotetramer consisted of 4 monomers with 629 amino acids, and holds the same amino acid sequence as human beta-glucuronidase (GUS) [FDA Label]. Vestronidase alfa is an enzyme replacement therapy for the treatment of mucopolysaccharidosis type VII (MPS VII), also known as Sly syndrome, which is an inherited, rare genetic metabolic condition that targets a small subset of population. MPS VII is a progressive condition that affects most tissues and organs due to the lack of a lysosomal enzyme called beta-glucuronidase, leading to buildup of toxic metabolites. The disorder is initiated with skeletal abnormalities, including short stature, along with other pathological conditions including enlarged liver and spleen, heart valve abnormalities, and narrowed airways which can lead to lung infections and trouble breathing. Last two conditions are leading causes of fatalities in patients with MPS VII. Some affected individuals do not survive infancy, while others may live into adolescence or adulthood and patients may experience developmental delay and progressive intellectual disability [FDA Label]. In clinical trials, vestronidase alfa treatment demonstrated improvement and stabilization in motor symptoms by increasing the patients' ability to walk longer distances in comparison to treatment with placebo . Few patients also experienced improved pulmonary function. Vestronidase alfa was FDA-approved on November 17th, 2017 under the trade name Mepsevii as an intravenous infusion for the treatment of pediatric and adult patients. | Indicated in pediatric and adult patients for the treatment of Mucopolysaccharidosis VII (MPS VII, Sly syndrome). | In all patients evaluated, MEPSEVII treatment resulted in reduction of urinary excretion of GAGs including chondroitin sulfate and dermatan sulfate, which was sustained with continued treatment [FDA Label]. | Beta-glucuronidase (GUS) is a lysosomal enzyme responsible for degradation of glucuronate-containing glycosaminoglycan (GAG) [A31278]. Resulting lysosomal storage and GAG accumulation in cells from incomplete metabolic degradation of macromolecules leads to damage to multiple tissues and organs. Vestronidase alfa serves as an exogenous source of GUS enzyme for uptake into cellular lysosomes, which is facilitated by the presence of mannose-6-phosphate (M6P) residues on the oligosaccharide chains of the recombinant enzyme. The chains allow binding of the enzyme to cell surface receptors to promote cellular uptake, and targets the lysosomes to achieve catabolism of accumulated GAGs in affected tissues [FDA Label]. | Treatment of vestronidase alfa with doses up to 20 mg/kg administered weekly in rats did not result in adverse effect on fertility and reproductive performance of male and female rats. Studies assessing the mutagenic or carcinogenic potential of vestronidase alfa have not been performed [FDA Label]. | Vestronidase alfa is eliminated by nonspecific proteolytic degradation into small peptides and amino acids [FDA Label]. | Serum exposures of vestronidase alfa increases in a dose-proportional manner, from 1 mg/kg (0.25 times the approved recommended dosage) to 2 mg/kg (0.5 times the approved recommended dosage), and 4 mg/kg (the recommended dosage). After repeated dosing of 4 mg/kg every other week in patients with MPS VII, the mean ± standard deviation of maximal concentration (Cmax) was 20.0 ± 8.1 mcg/mL (range: 6.6 to 34.9 mcg/mL). The mean ± standard deviation of area under the concentration-time curve from time zero to the last measurable concentration (AUC0-t) was 3440 ± 1430 mcg x min/mL (range: 1130 to 5820 mcg x min/mL) [FDA Label]. | After repeated dosing of 4 mg/kg every other week in MPS VII patients, the mean ± standard deviation of the total volume of distribution (Vss) was 260 ± 130 mL/kg (range: 97 to 598 mL/kg) [FDA Label]. | After repeated dosing of 4 mg/kg every other week in MPS VII patients, the mean ± standard deviation of the total clearance (CL) was 1.3 ± 0.7 mL/min/kg (range: 0.6 to 3.3 mL/min/kg) [FDA Label]. | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14371 | Th1496 | Velmanase alfa | NA | NA | NA | NA | NA | NA | NA | Recombinant Human Alpha Mannosidase has been investigated for the treatment of Alpha Mannosidosis and Alpha-Mannosidosis. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | zinc(2+) | NA | Link | NA | NA |
| 14372 | Th1496 | Velmanase alfa | NA | NA | NA | NA | NA | NA | NA | Recombinant Human Alpha Mannosidase has been investigated for the treatment of Alpha Mannosidosis and Alpha-Mannosidosis. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | zinc(2+) | NA | Link | NA | NA |
| 14386 | Th1498 | Vatreptacog alfa | NA | NA | NA | NA | NA | NA | NA | Vatreptacog Alfa (Activated) has been used in trials studying the treatment of Haemophilia B, Haemophilia A, Congenital Bleeding Disorder, Haemophilia A With Inhibitors, and Haemophilia B With Inhibitors. | NA | NA | NA | NA | NA | NA | NA | NA | Enzyme Precursors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14387 | Th1498 | Vatreptacog alfa | NA | NA | NA | NA | NA | NA | NA | Vatreptacog Alfa (Activated) has been used in trials studying the treatment of Haemophilia B, Haemophilia A, Congenital Bleeding Disorder, Haemophilia A With Inhibitors, and Haemophilia B With Inhibitors. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14388 | Th1498 | Vatreptacog alfa | NA | NA | NA | NA | NA | NA | NA | Vatreptacog Alfa (Activated) has been used in trials studying the treatment of Haemophilia B, Haemophilia A, Congenital Bleeding Disorder, Haemophilia A With Inhibitors, and Haemophilia B With Inhibitors. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14590 | Th1520 | Aviscumine | NA | NA | NA | NA | NA | NA | NA | Cy 503 is under investigation in clinical trial NCT00658437 (Aviscumine for the Treatment of Malignant Melanoma Stage IV After Failure of Prior Therapy). | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14591 | Th1520 | Aviscumine | NA | NA | NA | NA | NA | NA | NA | Cy 503 is under investigation in clinical trial NCT00658437 (Aviscumine for the Treatment of Malignant Melanoma Stage IV After Failure of Prior Therapy). | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14675 | Th1526 | Monteplase | NA | NA | NA | NA | NA | NA | NA | Monteplase has been used in trials studying the treatment of Pulmonary Embolism. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14676 | Th1526 | Monteplase | NA | NA | NA | NA | NA | NA | NA | Monteplase has been used in trials studying the treatment of Pulmonary Embolism. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14754 | Th1534 | Cepeginterferon alfa-2B | NA | NA | NA | NA | NA | NA | NA | Cepeginterferon alfa-2B is under investigation in clinical trial NCT01889433 (An Open-label Comparative Efficacy and Safety Study of Algeron (Cepeginterferon Alfa-2b) in Treatment-naive Patients With Chronic Hepatitis C). | NA | NA | NA | NA | NA | NA | NA | NA | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14804 | Th1540 | Olipudase alfa | NA | NA | NA | NA | NA | NA | NA | Olipudase alfa has been used in trials studying the treatment of Sphingomyelin Lipidosis and Human Acid Sphingomyelinase Deficiency. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14805 | Th1540 | Olipudase alfa | NA | NA | NA | NA | NA | NA | NA | Olipudase alfa has been used in trials studying the treatment of Sphingomyelin Lipidosis and Human Acid Sphingomyelinase Deficiency. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14844 | Th1545 | Glucose oxidase | NA | NA | NA | NA | NA | NA | NA | Glucose oxidase has been investigated for the treatment of Upper Respiratory Tract Infections. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14845 | Th1545 | Glucose oxidase | NA | NA | NA | NA | NA | NA | NA | Glucose oxidase has been investigated for the treatment of Upper Respiratory Tract Infections. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14888 | Th1549 | Factor XIII (human) | >Th1549_Factor_XIII_(human) GVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM | NA | NA | NA | NA | NA | 6.6 ±2.29 days [FDA Label], 6.6 days [A32364] | Factor XIII (human) is a heat-treated, lyophilized concentrate of coagulation factor XIII, an endogenous enzyme responsible for the crosslinking of fibrin and an essential component of the coagulation cascade [FDA Label]. For people with congenital deficiency or mutation of Factor XIII, a rare bleeding disorder, exogenous replacement of this key coagulation factor is essential for management and prevention of bleeding episodes. Also known as Fibrin Stabilizing Factor (FSF), Factor XIII is an endogenously produced coagulation factor and the final enzyme within the blood coagulation cascade. Within the body, FXIII circulates as a heterotetramer composed of 2 A-subunits and 2 B-subunits (A2B2)[A32363]. When activated by thrombin at the site of injury, the FXIII pro-enzyme is cleaved resulting in activation of the catalytic A-subunit and dissociation from its carrier B-subunit. As a result, the active transglutaminase from subunit A cross-links fibrin and other proteins resulting in increased mechanical strength and resistance to fibrinolysis of the fibrin clot. This contributes to enhanced platelet and clot adhesion to injured tissue, thereby improving blood coagulation and maintenance of hemostasis [A18581]. Other drug products with similar structure and function to Factor XIII (human) include [DB09310], which is a recombinant form of the A subunit of human coagulation factor XIII. Compared to Factor XIII (human), which is purified from pooled human plasma, [DB09310] is produced through recombinant DNA technology where the target protein is grown in yeast and then isolated [FDA Label]. Factor XIII (Human), available as the commercially available product Corifact, is approved by the Food and Drug Administration for routine prophylactic treatment and peri-operative management of surgical bleeding in adult and pediatric patients with congenital FXIII deficiency [FDA Label]. As the half-life of endogenous Factor XIII is long (5-11 days), prophylactic therapy with the replacement of FXIII can be given every 4-6 to maintain hemostasis[A32363]. | Factor XIII (Human), available as the commercially available product Corifact, is approved by the Food and Drug Administration for routine prophylactic treatment and peri-operative management of surgical bleeding in adult and pediatric patients with congenital FXIII deficiency [FDA Label]. | NA | Also known as Fibrin Stabilizing Factor (FSF), Factor XIII is an endogenously produced coagulation factor and the final enzyme within the blood coagulation cascade. Within the body, FXIII circulates as a heterotetramer composed of 2 A-subunits and 2 B-subunits (A2B2)[A32363]. When activated by thrombin at the site of injury, the FXIII pro-enzyme is cleaved resulting in activation of the catalytic A-subunit and dissociation from its carrier B-subunit. As a result, the active transglutaminase from subunit A cross-links fibrin and other proteins resulting in increased mechanical strength and resistance to fibrinolysis of the fibrin clot. This contributes to enhanced platelet and clot adhesion to injured tissue, thereby improving blood coagulation and maintenance of hemostasis [A18581]. Exogenous replacement of Factor XIII is a cornerstone of treatment for bleeding associated with congenital Factor XIII deficiency. | Corifact was studied in an acute toxicity study in mice and rats at doses up to 3550 units per kg and 1420 units per kg, respectively. Repeat dose toxicity was studied in rats at daily doses up to 350 units per kg for a period of 14 days. No signs of toxicity were observed in the single dose and repeat dose studies. A local tolerance study in rabbits demonstrated no clinical or histopathological changes at the injection site after intravenous, intra-arterial or para-venous administration of Corifact. A thrombogenicity test was performed in rabbits at doses up to 350 units per kg. Corifact showed no thrombogenic potential at the doses tested. | NA | Tmax = 1.7 ±1.44 hr [FDA Label] Tmax = 1.72 hr [A32364] Cmax = 0.9 ±0.20 units/mL (peak concentration at steady state) [FDA Label] Cmax = 87.7% (peak concentration at steady state) [A32364] | Vss = 51.1 mL/kg (volume of distribution at steady state) [A32364] | 0.25 ±0.09 mL/hr/kg [FDA Label] 0.25 mL/hr/kg [A32364] | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14889 | Th1549 | Factor XIII (human) | >Th1549_Factor_XIII_(human) GVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM | NA | NA | NA | NA | NA | 6.6 ±2.29 days [FDA Label], 6.6 days [A32364] | Factor XIII (human) is a heat-treated, lyophilized concentrate of coagulation factor XIII, an endogenous enzyme responsible for the crosslinking of fibrin and an essential component of the coagulation cascade [FDA Label]. For people with congenital deficiency or mutation of Factor XIII, a rare bleeding disorder, exogenous replacement of this key coagulation factor is essential for management and prevention of bleeding episodes. Also known as Fibrin Stabilizing Factor (FSF), Factor XIII is an endogenously produced coagulation factor and the final enzyme within the blood coagulation cascade. Within the body, FXIII circulates as a heterotetramer composed of 2 A-subunits and 2 B-subunits (A2B2)[A32363]. When activated by thrombin at the site of injury, the FXIII pro-enzyme is cleaved resulting in activation of the catalytic A-subunit and dissociation from its carrier B-subunit. As a result, the active transglutaminase from subunit A cross-links fibrin and other proteins resulting in increased mechanical strength and resistance to fibrinolysis of the fibrin clot. This contributes to enhanced platelet and clot adhesion to injured tissue, thereby improving blood coagulation and maintenance of hemostasis [A18581]. Other drug products with similar structure and function to Factor XIII (human) include [DB09310], which is a recombinant form of the A subunit of human coagulation factor XIII. Compared to Factor XIII (human), which is purified from pooled human plasma, [DB09310] is produced through recombinant DNA technology where the target protein is grown in yeast and then isolated [FDA Label]. Factor XIII (Human), available as the commercially available product Corifact, is approved by the Food and Drug Administration for routine prophylactic treatment and peri-operative management of surgical bleeding in adult and pediatric patients with congenital FXIII deficiency [FDA Label]. As the half-life of endogenous Factor XIII is long (5-11 days), prophylactic therapy with the replacement of FXIII can be given every 4-6 to maintain hemostasis[A32363]. | Factor XIII (Human), available as the commercially available product Corifact, is approved by the Food and Drug Administration for routine prophylactic treatment and peri-operative management of surgical bleeding in adult and pediatric patients with congenital FXIII deficiency [FDA Label]. | NA | Also known as Fibrin Stabilizing Factor (FSF), Factor XIII is an endogenously produced coagulation factor and the final enzyme within the blood coagulation cascade. Within the body, FXIII circulates as a heterotetramer composed of 2 A-subunits and 2 B-subunits (A2B2)[A32363]. When activated by thrombin at the site of injury, the FXIII pro-enzyme is cleaved resulting in activation of the catalytic A-subunit and dissociation from its carrier B-subunit. As a result, the active transglutaminase from subunit A cross-links fibrin and other proteins resulting in increased mechanical strength and resistance to fibrinolysis of the fibrin clot. This contributes to enhanced platelet and clot adhesion to injured tissue, thereby improving blood coagulation and maintenance of hemostasis [A18581]. Exogenous replacement of Factor XIII is a cornerstone of treatment for bleeding associated with congenital Factor XIII deficiency. | Corifact was studied in an acute toxicity study in mice and rats at doses up to 3550 units per kg and 1420 units per kg, respectively. Repeat dose toxicity was studied in rats at daily doses up to 350 units per kg for a period of 14 days. No signs of toxicity were observed in the single dose and repeat dose studies. A local tolerance study in rabbits demonstrated no clinical or histopathological changes at the injection site after intravenous, intra-arterial or para-venous administration of Corifact. A thrombogenicity test was performed in rabbits at doses up to 350 units per kg. Corifact showed no thrombogenic potential at the doses tested. | NA | Tmax = 1.7 ±1.44 hr [FDA Label] Tmax = 1.72 hr [A32364] Cmax = 0.9 ±0.20 units/mL (peak concentration at steady state) [FDA Label] Cmax = 87.7% (peak concentration at steady state) [A32364] | Vss = 51.1 mL/kg (volume of distribution at steady state) [A32364] | 0.25 ±0.09 mL/hr/kg [FDA Label] 0.25 mL/hr/kg [A32364] | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15002 | Th1560 | Dolcanatide | NA | NA | NA | NA | NA | NA | NA | Dolcanatide has been investigated in Exposure. | NA | NA | NA | NA | NA | NA | NA | NA | Enzyme Activators | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | (2R)-2-[[(1R,4S,7S,10S,13S,16R,19S,22S,25R,32S,38R)-10-(2-amino-2-oxoethyl)-25-[[(2S)-4-carboxy-2-[[(2S)-3-carboxy-2-[[(2R)-2,4-diamino-4-oxobutanoyl]amino]propanoyl]amino]butanoyl]amino]-22-(2-carboxyethyl)-32-[(1R)-1-hydroxyethyl]-4-methyl-19-(2-methylpropyl)-3,6,9,12,15,18,21,24,30,33,36-undecaoxo-7,13-di(propan-2-yl)-27,28,40,41-tetrathia-2,5,8,11,14,17,20,23,31,34,37-undecazabicyclo[14.13.13]dotetracontane-38-carbonyl]amino]-4-methylpentanoic acid | NA | Link | NA | NA |
| 15020 | Th1562 | Serrapeptase | >Th1562_Serrapeptase MQSTKKAIEITESNFAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYRDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEAQSSDFIHFVDHFSGAAGEALLSYNASNNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV | NA | NA | NA | NA | NA | NA | Serrapeptase is a proteolytic enzyme preparation used concomitantly with an antibiotic in osteoarticular infections. Serratiopeptidase is under investigation in clinical trial NCT02493179 (Efficacy Evaluation of the (Serodase 5 mg Tablet) in the Treatment of Inflammation After Third Molar Surgery). | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15021 | Th1562 | Serrapeptase | >Th1562_Serrapeptase MQSTKKAIEITESNFAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYRDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEAQSSDFIHFVDHFSGAAGEALLSYNASNNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV | NA | NA | NA | NA | NA | NA | Serrapeptase is a proteolytic enzyme preparation used concomitantly with an antibiotic in osteoarticular infections. Serratiopeptidase is under investigation in clinical trial NCT02493179 (Efficacy Evaluation of the (Serodase 5 mg Tablet) in the Treatment of Inflammation After Third Molar Surgery). | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15050 | Th1565 | Pancrelipase lipase | >Th1565_Pancrelipase_lipase SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSDEFDSDVEVGDLQKVKFIWYNNNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLNPC | 48000 | NA | 7.4 | NA | NA | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the elimination half-life is not relevant.105 | Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.[L2509] The amylases are enzymes that help in the chemical process of digestion by hydrolizing starch into more available saccharide forms.[T177] The pancrelipase amylase is a single polypeptide chain containing two SH groups and four disulfide bridges.[L2512] The pancrelipase mixture, including pancrelipase amylase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.[L2510] | The use of pancrelipase amylase is part of the pancreatic enzyme replacement therapy. This therapy is indicated for the treatment of pancreatic insufficiency attributed to cystic fibrosis, chronic pancreatitis or any other medically defined pancreatic disease that might require it. Pancreatic diseases are associated with the deterioration of pancreatic parenchyma and of the dual physiological functions of the pancreas. Once established, pancreatic insufficiency results in malnutrition, weight loss, and steatorrhea. | The major maldigestion/malabsorption problems arise from incomplete fat digestion. In clinical trials, the administration of pancrelipase as a mixture of amylase, lipase, and protease demonstrated a significant improvement in the coefficient of fat absorption and nitrogen absorption. These effects are accompanied by increased in body weight and body mass index. | Pancrelipase lipase catalyzes the hydrolysis of triglycerides to monoglycerides, glycerol, and fatty acids. This activity is performed by the hydrolyzation of the esters of fatty acids. The hydrolysis is started by the action of colipase which helps to anchor lipase to the lipid-water membrane of the micelle producing a surface change on lipase. The hydrophobic active site is exposed for the binding of triglycerides and further interaction with the catalytic triad. In this triad, the function of the three amino acids allows the formation of a deprotonated serine which becomes a nucleophile and act on the ester carbonyl of the fatty acids for the later formation of monoglyceride and fatty acid monomers.[A32750] | The studies of the toxicology of pancrelipase are not needed as this drug has been used clinically for a long time. Clinical overdose studies proved no effect on lungs, pancreas, liver and kidneys but it can produce symptoms such as diarrhea or stomach upset. Carcinogenicity studies have not shown any increased incidence with the use of pancrelipase. As pancrelipase is not absorbed, the effect on fetal development or reproduction is not expected. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the metabolism is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the volume of distribution is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the clearance rate is not relevant. | Enzymes | 8562979 | 22-10-2013 | 20-02-2028 | NA | Dietary fat | Cotazym | Organon Canada Inc. | Organon Canada Inc. | Oral | NA | NA | Abnormal feces anxiety bloated feeling chills cold sweats confusion cool, pale skin depression excess air or gas in the stomach or intestines feeling of fullness fever frequent bowel movements loss of consciousness muscle aches nightmares passing gas runny nose seizures shakiness slurred speech sore throat | NA | NA | NA | NA | Link | Link | NA |
| 15051 | Th1565 | Pancrelipase lipase | >Th1565_Pancrelipase_lipase SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTITNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSDEFDSDVEVGDLQKVKFIWYNNNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLNPC | 48000 | NA | 7.4 | NA | NA | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the elimination half-life is not relevant.105 | Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.[L2509] The amylases are enzymes that help in the chemical process of digestion by hydrolizing starch into more available saccharide forms.[T177] The pancrelipase amylase is a single polypeptide chain containing two SH groups and four disulfide bridges.[L2512] The pancrelipase mixture, including pancrelipase amylase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.[L2510] | The use of pancrelipase amylase is part of the pancreatic enzyme replacement therapy. This therapy is indicated for the treatment of pancreatic insufficiency attributed to cystic fibrosis, chronic pancreatitis or any other medically defined pancreatic disease that might require it. Pancreatic diseases are associated with the deterioration of pancreatic parenchyma and of the dual physiological functions of the pancreas. Once established, pancreatic insufficiency results in malnutrition, weight loss, and steatorrhea. | The major maldigestion/malabsorption problems arise from incomplete fat digestion. In clinical trials, the administration of pancrelipase as a mixture of amylase, lipase, and protease demonstrated a significant improvement in the coefficient of fat absorption and nitrogen absorption. These effects are accompanied by increased in body weight and body mass index. | Pancrelipase lipase catalyzes the hydrolysis of triglycerides to monoglycerides, glycerol, and fatty acids. This activity is performed by the hydrolyzation of the esters of fatty acids. The hydrolysis is started by the action of colipase which helps to anchor lipase to the lipid-water membrane of the micelle producing a surface change on lipase. The hydrophobic active site is exposed for the binding of triglycerides and further interaction with the catalytic triad. In this triad, the function of the three amino acids allows the formation of a deprotonated serine which becomes a nucleophile and act on the ester carbonyl of the fatty acids for the later formation of monoglyceride and fatty acid monomers.[A32750] | The studies of the toxicology of pancrelipase are not needed as this drug has been used clinically for a long time. Clinical overdose studies proved no effect on lungs, pancreas, liver and kidneys but it can produce symptoms such as diarrhea or stomach upset. Carcinogenicity studies have not shown any increased incidence with the use of pancrelipase. As pancrelipase is not absorbed, the effect on fetal development or reproduction is not expected. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the metabolism is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the volume of distribution is not relevant. | Pancrelipase acts locally in the GI tract and it is not absorbed in any significant amount thus, the clearance rate is not relevant. | Enzymes and Coenzymes | 8562980 | 22-10-2013 | 20-02-2028 | NA | Dietary fat | Cotazym Ecs 20 | Organon Canada Inc. | Organon Canada Inc. | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15106 | Th1566 | Coagulation factor VII human | >Th1566_Coagulation_factor_VII_human MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | NA | NA | NA | NA | NA | 5 h | Coagulation factor VII is human serine protease type enzyme that is involved in the extrinsic coagulation cascade which results in blood clotting. | May be administered in cases of uncontrolled bleeding. Factor VII alone can be used in the treatment of congenital hemophilia A or B, acquired hemophilia, congenital factor VII deficiency, and Glanzmann's thrombasthenia. Off label use in the treatment of refractory bleeding after cardiac surgery and warfarin related intracerebral hemorrhage. Brands for human factor VII are currently only in combination with other vitamin K coagulation factors and can be used to reverse vitamin K antagonist activity in patients with acute major bleeds or for urgent surgery/invasive procedures. | Human Factor VII complexes with tissue factor resulting in its activation to VIIa. It is the activated Factor VIIa that then binds to Factor X activating it to Factor Xa, as well as coagulation Factor IX is activated to Factor IXa. Factor Xa continues the coagulation cascade to eventually convert prothrombin to thrombin, which leads to the formation of a clot by converting fibrinogen to fibrin. | Factor VII is required in the extrinsic clotting cascade. When there is vascular damage tissue factor (TF) is released which then interacts with Factor VII resulting in the formation of the activated complex VIIa. Factor VIIa then continues to activate coagulation factors in the cascade until a clot is formed. | No evidence of toxicity. Adverse effect of excessive clotting in certain individuals. | Degraded by catabolism | No absorption since given IV. | 45 ml/kg | 7.4 ml/kgh | Enzyme Precursors | NA | NA | NA | NA | Tissue factor,Coagulation factor X,Coagulation factor IX | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15107 | Th1566 | Coagulation factor VII human | >Th1566_Coagulation_factor_VII_human MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | NA | NA | NA | NA | NA | 5 h | Coagulation factor VII is human serine protease type enzyme that is involved in the extrinsic coagulation cascade which results in blood clotting. | May be administered in cases of uncontrolled bleeding. Factor VII alone can be used in the treatment of congenital hemophilia A or B, acquired hemophilia, congenital factor VII deficiency, and Glanzmann's thrombasthenia. Off label use in the treatment of refractory bleeding after cardiac surgery and warfarin related intracerebral hemorrhage. Brands for human factor VII are currently only in combination with other vitamin K coagulation factors and can be used to reverse vitamin K antagonist activity in patients with acute major bleeds or for urgent surgery/invasive procedures. | Human Factor VII complexes with tissue factor resulting in its activation to VIIa. It is the activated Factor VIIa that then binds to Factor X activating it to Factor Xa, as well as coagulation Factor IX is activated to Factor IXa. Factor Xa continues the coagulation cascade to eventually convert prothrombin to thrombin, which leads to the formation of a clot by converting fibrinogen to fibrin. | Factor VII is required in the extrinsic clotting cascade. When there is vascular damage tissue factor (TF) is released which then interacts with Factor VII resulting in the formation of the activated complex VIIa. Factor VIIa then continues to activate coagulation factors in the cascade until a clot is formed. | No evidence of toxicity. Adverse effect of excessive clotting in certain individuals. | Degraded by catabolism | No absorption since given IV. | 45 ml/kg | 7.4 ml/kgh | Enzymes and Coenzymes | NA | NA | NA | NA | Tissue factor,Coagulation factor X,Coagulation factor IX | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15116 | Th1567 | Coagulation Factor IX Human | >Th1567_Coagulation_Factor_IX_Human YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAEAVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT | 46548.2 | C2041H3136N558O641S25 | 5.2 | -0.431 | 54 °C | 18.8 ± 5.4 hours. | Factor IX (or Christmas factor) is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this protein causes hemophilia B. | Factor IX is used to treat Christmas disease. Factor IX deficiency is treated by injection factor IX produced from human plasma. Tranexamic acid may be of value in patients undergoing surgery who have inherited factor IX deficiency in order to reduce the perioperative risk of bleeding. | Binds vitamin K and factor VIIIa. Cleaves the Arg-Ile bond in factor X to form active factor Xa. Plays a key role in blood coagulation and clotting. Injections of factor IX are used to treat hemophilia B, which is sometimes called Christmas disease. AlphaNine is injected to increase plasma levels of Factor IX and can temporarily correct this coagulation defect. The activated partial thromboplastin time (aPTT) is prolonged in people with hemophilia B. Treatment with factor IX concentrate may normalize the aPTT by temporarily replacing the factor IX. The administration of BeneFIX increases plasma levels of factor IX, and can temporarily correct the coagulation defect in these patients. | Coagulation Factor IX is an important protein in the process of hemostasis and normal blood clotting as it plays a key role within the coagulation cascade. It is located within the blood plasma as a zymogen, an antecedent to enzymatic function, in its inactivated state. Factor IX is dependent on the presence of Vitamin K, and is activated to a serine protease by the function of Coagulation Factor XIa. Factor XIa cleaves the peptide bond associated with protein activation in Factor IX, leaving Factor IX with two exposed chains, a light chain and a heavy chain. These two chains are held together by several disulfide bonds that reinforce the structure of Factor IX's activated form. After being activated, Factor IX forms a complex with calcium ions, membrane phospholipids and Coagulation Factor VIII to activate Coagulation Factor X. The activation of Factor X then performs a similarly integral step in the blood coagulation cascade. The ultimate result of phenotypically normal coagulation factors is the creation of platelets for normal blood clotting. | NA | NA | NA | NA | 8.62 ± 1.7. | Enzyme Precursors | NA | NA | NA | NA | Coagulation factor X,Coagulation factor XI,Coagulation factor VII,Coagulation factor VIII,Prothrombin,Prolow-density lipoprotein receptor-related protein 1,Vitamin K-dependent gamma-carboxylase | Immunine Vh | Takeda | Takeda | Intravenous | 720 unit / 5 mL | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15117 | Th1567 | Coagulation Factor IX Human | >Th1567_Coagulation_Factor_IX_Human YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAEAVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT | 46548.2 | C2041H3136N558O641S25 | 5.2 | -0.431 | 54 °C | 18.8 ± 5.4 hours. | Factor IX (or Christmas factor) is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this protein causes hemophilia B. | Factor IX is used to treat Christmas disease. Factor IX deficiency is treated by injection factor IX produced from human plasma. Tranexamic acid may be of value in patients undergoing surgery who have inherited factor IX deficiency in order to reduce the perioperative risk of bleeding. | Binds vitamin K and factor VIIIa. Cleaves the Arg-Ile bond in factor X to form active factor Xa. Plays a key role in blood coagulation and clotting. Injections of factor IX are used to treat hemophilia B, which is sometimes called Christmas disease. AlphaNine is injected to increase plasma levels of Factor IX and can temporarily correct this coagulation defect. The activated partial thromboplastin time (aPTT) is prolonged in people with hemophilia B. Treatment with factor IX concentrate may normalize the aPTT by temporarily replacing the factor IX. The administration of BeneFIX increases plasma levels of factor IX, and can temporarily correct the coagulation defect in these patients. | Coagulation Factor IX is an important protein in the process of hemostasis and normal blood clotting as it plays a key role within the coagulation cascade. It is located within the blood plasma as a zymogen, an antecedent to enzymatic function, in its inactivated state. Factor IX is dependent on the presence of Vitamin K, and is activated to a serine protease by the function of Coagulation Factor XIa. Factor XIa cleaves the peptide bond associated with protein activation in Factor IX, leaving Factor IX with two exposed chains, a light chain and a heavy chain. These two chains are held together by several disulfide bonds that reinforce the structure of Factor IX's activated form. After being activated, Factor IX forms a complex with calcium ions, membrane phospholipids and Coagulation Factor VIII to activate Coagulation Factor X. The activation of Factor X then performs a similarly integral step in the blood coagulation cascade. The ultimate result of phenotypically normal coagulation factors is the creation of platelets for normal blood clotting. | NA | NA | NA | NA | 8.62 ± 1.7. | Enzymes and Coenzymes | NA | NA | NA | NA | Coagulation factor X,Coagulation factor XI,Coagulation factor VII,Coagulation factor VIII,Prothrombin,Prolow-density lipoprotein receptor-related protein 1,Vitamin K-dependent gamma-carboxylase | Kcentra | CSL Behring GmbH | CSL Behring GmbH | Intravenous | NA | Kcentra is contraindicated in: Patients with known anaphylactic or severe systemic reactions to Kcentra or any components in Kcentra including heparin, Factors II, VII, IX, X, Proteins C and S, Antithrombin III and Human albumin. Patients with disseminated intravascular coagulation (DIC). Patients with known heparin-induced thrombocytopenia (HIT). Kcentra contains heparin [see DESCRIPTION]. | headache, nausea, vomiting, joint pain, low blood pressure (hypotension), and low levels of iron in the blood (anemia) | Kcentra is a blood coagulation factor replacement product. Kcentra is used to quickly reverse the effects of a blood-thinning medicine (such as warfarin) during a major bleeding episode, or when there is a need for emergency surgery or invasive medical procedure. Kcentra is for use in adults and dosing... | Kcentra is a prescription medicine used to treat the symptoms of Vitamin K Antagonist Reversal. Kcentra may be used alone or with other medications. | NA | NA | Link | Link | NA |
| 15124 | Th1568 | Cerliponase alfa | >Th1568_Cerliponase_alfa SYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP | 59 | NA | NA | NA | NA | Refer to FDA Label | Cerliponase alfa is an enzyme replacement treatment for a specific form of Batten disease. It was the first FDA-approved treatment to slow loss of walking ability (ambulation) in symptomatic pediatric patients 3 years of age and older with late infantile neuronal ceroid lipofuscinosis type 2 (CLN2), also known as tripeptidyl peptidase-1 (TPP1) deficiency. Intraventricular administration of the drug allows significant uptake into the brain. Cerliponase alfa was approved in April, 2017 (as Brineura). | Cerliponase alfa is a treatment for late infantile neuronal ceroid lipofuscinosis type 2 (CLN2) disease to decelerate the progressive motor function decline in patients 3 years of age and older. CLN2 disease is a form of Batten disease, a rare inherited neurodegenerative disorder and is associated with seizures, ataxia, rapid loss of language and motor functions, blindness, and early death [L755]. It is caused by the lack the lysosomal enzyme tripeptidyl peptidase-1 (TPP1) and subsequent accumulation of lysosomal storage materials normally metabolized by this enzyme in the central nervous system. | Cerliponase alfa contains the active substance tripeptidyl peptidase-1 (rhTPP1), a recombinant human lysosomal exopeptidase which cleaves the N-terminal of tripeptides with a broad substrate specificity. Cerliponase alfa slows the progressive decline in motor function caused by abnormal motor signalling in the brain by restoring the normal levels and activity of TPP1. | The mature form of enzyme contains 5 consensus N-glycosylation sites with high mannose, phosphorylated high mannose and complex glycosylation structures. It is taken up by LINCL fibroblasts and translocated to the lysosomes through the Cation Independent Mannose-6-Phosphate Receptor (CI-MPR, also known as M6P/IGF2 receptor). Cerliponase alfa is activated in the lysosome under low pH conditions and the activated proteolytic form of rhTPP1 cleaves tripeptides from the N-terminus of stored proteins. | No data from carcinogenicity, genotoxicity, and fertility studies. Unwanted effects of cerliponase alfa treatment include pyrexia, ECG abnormalities, decreased CSF protein, seizure and hypersensitivity. | Predicted to be metabolized through peptide hydrolysis. | Refer to FDA Label | The estimated CSF volume of distribution of cerliponase alfa following intraventricular infusion of 300mg of Brineura (median Vss = 245 mL) exceeds the typical CSF volume (100 mL) [FDA label]. | Refer to FDA Label | Enzymes | NA | NA | NA | NA | Cation-independent mannose-6-phosphate receptor | Brineura | Biomarin International Limited | Biomarin International Limited | Intracerebral | 150 mg | Brineura is contraindicated in patients with:any sign or symptom of acute, unresolved localized infection on or around the device insertion site (e.g. cellulitis or abscess); or suspected or confirmed CNS infection (e.g. cloudy CSF or positive CSF gram stain, or meningitis) [see WARNINGS AND PRECAUTIONS].any acute intraventricular access device-related complication (e.g., leakage, extravasation of fluid, or device failure) [see WARNINGS AND PRECAUTIONS].ventriculoperitoneal shunts. | fever, ECG abnormalities, increased or decreased cerebrospinal fluid (CSF) protein, vomiting, seizures, hypersensitivity, blood clotting, headache, irritability, increased white blood cell count (pleocytosis), device-related infection, slow heart rate, feeling jittery, and low blood pressure (hypotension). | Brineura is used to slow the loss of ability to crawl or walk in children with symptoms of a rare genetic condition called ceroid lipofuscinosis type 2 disease (CLN2). Brineura is for use in children who are at least 3 years old. Brineura may help slow the loss of certain physical abilities in children... | Brineura (cerliponase alfa) injection is a hydrolytic lysosomal N-terminal tripeptidyl peptidase indicated to slow the loss of ambulation in symptomatic pediatric patients 3 years of age and older with late infantile neuronal ceroid lipofuscinosis type 2 (CLN2), also known as tripeptidyl peptidase1 (TPP1) deficiency. | NA | NA | Link | Link | NA |
| 15125 | Th1568 | Cerliponase alfa | >Th1568_Cerliponase_alfa SYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP | 59 | NA | NA | NA | NA | Refer to FDA Label | Cerliponase alfa is an enzyme replacement treatment for a specific form of Batten disease. It was the first FDA-approved treatment to slow loss of walking ability (ambulation) in symptomatic pediatric patients 3 years of age and older with late infantile neuronal ceroid lipofuscinosis type 2 (CLN2), also known as tripeptidyl peptidase-1 (TPP1) deficiency. Intraventricular administration of the drug allows significant uptake into the brain. Cerliponase alfa was approved in April, 2017 (as Brineura). | Cerliponase alfa is a treatment for late infantile neuronal ceroid lipofuscinosis type 2 (CLN2) disease to decelerate the progressive motor function decline in patients 3 years of age and older. CLN2 disease is a form of Batten disease, a rare inherited neurodegenerative disorder and is associated with seizures, ataxia, rapid loss of language and motor functions, blindness, and early death [L755]. It is caused by the lack the lysosomal enzyme tripeptidyl peptidase-1 (TPP1) and subsequent accumulation of lysosomal storage materials normally metabolized by this enzyme in the central nervous system. | Cerliponase alfa contains the active substance tripeptidyl peptidase-1 (rhTPP1), a recombinant human lysosomal exopeptidase which cleaves the N-terminal of tripeptides with a broad substrate specificity. Cerliponase alfa slows the progressive decline in motor function caused by abnormal motor signalling in the brain by restoring the normal levels and activity of TPP1. | The mature form of enzyme contains 5 consensus N-glycosylation sites with high mannose, phosphorylated high mannose and complex glycosylation structures. It is taken up by LINCL fibroblasts and translocated to the lysosomes through the Cation Independent Mannose-6-Phosphate Receptor (CI-MPR, also known as M6P/IGF2 receptor). Cerliponase alfa is activated in the lysosome under low pH conditions and the activated proteolytic form of rhTPP1 cleaves tripeptides from the N-terminus of stored proteins. | No data from carcinogenicity, genotoxicity, and fertility studies. Unwanted effects of cerliponase alfa treatment include pyrexia, ECG abnormalities, decreased CSF protein, seizure and hypersensitivity. | Predicted to be metabolized through peptide hydrolysis. | Refer to FDA Label | The estimated CSF volume of distribution of cerliponase alfa following intraventricular infusion of 300mg of Brineura (median Vss = 245 mL) exceeds the typical CSF volume (100 mL) [FDA label]. | Refer to FDA Label | Enzymes and Coenzymes | NA | NA | NA | NA | Cation-independent mannose-6-phosphate receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15170 | Th1570 | Pepsin | >Th1570_Pepsin MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA | NA | NA | NA | NA | NA | NA | Pepsin is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products [L2358]. Studies on gastric digestion from 1820-1840 led to the discovery of pepsin as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by pepsin to products called _peptones_ [A32603]. Pepsin is often used as a replacement enzyme for those with pancreatic insufficiency [L2357]. Stimulation of the pancreas and therefore enzymatic digestion of food is a tightly controlled and is a hormonally mediated process. Any changes or conditions affecting metabolic steps for successful digestion and absorption negatively affect pancreatic enzymatic secretion, entry into the intestine, functionality once inside the intestine, and appropriate mixing with foods/nutrients. Many causes of pancreatic insufficiency require that enzyme replacement therapy is started, including cystic fibrosis, pancreatic cancer, acute and chronic pancreatitis, as well as pancreatic surgery [L2357]. Pepsin is approved by the FDA and is used in food at levels not to exceed current good manufacturing practice [L2363]. Interestingly, it has been used as a marker for laryngopharyngeal reflux (LPR), which is a common illness of otolaryngology (ear, nose and throat specialist) visits [A32604]. Interestingly, recent research has suggested that pepsin participates in the digestion of nucleic acids [L2391]. | Used as a pancreatic enzyme replacement in pancreatic insufficiency [L2357]. It is intended to mimic naturally produced human pepsin [L2360]. Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep [L2367]. In the laboratory, it is primarily used for the unspecific hydrolysis of proteins and peptides in acidic media. In addition, it provides limited hydrolysis of native immunoglobulins, yielding biologically active fragments [L2353]. In certain supplements, pepsin may be combined with betaine and HCl (hydrochloric acid) to aid in digestion in various gastrointestinal conditions [L2360], [L2352]. | Pepsin digests protein [L2358]. It classified by the FDA that is characterizing enzyme activity is that of a peptide _hydrolase_ [L2363]. | Glands present in the mucous membrane lining of the stomach produce and store an inactive protein named _pepsinogen_. Impulses from the vagus nerve and the hormonal secretions of the hormones _gastrin_ and _secretin_ promote the release of pepsinogen into the stomach, where it is mixed with hydrochloric acid and quickly converted to the active enzyme _pepsin_. The digestive potency of pepsin is highest at the acidic pH of normal gastric juice. In the intestine, the gastric acids are then neutralized, and pepsin is no longer effective [L2358]. Pepsin, the proteolytic enzyme of the stomach is normally responsible for less than 20% of the protein digestion occuring the gastrointestinal tract. It is an endopeptidase enzyme that metabolizes proteins to peptides. It preferentially hydrolyzes peptide linkages where one of the amino acids is aromatic. Pepsin, like other protease enzymes, is produced from an inactive precursor, _pepsinogen_, which is stored in granule form in the chief cells of the stomach and are released by a process called _exocytosis_ [L2362]. In the digestive tract, pepsin activity only contributes to the partial breakdown of proteins into smaller units called peptides, which then either are absorbed from the intestine into the bloodstream or are broken down further by pancreatic enzymes [L2358]. | Oral LD50 Rat 90000 mg/kg [MSDS] Chronic backflow of pepsin, acid, and other substances from the stomach into the esophagus, is the basis of reflux conditions, particularly gastroesophageal reflux disease (GERD) and laryngopharyngeal reflux. In the latter, pepsin and acid travel all the way up to the larynx, where they can lead to damage of the laryngeal mucosa and lead to symptoms ranging from hoarseness of the voice and chronic cough to laryngospasm (involuntary contraction of the vocal cords) as well as laryngeal cancer [L2358]. Though limited data is available on the toxicity of exogenous pepsin (not naturally produced in one's gastrointestinal tract), it can be extrapolated from the above-mentioned information that pepsin overdose may lead to mucosal tissue damage of the gastrointestinal tract. | Pepsin is the first of several enzymes that digest proteins. In the stomach, polypeptide chains bind in the deep active site groove of pepsin, and are then digested into smaller pieces. Following this, a variety of proteases and peptidases in the intestine complete the process. The small fragments, which are amino acids and dipeptides, are then absorbed by cells for use as metabolic energy or construction of new proteins [L2361]. | NA | NA | NA | Digestives, Incl. Enzymes | NA | NA | NA | NA | NA | Debiline | Lab Nadeau LtÉe, Division Of Technilab Inc. | Lab Nadeau LtÉe, Division Of Technilab Inc. | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15172 | Th1570 | Pepsin | >Th1570_Pepsin MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA | NA | NA | NA | NA | NA | NA | Pepsin is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products [L2358]. Studies on gastric digestion from 1820-1840 led to the discovery of pepsin as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by pepsin to products called _peptones_ [A32603]. Pepsin is often used as a replacement enzyme for those with pancreatic insufficiency [L2357]. Stimulation of the pancreas and therefore enzymatic digestion of food is a tightly controlled and is a hormonally mediated process. Any changes or conditions affecting metabolic steps for successful digestion and absorption negatively affect pancreatic enzymatic secretion, entry into the intestine, functionality once inside the intestine, and appropriate mixing with foods/nutrients. Many causes of pancreatic insufficiency require that enzyme replacement therapy is started, including cystic fibrosis, pancreatic cancer, acute and chronic pancreatitis, as well as pancreatic surgery [L2357]. Pepsin is approved by the FDA and is used in food at levels not to exceed current good manufacturing practice [L2363]. Interestingly, it has been used as a marker for laryngopharyngeal reflux (LPR), which is a common illness of otolaryngology (ear, nose and throat specialist) visits [A32604]. Interestingly, recent research has suggested that pepsin participates in the digestion of nucleic acids [L2391]. | Used as a pancreatic enzyme replacement in pancreatic insufficiency [L2357]. It is intended to mimic naturally produced human pepsin [L2360]. Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep [L2367]. In the laboratory, it is primarily used for the unspecific hydrolysis of proteins and peptides in acidic media. In addition, it provides limited hydrolysis of native immunoglobulins, yielding biologically active fragments [L2353]. In certain supplements, pepsin may be combined with betaine and HCl (hydrochloric acid) to aid in digestion in various gastrointestinal conditions [L2360], [L2352]. | Pepsin digests protein [L2358]. It classified by the FDA that is characterizing enzyme activity is that of a peptide _hydrolase_ [L2363]. | Glands present in the mucous membrane lining of the stomach produce and store an inactive protein named _pepsinogen_. Impulses from the vagus nerve and the hormonal secretions of the hormones _gastrin_ and _secretin_ promote the release of pepsinogen into the stomach, where it is mixed with hydrochloric acid and quickly converted to the active enzyme _pepsin_. The digestive potency of pepsin is highest at the acidic pH of normal gastric juice. In the intestine, the gastric acids are then neutralized, and pepsin is no longer effective [L2358]. Pepsin, the proteolytic enzyme of the stomach is normally responsible for less than 20% of the protein digestion occuring the gastrointestinal tract. It is an endopeptidase enzyme that metabolizes proteins to peptides. It preferentially hydrolyzes peptide linkages where one of the amino acids is aromatic. Pepsin, like other protease enzymes, is produced from an inactive precursor, _pepsinogen_, which is stored in granule form in the chief cells of the stomach and are released by a process called _exocytosis_ [L2362]. In the digestive tract, pepsin activity only contributes to the partial breakdown of proteins into smaller units called peptides, which then either are absorbed from the intestine into the bloodstream or are broken down further by pancreatic enzymes [L2358]. | Oral LD50 Rat 90000 mg/kg [MSDS] Chronic backflow of pepsin, acid, and other substances from the stomach into the esophagus, is the basis of reflux conditions, particularly gastroesophageal reflux disease (GERD) and laryngopharyngeal reflux. In the latter, pepsin and acid travel all the way up to the larynx, where they can lead to damage of the laryngeal mucosa and lead to symptoms ranging from hoarseness of the voice and chronic cough to laryngospasm (involuntary contraction of the vocal cords) as well as laryngeal cancer [L2358]. Though limited data is available on the toxicity of exogenous pepsin (not naturally produced in one's gastrointestinal tract), it can be extrapolated from the above-mentioned information that pepsin overdose may lead to mucosal tissue damage of the gastrointestinal tract. | Pepsin is the first of several enzymes that digest proteins. In the stomach, polypeptide chains bind in the deep active site groove of pepsin, and are then digested into smaller pieces. Following this, a variety of proteases and peptidases in the intestine complete the process. The small fragments, which are amino acids and dipeptides, are then absorbed by cells for use as metabolic energy or construction of new proteins [L2361]. | NA | NA | NA | Enzyme Preparations | NA | NA | NA | NA | NA | Digestex | Theralab Inc. | Theralab Inc. | Oral | 100 mg / 30 mL | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15173 | Th1570 | Pepsin | >Th1570_Pepsin MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA | NA | NA | NA | NA | NA | NA | Pepsin is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products [L2358]. Studies on gastric digestion from 1820-1840 led to the discovery of pepsin as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by pepsin to products called _peptones_ [A32603]. Pepsin is often used as a replacement enzyme for those with pancreatic insufficiency [L2357]. Stimulation of the pancreas and therefore enzymatic digestion of food is a tightly controlled and is a hormonally mediated process. Any changes or conditions affecting metabolic steps for successful digestion and absorption negatively affect pancreatic enzymatic secretion, entry into the intestine, functionality once inside the intestine, and appropriate mixing with foods/nutrients. Many causes of pancreatic insufficiency require that enzyme replacement therapy is started, including cystic fibrosis, pancreatic cancer, acute and chronic pancreatitis, as well as pancreatic surgery [L2357]. Pepsin is approved by the FDA and is used in food at levels not to exceed current good manufacturing practice [L2363]. Interestingly, it has been used as a marker for laryngopharyngeal reflux (LPR), which is a common illness of otolaryngology (ear, nose and throat specialist) visits [A32604]. Interestingly, recent research has suggested that pepsin participates in the digestion of nucleic acids [L2391]. | Used as a pancreatic enzyme replacement in pancreatic insufficiency [L2357]. It is intended to mimic naturally produced human pepsin [L2360]. Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep [L2367]. In the laboratory, it is primarily used for the unspecific hydrolysis of proteins and peptides in acidic media. In addition, it provides limited hydrolysis of native immunoglobulins, yielding biologically active fragments [L2353]. In certain supplements, pepsin may be combined with betaine and HCl (hydrochloric acid) to aid in digestion in various gastrointestinal conditions [L2360], [L2352]. | Pepsin digests protein [L2358]. It classified by the FDA that is characterizing enzyme activity is that of a peptide _hydrolase_ [L2363]. | Glands present in the mucous membrane lining of the stomach produce and store an inactive protein named _pepsinogen_. Impulses from the vagus nerve and the hormonal secretions of the hormones _gastrin_ and _secretin_ promote the release of pepsinogen into the stomach, where it is mixed with hydrochloric acid and quickly converted to the active enzyme _pepsin_. The digestive potency of pepsin is highest at the acidic pH of normal gastric juice. In the intestine, the gastric acids are then neutralized, and pepsin is no longer effective [L2358]. Pepsin, the proteolytic enzyme of the stomach is normally responsible for less than 20% of the protein digestion occuring the gastrointestinal tract. It is an endopeptidase enzyme that metabolizes proteins to peptides. It preferentially hydrolyzes peptide linkages where one of the amino acids is aromatic. Pepsin, like other protease enzymes, is produced from an inactive precursor, _pepsinogen_, which is stored in granule form in the chief cells of the stomach and are released by a process called _exocytosis_ [L2362]. In the digestive tract, pepsin activity only contributes to the partial breakdown of proteins into smaller units called peptides, which then either are absorbed from the intestine into the bloodstream or are broken down further by pancreatic enzymes [L2358]. | Oral LD50 Rat 90000 mg/kg [MSDS] Chronic backflow of pepsin, acid, and other substances from the stomach into the esophagus, is the basis of reflux conditions, particularly gastroesophageal reflux disease (GERD) and laryngopharyngeal reflux. In the latter, pepsin and acid travel all the way up to the larynx, where they can lead to damage of the laryngeal mucosa and lead to symptoms ranging from hoarseness of the voice and chronic cough to laryngospasm (involuntary contraction of the vocal cords) as well as laryngeal cancer [L2358]. Though limited data is available on the toxicity of exogenous pepsin (not naturally produced in one's gastrointestinal tract), it can be extrapolated from the above-mentioned information that pepsin overdose may lead to mucosal tissue damage of the gastrointestinal tract. | Pepsin is the first of several enzymes that digest proteins. In the stomach, polypeptide chains bind in the deep active site groove of pepsin, and are then digested into smaller pieces. Following this, a variety of proteases and peptidases in the intestine complete the process. The small fragments, which are amino acids and dipeptides, are then absorbed by cells for use as metabolic energy or construction of new proteins [L2361]. | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | Duchol Ect | Duchesnay Inc. | Duchesnay Inc. | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15174 | Th1570 | Pepsin | >Th1570_Pepsin MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA | NA | NA | NA | NA | NA | NA | Pepsin is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products [L2358]. Studies on gastric digestion from 1820-1840 led to the discovery of pepsin as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by pepsin to products called _peptones_ [A32603]. Pepsin is often used as a replacement enzyme for those with pancreatic insufficiency [L2357]. Stimulation of the pancreas and therefore enzymatic digestion of food is a tightly controlled and is a hormonally mediated process. Any changes or conditions affecting metabolic steps for successful digestion and absorption negatively affect pancreatic enzymatic secretion, entry into the intestine, functionality once inside the intestine, and appropriate mixing with foods/nutrients. Many causes of pancreatic insufficiency require that enzyme replacement therapy is started, including cystic fibrosis, pancreatic cancer, acute and chronic pancreatitis, as well as pancreatic surgery [L2357]. Pepsin is approved by the FDA and is used in food at levels not to exceed current good manufacturing practice [L2363]. Interestingly, it has been used as a marker for laryngopharyngeal reflux (LPR), which is a common illness of otolaryngology (ear, nose and throat specialist) visits [A32604]. Interestingly, recent research has suggested that pepsin participates in the digestion of nucleic acids [L2391]. | Used as a pancreatic enzyme replacement in pancreatic insufficiency [L2357]. It is intended to mimic naturally produced human pepsin [L2360]. Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep [L2367]. In the laboratory, it is primarily used for the unspecific hydrolysis of proteins and peptides in acidic media. In addition, it provides limited hydrolysis of native immunoglobulins, yielding biologically active fragments [L2353]. In certain supplements, pepsin may be combined with betaine and HCl (hydrochloric acid) to aid in digestion in various gastrointestinal conditions [L2360], [L2352]. | Pepsin digests protein [L2358]. It classified by the FDA that is characterizing enzyme activity is that of a peptide _hydrolase_ [L2363]. | Glands present in the mucous membrane lining of the stomach produce and store an inactive protein named _pepsinogen_. Impulses from the vagus nerve and the hormonal secretions of the hormones _gastrin_ and _secretin_ promote the release of pepsinogen into the stomach, where it is mixed with hydrochloric acid and quickly converted to the active enzyme _pepsin_. The digestive potency of pepsin is highest at the acidic pH of normal gastric juice. In the intestine, the gastric acids are then neutralized, and pepsin is no longer effective [L2358]. Pepsin, the proteolytic enzyme of the stomach is normally responsible for less than 20% of the protein digestion occuring the gastrointestinal tract. It is an endopeptidase enzyme that metabolizes proteins to peptides. It preferentially hydrolyzes peptide linkages where one of the amino acids is aromatic. Pepsin, like other protease enzymes, is produced from an inactive precursor, _pepsinogen_, which is stored in granule form in the chief cells of the stomach and are released by a process called _exocytosis_ [L2362]. In the digestive tract, pepsin activity only contributes to the partial breakdown of proteins into smaller units called peptides, which then either are absorbed from the intestine into the bloodstream or are broken down further by pancreatic enzymes [L2358]. | Oral LD50 Rat 90000 mg/kg [MSDS] Chronic backflow of pepsin, acid, and other substances from the stomach into the esophagus, is the basis of reflux conditions, particularly gastroesophageal reflux disease (GERD) and laryngopharyngeal reflux. In the latter, pepsin and acid travel all the way up to the larynx, where they can lead to damage of the laryngeal mucosa and lead to symptoms ranging from hoarseness of the voice and chronic cough to laryngospasm (involuntary contraction of the vocal cords) as well as laryngeal cancer [L2358]. Though limited data is available on the toxicity of exogenous pepsin (not naturally produced in one's gastrointestinal tract), it can be extrapolated from the above-mentioned information that pepsin overdose may lead to mucosal tissue damage of the gastrointestinal tract. | Pepsin is the first of several enzymes that digest proteins. In the stomach, polypeptide chains bind in the deep active site groove of pepsin, and are then digested into smaller pieces. Following this, a variety of proteases and peptidases in the intestine complete the process. The small fragments, which are amino acids and dipeptides, are then absorbed by cells for use as metabolic energy or construction of new proteins [L2361]. | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | Dygest | Creative Nutrition Canada Corp. | Creative Nutrition Canada Corp. | Oral | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15213 | Th1572 | Trenonacog alfa | NA | NA | NA | NA | NA | NA | NA | Human coagulation factor IX (EC 3.4.21.22, Christmas factor, plasma thromboplastin component), produced in CHO cells. | NA | NA | NA | NA | NA | NA | NA | NA | Enzyme Precursors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15214 | Th1572 | Trenonacog alfa | NA | NA | NA | NA | NA | NA | NA | Human coagulation factor IX (EC 3.4.21.22, Christmas factor, plasma thromboplastin component), produced in CHO cells. | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15222 | Th1574 | Lysozyme | >Th1574_Lysozyme MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV | NA | NA | NA | NA | NA | NA | 0 | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15223 | Th1574 | Lysozyme | >Th1574_Lysozyme MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV | NA | NA | NA | NA | NA | NA | 0 | NA | NA | NA | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15249 | Th1577 | Tilactase | >Th1577_Tilactase MKLLSVAAVALLAAQAAGASIKHRLNGFTILEHPDPAKRDLLQDIVTWDDKSLFINGERIMLFSGEVHPFRLPVPSLWLDIFHKIRALGFNCVSFYIDWALLEGKPGDYRAEGIFALEPFFDAAKEAGIYLIARPGSYINAEVSGGGFPGWLQRVNGTLRSSDEPFLKATDNYIANAAAAVAKAQITNGGPVILYQPENEYSGGCCGVKYPDADYMQYVMDQARKADIVVPFISNDASPSGHNAPGSGTSAVDIYGHDSYPLGFDCANPSVWPEGKLPDNFRTLHLEQSPSTPYSLLEFQAGAFDPWGGPGFEKCYALVNHEFSRVFYRNDLSFGVSTFNLYMTFGGTNWGNLGHPGGYTSYDYGSPITETRNVTREKYSDIKLLANFVKASPSYLTATPRNLTTGVYTDTSDLAVTPLIGDSPGSFFVVRHTDYSSQESTSYKLKLPTSAGNLTIPQLEGTLSLNGRDSKIHVVDYNVSGTNIIYSTAEVFTWKKFDGNKVLVLYGGPKEHHELAIASKSNVTIIEGSDSGIVSTRKGSSVIIGWDVSSTRRIVQVGDLRVFLLDRNSAYNYWVPELPTEGTSPGFSTSKTTASSIIVKAGYLLRGAHLDGADLHLTADFNATTPIEVIGAPTGAKNLFVNGEKASHTVDKNGIWSSEVKYAAPEIKLPGLKDLDWKYLDTLPEIKSSYDDSAWVSADLPKTKNTHRPLDTPTSLYSSDYGFHTGYLIYRGHFVANGKESEFFIRTQGGSAFGSSVWLNETYLGSWTGADYAMDGNSTYKLSQLESGKNYVITVVIDNLGLDENWTVGEETMKNPRGILSYKLSGQDASAITWKLTGNLGGEDYQDKVRGPLNEGGLYAERQGFHQPQPPSESWESGSPLEGLSKPGIGFYTAQFDLDLPKGWDVPLYFNFGNNTQAARAQLYVNGYQYGKFTGNVGPQTSFPVPEGILNYRGTNYVALSLWALESDGAKLGSFELSYTTPVLTGYGNVESPEQPKYEQRKGAY | 102000 | NA | 4.5 | NA | NA | Tilactase half-life at 35ºC is registered to be 123.77 min. This half-life can be affected by temperature in an inversely proportional manner.[A32597] | Tilactase is a beta-D-galactosidase obtained from _Aspergillus oryzae_. It is produced as a chewable tablet that has to be taken before the consumption of a lactose-containing meal.[A27172] The beta-D-galactosidase us a large monomeric multi-domain enzyme of 985 residues that presents a catalytic (alpha/beta)8-barrel domain.[A32591] It is considered by the WHO as part of the International Nonpropietary Names for Pharmaceutical Substances.[L2338] | Tilactase is indicated for the symptomatic treatment of lactose intolerance in infants and older patients requiring a parenteral nutrition or fluid diet.[L2338] Lactose intolerance occurs when there is an existence of an inability to break down lactose which is commonly found in dairy products. This inability occurs when the lactase levels are reduced and thus there is no via to digest and break down the lactose. The undigested lactose moves into the large intestine where normal flora bacteria can interact with it and cause bloating, gas and diarrhea.[A32592] | The use of a single oral administration of tilactase has been shown to be highly effective in decreasing the symptoms and hydrogen excretion of hypolactasia in tests of lactose H(2)-breath. The analysis has shown a decrease of approximately 80% in both malabsorbers and intolerants.[A27172]The administration of tilacatase also decreases the presence of bloating and flatus.[A27173] | Lactose is the primary disaccharide found in dairy products. Tilactase is a type of lactase which is the enzyme that is in charge of the breakdown of lactose to glucose and galactose which can be used by the body.[L2340] Basically, tilactase acts by replacing the missing lactase in the body and allows avoidance of the reach of lactose to the small intestine and the normal bacteria and thus, preventing the symptoms of the lactose intolerance. Once tilactase has metabolized the lactose, the metabolism products are reabsorbed by the normal process of digestion.[L2345] | Tilactase is known to present a low acute oral toxicity in preclinical trials. The lowest toxic dose for subcutaneous exposure is of 26 g/kg administered over 30 days.[L2340] There have not been performed enough studies regarding the use of pregnancy or related to the fetal development. There are no reports of overdose with tilactase.[L2345] | Tilactase is degraded by the stomach acid and by the normal flora bacterial metabolism.[L2345] | Tilactase is not absorbed in the GI tract and thus the pharmacokinetic parameters related to absorption are not relevant.[L2345] | Tilactase is not absorbed and thus the volume of distribution is not relevant. | Tilactase is not absorbed and thus the clearance rate is not relevant. | Digestives, Incl. Enzymes | NA | NA | NA | NA | Lactose | Lactaid Tab 3300unit | Mcneil Consumer Healthcare Division Of Johnson & Johnson Inc | Mcneil Consumer Healthcare Division Of Johnson & Johnson Inc | Oral | 3300 unit | NA | hives; difficult breathing; swelling of your face, lips, tongue, or throat. | Lactase is often sold as a dietary supplement. There are no regulated manufacturing standards in place for supplements and some marketed products have been found to be contaminated with toxic metals or other drugs. Dietary supplements should be purchased from a reliable source to minimize the risk of contamination. | Lactase is an enzyme that helps your body break down lactose in dairy products. If you are lactose-intolerant, consuming a dairy product can cause gas, bloating, stomach pain, or diarrhea. | NA | NA | Link | Link | NA |
| 15250 | Th1577 | Tilactase | >Th1577_Tilactase MKLLSVAAVALLAAQAAGASIKHRLNGFTILEHPDPAKRDLLQDIVTWDDKSLFINGERIMLFSGEVHPFRLPVPSLWLDIFHKIRALGFNCVSFYIDWALLEGKPGDYRAEGIFALEPFFDAAKEAGIYLIARPGSYINAEVSGGGFPGWLQRVNGTLRSSDEPFLKATDNYIANAAAAVAKAQITNGGPVILYQPENEYSGGCCGVKYPDADYMQYVMDQARKADIVVPFISNDASPSGHNAPGSGTSAVDIYGHDSYPLGFDCANPSVWPEGKLPDNFRTLHLEQSPSTPYSLLEFQAGAFDPWGGPGFEKCYALVNHEFSRVFYRNDLSFGVSTFNLYMTFGGTNWGNLGHPGGYTSYDYGSPITETRNVTREKYSDIKLLANFVKASPSYLTATPRNLTTGVYTDTSDLAVTPLIGDSPGSFFVVRHTDYSSQESTSYKLKLPTSAGNLTIPQLEGTLSLNGRDSKIHVVDYNVSGTNIIYSTAEVFTWKKFDGNKVLVLYGGPKEHHELAIASKSNVTIIEGSDSGIVSTRKGSSVIIGWDVSSTRRIVQVGDLRVFLLDRNSAYNYWVPELPTEGTSPGFSTSKTTASSIIVKAGYLLRGAHLDGADLHLTADFNATTPIEVIGAPTGAKNLFVNGEKASHTVDKNGIWSSEVKYAAPEIKLPGLKDLDWKYLDTLPEIKSSYDDSAWVSADLPKTKNTHRPLDTPTSLYSSDYGFHTGYLIYRGHFVANGKESEFFIRTQGGSAFGSSVWLNETYLGSWTGADYAMDGNSTYKLSQLESGKNYVITVVIDNLGLDENWTVGEETMKNPRGILSYKLSGQDASAITWKLTGNLGGEDYQDKVRGPLNEGGLYAERQGFHQPQPPSESWESGSPLEGLSKPGIGFYTAQFDLDLPKGWDVPLYFNFGNNTQAARAQLYVNGYQYGKFTGNVGPQTSFPVPEGILNYRGTNYVALSLWALESDGAKLGSFELSYTTPVLTGYGNVESPEQPKYEQRKGAY | 102000 | NA | 4.5 | NA | NA | Tilactase half-life at 35ºC is registered to be 123.77 min. This half-life can be affected by temperature in an inversely proportional manner.[A32597] | Tilactase is a beta-D-galactosidase obtained from _Aspergillus oryzae_. It is produced as a chewable tablet that has to be taken before the consumption of a lactose-containing meal.[A27172] The beta-D-galactosidase us a large monomeric multi-domain enzyme of 985 residues that presents a catalytic (alpha/beta)8-barrel domain.[A32591] It is considered by the WHO as part of the International Nonpropietary Names for Pharmaceutical Substances.[L2338] | Tilactase is indicated for the symptomatic treatment of lactose intolerance in infants and older patients requiring a parenteral nutrition or fluid diet.[L2338] Lactose intolerance occurs when there is an existence of an inability to break down lactose which is commonly found in dairy products. This inability occurs when the lactase levels are reduced and thus there is no via to digest and break down the lactose. The undigested lactose moves into the large intestine where normal flora bacteria can interact with it and cause bloating, gas and diarrhea.[A32592] | The use of a single oral administration of tilactase has been shown to be highly effective in decreasing the symptoms and hydrogen excretion of hypolactasia in tests of lactose H(2)-breath. The analysis has shown a decrease of approximately 80% in both malabsorbers and intolerants.[A27172]The administration of tilacatase also decreases the presence of bloating and flatus.[A27173] | Lactose is the primary disaccharide found in dairy products. Tilactase is a type of lactase which is the enzyme that is in charge of the breakdown of lactose to glucose and galactose which can be used by the body.[L2340] Basically, tilactase acts by replacing the missing lactase in the body and allows avoidance of the reach of lactose to the small intestine and the normal bacteria and thus, preventing the symptoms of the lactose intolerance. Once tilactase has metabolized the lactose, the metabolism products are reabsorbed by the normal process of digestion.[L2345] | Tilactase is known to present a low acute oral toxicity in preclinical trials. The lowest toxic dose for subcutaneous exposure is of 26 g/kg administered over 30 days.[L2340] There have not been performed enough studies regarding the use of pregnancy or related to the fetal development. There are no reports of overdose with tilactase.[L2345] | Tilactase is degraded by the stomach acid and by the normal flora bacterial metabolism.[L2345] | Tilactase is not absorbed in the GI tract and thus the pharmacokinetic parameters related to absorption are not relevant.[L2345] | Tilactase is not absorbed and thus the volume of distribution is not relevant. | Tilactase is not absorbed and thus the clearance rate is not relevant. | Enzyme Preparations | NA | NA | NA | NA | Lactose | Lactase 3400 Fcc Units Cap | Attogram Corp | Attogram Corp | Oral | 3400 unit / cap | NA | hives; difficult breathing; swelling of your face, lips, tongue, or throat. | Lactase is often sold as a dietary supplement. There are no regulated manufacturing standards in place for supplements and some marketed products have been found to be contaminated with toxic metals or other drugs. Dietary supplements should be purchased from a reliable source to minimize the risk of contamination. | Lactase is an enzyme that helps your body break down lactose in dairy products. If you are lactose-intolerant, consuming a dairy product can cause gas, bloating, stomach pain, or diarrhea. | NA | NA | Link | Link | NA |
| 15251 | Th1577 | Tilactase | >Th1577_Tilactase MKLLSVAAVALLAAQAAGASIKHRLNGFTILEHPDPAKRDLLQDIVTWDDKSLFINGERIMLFSGEVHPFRLPVPSLWLDIFHKIRALGFNCVSFYIDWALLEGKPGDYRAEGIFALEPFFDAAKEAGIYLIARPGSYINAEVSGGGFPGWLQRVNGTLRSSDEPFLKATDNYIANAAAAVAKAQITNGGPVILYQPENEYSGGCCGVKYPDADYMQYVMDQARKADIVVPFISNDASPSGHNAPGSGTSAVDIYGHDSYPLGFDCANPSVWPEGKLPDNFRTLHLEQSPSTPYSLLEFQAGAFDPWGGPGFEKCYALVNHEFSRVFYRNDLSFGVSTFNLYMTFGGTNWGNLGHPGGYTSYDYGSPITETRNVTREKYSDIKLLANFVKASPSYLTATPRNLTTGVYTDTSDLAVTPLIGDSPGSFFVVRHTDYSSQESTSYKLKLPTSAGNLTIPQLEGTLSLNGRDSKIHVVDYNVSGTNIIYSTAEVFTWKKFDGNKVLVLYGGPKEHHELAIASKSNVTIIEGSDSGIVSTRKGSSVIIGWDVSSTRRIVQVGDLRVFLLDRNSAYNYWVPELPTEGTSPGFSTSKTTASSIIVKAGYLLRGAHLDGADLHLTADFNATTPIEVIGAPTGAKNLFVNGEKASHTVDKNGIWSSEVKYAAPEIKLPGLKDLDWKYLDTLPEIKSSYDDSAWVSADLPKTKNTHRPLDTPTSLYSSDYGFHTGYLIYRGHFVANGKESEFFIRTQGGSAFGSSVWLNETYLGSWTGADYAMDGNSTYKLSQLESGKNYVITVVIDNLGLDENWTVGEETMKNPRGILSYKLSGQDASAITWKLTGNLGGEDYQDKVRGPLNEGGLYAERQGFHQPQPPSESWESGSPLEGLSKPGIGFYTAQFDLDLPKGWDVPLYFNFGNNTQAARAQLYVNGYQYGKFTGNVGPQTSFPVPEGILNYRGTNYVALSLWALESDGAKLGSFELSYTTPVLTGYGNVESPEQPKYEQRKGAY | 102000 | NA | 4.5 | NA | NA | Tilactase half-life at 35ºC is registered to be 123.77 min. This half-life can be affected by temperature in an inversely proportional manner.[A32597] | Tilactase is a beta-D-galactosidase obtained from _Aspergillus oryzae_. It is produced as a chewable tablet that has to be taken before the consumption of a lactose-containing meal.[A27172] The beta-D-galactosidase us a large monomeric multi-domain enzyme of 985 residues that presents a catalytic (alpha/beta)8-barrel domain.[A32591] It is considered by the WHO as part of the International Nonpropietary Names for Pharmaceutical Substances.[L2338] | Tilactase is indicated for the symptomatic treatment of lactose intolerance in infants and older patients requiring a parenteral nutrition or fluid diet.[L2338] Lactose intolerance occurs when there is an existence of an inability to break down lactose which is commonly found in dairy products. This inability occurs when the lactase levels are reduced and thus there is no via to digest and break down the lactose. The undigested lactose moves into the large intestine where normal flora bacteria can interact with it and cause bloating, gas and diarrhea.[A32592] | The use of a single oral administration of tilactase has been shown to be highly effective in decreasing the symptoms and hydrogen excretion of hypolactasia in tests of lactose H(2)-breath. The analysis has shown a decrease of approximately 80% in both malabsorbers and intolerants.[A27172]The administration of tilacatase also decreases the presence of bloating and flatus.[A27173] | Lactose is the primary disaccharide found in dairy products. Tilactase is a type of lactase which is the enzyme that is in charge of the breakdown of lactose to glucose and galactose which can be used by the body.[L2340] Basically, tilactase acts by replacing the missing lactase in the body and allows avoidance of the reach of lactose to the small intestine and the normal bacteria and thus, preventing the symptoms of the lactose intolerance. Once tilactase has metabolized the lactose, the metabolism products are reabsorbed by the normal process of digestion.[L2345] | Tilactase is known to present a low acute oral toxicity in preclinical trials. The lowest toxic dose for subcutaneous exposure is of 26 g/kg administered over 30 days.[L2340] There have not been performed enough studies regarding the use of pregnancy or related to the fetal development. There are no reports of overdose with tilactase.[L2345] | Tilactase is degraded by the stomach acid and by the normal flora bacterial metabolism.[L2345] | Tilactase is not absorbed in the GI tract and thus the pharmacokinetic parameters related to absorption are not relevant.[L2345] | Tilactase is not absorbed and thus the volume of distribution is not relevant. | Tilactase is not absorbed and thus the clearance rate is not relevant. | Enzymes | NA | NA | NA | NA | Lactose | Lactase Enzyme | Holista Health (Canada) Inc. | Holista Health (Canada) Inc. | Oral | 3000 unit | NA | hives; difficult breathing; swelling of your face, lips, tongue, or throat. | Lactase is often sold as a dietary supplement. There are no regulated manufacturing standards in place for supplements and some marketed products have been found to be contaminated with toxic metals or other drugs. Dietary supplements should be purchased from a reliable source to minimize the risk of contamination. | Lactase is an enzyme that helps your body break down lactose in dairy products. If you are lactose-intolerant, consuming a dairy product can cause gas, bloating, stomach pain, or diarrhea. | NA | NA | Link | Link | NA |
| 15252 | Th1577 | Tilactase | >Th1577_Tilactase MKLLSVAAVALLAAQAAGASIKHRLNGFTILEHPDPAKRDLLQDIVTWDDKSLFINGERIMLFSGEVHPFRLPVPSLWLDIFHKIRALGFNCVSFYIDWALLEGKPGDYRAEGIFALEPFFDAAKEAGIYLIARPGSYINAEVSGGGFPGWLQRVNGTLRSSDEPFLKATDNYIANAAAAVAKAQITNGGPVILYQPENEYSGGCCGVKYPDADYMQYVMDQARKADIVVPFISNDASPSGHNAPGSGTSAVDIYGHDSYPLGFDCANPSVWPEGKLPDNFRTLHLEQSPSTPYSLLEFQAGAFDPWGGPGFEKCYALVNHEFSRVFYRNDLSFGVSTFNLYMTFGGTNWGNLGHPGGYTSYDYGSPITETRNVTREKYSDIKLLANFVKASPSYLTATPRNLTTGVYTDTSDLAVTPLIGDSPGSFFVVRHTDYSSQESTSYKLKLPTSAGNLTIPQLEGTLSLNGRDSKIHVVDYNVSGTNIIYSTAEVFTWKKFDGNKVLVLYGGPKEHHELAIASKSNVTIIEGSDSGIVSTRKGSSVIIGWDVSSTRRIVQVGDLRVFLLDRNSAYNYWVPELPTEGTSPGFSTSKTTASSIIVKAGYLLRGAHLDGADLHLTADFNATTPIEVIGAPTGAKNLFVNGEKASHTVDKNGIWSSEVKYAAPEIKLPGLKDLDWKYLDTLPEIKSSYDDSAWVSADLPKTKNTHRPLDTPTSLYSSDYGFHTGYLIYRGHFVANGKESEFFIRTQGGSAFGSSVWLNETYLGSWTGADYAMDGNSTYKLSQLESGKNYVITVVIDNLGLDENWTVGEETMKNPRGILSYKLSGQDASAITWKLTGNLGGEDYQDKVRGPLNEGGLYAERQGFHQPQPPSESWESGSPLEGLSKPGIGFYTAQFDLDLPKGWDVPLYFNFGNNTQAARAQLYVNGYQYGKFTGNVGPQTSFPVPEGILNYRGTNYVALSLWALESDGAKLGSFELSYTTPVLTGYGNVESPEQPKYEQRKGAY | 102000 | NA | 4.5 | NA | NA | Tilactase half-life at 35ºC is registered to be 123.77 min. This half-life can be affected by temperature in an inversely proportional manner.[A32597] | Tilactase is a beta-D-galactosidase obtained from _Aspergillus oryzae_. It is produced as a chewable tablet that has to be taken before the consumption of a lactose-containing meal.[A27172] The beta-D-galactosidase us a large monomeric multi-domain enzyme of 985 residues that presents a catalytic (alpha/beta)8-barrel domain.[A32591] It is considered by the WHO as part of the International Nonpropietary Names for Pharmaceutical Substances.[L2338] | Tilactase is indicated for the symptomatic treatment of lactose intolerance in infants and older patients requiring a parenteral nutrition or fluid diet.[L2338] Lactose intolerance occurs when there is an existence of an inability to break down lactose which is commonly found in dairy products. This inability occurs when the lactase levels are reduced and thus there is no via to digest and break down the lactose. The undigested lactose moves into the large intestine where normal flora bacteria can interact with it and cause bloating, gas and diarrhea.[A32592] | The use of a single oral administration of tilactase has been shown to be highly effective in decreasing the symptoms and hydrogen excretion of hypolactasia in tests of lactose H(2)-breath. The analysis has shown a decrease of approximately 80% in both malabsorbers and intolerants.[A27172]The administration of tilacatase also decreases the presence of bloating and flatus.[A27173] | Lactose is the primary disaccharide found in dairy products. Tilactase is a type of lactase which is the enzyme that is in charge of the breakdown of lactose to glucose and galactose which can be used by the body.[L2340] Basically, tilactase acts by replacing the missing lactase in the body and allows avoidance of the reach of lactose to the small intestine and the normal bacteria and thus, preventing the symptoms of the lactose intolerance. Once tilactase has metabolized the lactose, the metabolism products are reabsorbed by the normal process of digestion.[L2345] | Tilactase is known to present a low acute oral toxicity in preclinical trials. The lowest toxic dose for subcutaneous exposure is of 26 g/kg administered over 30 days.[L2340] There have not been performed enough studies regarding the use of pregnancy or related to the fetal development. There are no reports of overdose with tilactase.[L2345] | Tilactase is degraded by the stomach acid and by the normal flora bacterial metabolism.[L2345] | Tilactase is not absorbed in the GI tract and thus the pharmacokinetic parameters related to absorption are not relevant.[L2345] | Tilactase is not absorbed and thus the volume of distribution is not relevant. | Tilactase is not absorbed and thus the clearance rate is not relevant. | Enzymes and Coenzymes | NA | NA | NA | NA | Lactose | Lactase Enzyme | Holista Health (Canada) Inc. | Holista Health (Canada) Inc. | Oral | 3300 unit / cap | NA | hives; difficult breathing; swelling of your face, lips, tongue, or throat. | Lactase is often sold as a dietary supplement. There are no regulated manufacturing standards in place for supplements and some marketed products have been found to be contaminated with toxic metals or other drugs. Dietary supplements should be purchased from a reliable source to minimize the risk of contamination. | Lactase is an enzyme that helps your body break down lactose in dairy products. If you are lactose-intolerant, consuming a dairy product can cause gas, bloating, stomach pain, or diarrhea. | NA | NA | Link | Link | NA |
| 15265 | Th1579 | Albutrepenonacog alfa | >Th1579_Albutrepenonacog_alfa YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLTPVSQTSKLTRAETVFPDVDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL | 125000 | C5077N7846O1588PS67 | NA | NA | NA | The fusion of the rFIX with rAlbumin prolongs the elimination half-life of rIX-RFP in the circulation. The reported half-life in clinical trials is 92 hours.[A32547] | Albutrepenonacog alfa (rIX-RFP) is a recombinant fusion protein that links a recombinant coagulation factor IX (rFIX) with a recombinant human albumin (rAlbumin).[A32547] It was developed by CSL Behring Canada, Inc and approved by Health Canada on April 26, 2017. It was also approved by FDA and EMA in 2016. It is currently marketed in the forms of 250, 500, 1000 and 2000 IU/vial.[L2305] | Under the EMA and FDA, rIX-RFP is indicated in the treatment of hemophilia B.[L2306] For Health Canada, rIX-FRP is also indicated to prevent or reduce bleeding episodes.[L2305] Hemophilia B is the second most common type of hemophilia. It is a rare inherited bleeding disorder caused by reduced or absent levels of factor IX (FIX). The FIX is a vitamin K-dependent plasma protease that when activated is involved in the blood coagulation cascade.[A32551] The hemophilia B is caused by mutations in the _FIX_ gene which can cause different phenotypes. The severe form is characterized by the presence of spontaneous and recurring bleeds into the joints and muscles and excessive bleeding after trauma or surgery.[A32552] | Clinical trials with rIX-RFP in patients with moderately to severe hemophilia B demonstrated a lower annualized spontaneous, total and joint bleeding rates. It was also efficient against bleeding episodes and maintenance of hemostasis in the perioperative setting when compared with on-demand treatment. The administration of rIX-RFP presented no reports of inhibitor development.[A32547] | The current therapies against hemophilia B are hampered by the short half-life of the replacement FIX therapy.[A32547] Thus, to solve this problem, in rIX-RFP there is the fusion of rFIX with rAlbumin which presents a much longer half-life and it does not present interactions with the immune system.[A32547] The administration of rIX-RFP increases the plasma concentration of FIX, thus addressing the coagulation deficiency of the patient. rIX-RFP is able to circulate in the plasma as an intact zymogen thanks to the pH-dependent binding to FcRn which is a normal protection pathway from lysosomal degradation of albumin. When the FIX is needed, rAlbumin is cleaved by the same proteases that activate the FIX.[A32547] | rIX-RFP is very well tolerated.[A32547]Mutaginicity trials were performed and they confirmed an absent mutagenic potential.[L2305]Fertility studies have not been performed. Developmental studies are not of major importance as there is a very low rate of incidence of hemophilia B in females. | The metabolism of rIX-RFP is not relevant as it is a recombinant protein and it is thought to be metabolized to peptides and amino acids.[L2313] | rIX-RFP absorption is very rapid as it is directly administered intravenously. In clinical trials, the maximum plasma concentration, area under the curve and mean residence time are reported to be approximately 55 IU/dL, 5500 IU.h/dL and 125 hours respectively.[A32547] | The reported volume of distribution for rIX-RFP according to phase I/II and III clinical trials is 95 ml/kg.[A32556] | In clinical trials, the weight-adjusted clearance in children and adults is reported to be 1.1 and 0.9 ml/h/kg.[A32547] | Enzyme Precursors | NA | NA | NA | NA | Coagulation factor X | Idelvion | Csl Behring | Csl Behring | Intravenous | 1000 IU | IDELVION, Coagulation Factor IX (Recombinant), Albumin Fusion Protein (rIX-FP), is contraindicated in patients who have a known hypersensitivity to IDELVION, any of its components, excipients or hamster protein. For a complete listing, see Dosage Forms, Composition And Packaging. | headache, dizziness, rash, and infusion site reaction | Idelvion is used to treat or prevent bleeding in people with hemophilia B. This medication is not for treating people with hemophilia A factor VIII deficiency. Idelvion may also be used for purposes not listed in this medication guide. Warnings Follow all directions on your medicine label and package.... | Idelvion is a prescription medicine used as prophylaxis and to treat the symptoms of Hemophilia B. Idelvion may be used alone or with other medications. | NA | NA | Link | Link | NA |
| 15266 | Th1579 | Albutrepenonacog alfa | >Th1579_Albutrepenonacog_alfa YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLTPVSQTSKLTRAETVFPDVDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL | 125000 | C5077N7846O1588PS67 | NA | NA | NA | The fusion of the rFIX with rAlbumin prolongs the elimination half-life of rIX-RFP in the circulation. The reported half-life in clinical trials is 92 hours.[A32547] | Albutrepenonacog alfa (rIX-RFP) is a recombinant fusion protein that links a recombinant coagulation factor IX (rFIX) with a recombinant human albumin (rAlbumin).[A32547] It was developed by CSL Behring Canada, Inc and approved by Health Canada on April 26, 2017. It was also approved by FDA and EMA in 2016. It is currently marketed in the forms of 250, 500, 1000 and 2000 IU/vial.[L2305] | Under the EMA and FDA, rIX-RFP is indicated in the treatment of hemophilia B.[L2306] For Health Canada, rIX-FRP is also indicated to prevent or reduce bleeding episodes.[L2305] Hemophilia B is the second most common type of hemophilia. It is a rare inherited bleeding disorder caused by reduced or absent levels of factor IX (FIX). The FIX is a vitamin K-dependent plasma protease that when activated is involved in the blood coagulation cascade.[A32551] The hemophilia B is caused by mutations in the _FIX_ gene which can cause different phenotypes. The severe form is characterized by the presence of spontaneous and recurring bleeds into the joints and muscles and excessive bleeding after trauma or surgery.[A32552] | Clinical trials with rIX-RFP in patients with moderately to severe hemophilia B demonstrated a lower annualized spontaneous, total and joint bleeding rates. It was also efficient against bleeding episodes and maintenance of hemostasis in the perioperative setting when compared with on-demand treatment. The administration of rIX-RFP presented no reports of inhibitor development.[A32547] | The current therapies against hemophilia B are hampered by the short half-life of the replacement FIX therapy.[A32547] Thus, to solve this problem, in rIX-RFP there is the fusion of rFIX with rAlbumin which presents a much longer half-life and it does not present interactions with the immune system.[A32547] The administration of rIX-RFP increases the plasma concentration of FIX, thus addressing the coagulation deficiency of the patient. rIX-RFP is able to circulate in the plasma as an intact zymogen thanks to the pH-dependent binding to FcRn which is a normal protection pathway from lysosomal degradation of albumin. When the FIX is needed, rAlbumin is cleaved by the same proteases that activate the FIX.[A32547] | rIX-RFP is very well tolerated.[A32547]Mutaginicity trials were performed and they confirmed an absent mutagenic potential.[L2305]Fertility studies have not been performed. Developmental studies are not of major importance as there is a very low rate of incidence of hemophilia B in females. | The metabolism of rIX-RFP is not relevant as it is a recombinant protein and it is thought to be metabolized to peptides and amino acids.[L2313] | rIX-RFP absorption is very rapid as it is directly administered intravenously. In clinical trials, the maximum plasma concentration, area under the curve and mean residence time are reported to be approximately 55 IU/dL, 5500 IU.h/dL and 125 hours respectively.[A32547] | The reported volume of distribution for rIX-RFP according to phase I/II and III clinical trials is 95 ml/kg.[A32556] | In clinical trials, the weight-adjusted clearance in children and adults is reported to be 1.1 and 0.9 ml/h/kg.[A32547] | Enzymes and Coenzymes | NA | NA | NA | NA | Coagulation factor X | Idelvion | CSL Behring Lengnau AG | CSL Behring Lengnau AG | Intravenous | 2000 [iU]/5mL | IDELVION, Coagulation Factor IX (Recombinant), Albumin Fusion Protein (rIX-FP), is contraindicated in patients who have a known hypersensitivity to IDELVION, any of its components, excipients or hamster protein. For a complete listing, see Dosage Forms, Composition And Packaging. | headache, dizziness, rash, and infusion site reaction | Idelvion is used to treat or prevent bleeding in people with hemophilia B. This medication is not for treating people with hemophilia A factor VIII deficiency. Idelvion may also be used for purposes not listed in this medication guide. Warnings Follow all directions on your medicine label and package.... | Idelvion is a prescription medicine used as prophylaxis and to treat the symptoms of Hemophilia B. Idelvion may be used alone or with other medications. | NA | NA | Link | Link | NA |
| 15513 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Enzymes | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15514 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Enzymes and Coenzymes | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15579 | Th1609 | Elapegademase | >Th1609_Elapegademase AQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGSREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDTTLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPA | 115000 | C1797H2795N477O544S12 | NA | NA | NA | This pharmacokinetic property has not been fully studied. | Elapegademase is a PEGylated recombinant adenosine deaminase. It can be defined molecularly as a genetically modified bovine adenosine deaminase with a modification in cysteine 74 for serine and with about 13 methoxy polyethylene glycol chains bound via carbonyl group in alanine and lysine residues.[F1937] Elapegademase is generated in _E. coli_, developed by Leadiant Biosciences and FDA approved on October 5, 2018.[L4654,F1939] | Elapegademase is approved for the treatment of adenosine deaminase severe combined immune deficiency (ADA-SCID) in pediatric and adult patients.[L4654] This condition was previously treated by the use of bovine pegamedase as part of an enzyme replacement therapy.[L4655] ADA-SCID is a genetically inherited disorder that is very rare and characterized by a deficiency in the adenosine deaminase enzyme. The patients suffering from this disease often present with a compromised immune system. This condition is characterized by very low levels of white blood cells and immunoglobulin levels which results in severe and recurring infections.[L4656] | In clinical trials, elapegademase was shown to increase adenosine deaminase activity while reducing the concentrations of toxic metabolites which are the hallmark of ADA-SCID. As well, it was shown to improve the total lymphocyte count.[F1940] | The ADA-SCID is caused by the presence of mutations in the ADA gene which is responsible for the synthesis of adenosine deaminase. This enzyme is found throughout the body but it is mainly active in lymphocytes. The normal function of adenosine deaminase is to eliminate deoxyadenosine, created when DNA is degraded, by converting it into deoxyinosine. This degradation process is very important as deoxyadenosine is cytotoxic, especially for lymphocytes. Immature lymphocytes are particularly vulnerable as deoxyadenosine kills them before maturation making them unable to produce their immune function.[L4656] Therefore, based on the causes of ADA-SCID, elapegademase works by supplementing the levels of adenosine deaminase. Being a recombinant and an _E. coli_-produced molecule, the use of this drug eliminates the need to source the enzyme from animals, as it was previously.[L4654] | As elapegademase is a therapeutic protein, there is a potential risk of immunogenicity. There are no studies related to overdose but the highest weekly prescribed dose in clinical trials was 0.4 mg/kg. In nonclinical studies, a dosage of 1.8 fold of the clinical dose produced a slight increase in the activated partial thromboplastin time.[FDA label] | Metabolism studies have not been performed but it is thought to be degraded by proteases to small peptides and individual amino acids. | Elapegademase is administered intramuscularly and the reported Tmax, Cmax and AUC are approximately 60 hours, 240 mmol.h/L and 33000 hr.mmol/L as reported during a week.[FDA label] | This pharmacokinetic property has not been fully studied. | This pharmacokinetic property has not been fully studied. | Enzyme Replacement Therapy | NA | NA | NA | NA | Adenosine | NA | NA | NA | NA | NA | NA | NA | NA | NA | (2S)-2-amino-6-(2-methoxyethoxycarbonylamino)hexanoic acid | NA | Link | NA | NA |
| 15737 | Th1622 | Somapacitan | >Th1622_Somapacitan FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSCVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | NA | C1038H1609N273O319S9 | NA | NA | NA | The elimination half life of somapacitan is 2-3 days.[L15661] | Somapacitan, also known as NNC0195-0092,[A219136] is a growth hormone analog indicated to treat adults with growth hormone deficiency.[A219126,L15661] This human growth hormone analog differs by the creation of an albumin binding site, and prolonging the effect so that it requires weekly dosing rather than daily.[A219146] Somapacitan was granted FDA approval on 28 August 2020.[L15666] | Somapacitan is indicated as a replacement for growth hormone in adult patients with growth hormone deficiency.[L15661] | Somapacitan stimulates the growth hormone receptor.[L15661] Somapacitan has a long duration of action as it is given once weekly.[L15661] It has a moderately wide therapeutic window as an acute overdose may cause hypoglycemia followed by hyperglycemia.[L15661] Patients should be counselled regarding the risk of increased mortality in patients with critical illness, risk of neoplasms, glucose intolerance in diabetes mellitus, intracranial hypertension, hypersensitivity, fluid retention, hypoadrenalism, hypothyroidism, pancreatitis, lipohypertrophy, and lipoatrophy.[L15661] | Somapacitan binds to the growth hormone receptor and induces intracellular signalling to up-regulate insulin-like growth factor I (IGF-1).[A219096,L15661] IGF-1 causes growth in bones and muscle tissue.[A219096] Growth hormones more directly cause the fusion of myoblasts and myotubes to cause muscle fibre growth, activate neural stem cells, and induce chondrocyte proliferation.[A219096] | Patients experiencing an acute overdose of somapacitan may present with fluid retention.[L15661] Chronic overdose may resemble gigantism or acromegaly.[L15661] Treat patients with symptomatic and supportive measures to minimize the permanent effects.[A219141] | Studies in humans and rats show that somapacitan is metabolized through cleavage of the albumin-binding moiety and linker sidechain before further non-specific mechanisms.[A219096,L15661] | A 0.02mg/kg single dose of somapacitan reaches a Cmax of 14.4 ng/mL, with a Tmax of 11.1 hours, and an AUC of 475 ng | The approximate volume of distribution of somapacitan is 14.6 L.[L15661] | The apparent maximum rate of saturable elimination is estimated to be 0.268 ± 0.03 mg/h.[A219126] | Cytochrome P-450 Enzyme Inducers | NA | NA | NA | NA | Growth hormone receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | (2S)-5-[2-[2-[2-[[(2S)-1-amino-6-[[2-[(2R)-2-amino-2-carboxyethyl]sulfanylacetyl]amino]-1-oxohexan-2-yl]amino]-2-oxoethoxy]ethoxy]ethylamino]-2-[[(4S)-4-carboxy-4-[[2-[2-[2-[4-[16-(2H-tetrazol-5-yl)hexadecanoylsulfamoyl]butanoylamino]ethoxy]ethoxy]acetyl]amino]butanoyl]amino]-5-oxopentanoic acid | NA | Link | NA | NA |
| 15738 | Th1622 | Somapacitan | >Th1622_Somapacitan FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSCVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | NA | C1038H1609N273O319S9 | NA | NA | NA | The elimination half life of somapacitan is 2-3 days.[L15661] | Somapacitan, also known as NNC0195-0092,[A219136] is a growth hormone analog indicated to treat adults with growth hormone deficiency.[A219126,L15661] This human growth hormone analog differs by the creation of an albumin binding site, and prolonging the effect so that it requires weekly dosing rather than daily.[A219146] Somapacitan was granted FDA approval on 28 August 2020.[L15666] | Somapacitan is indicated as a replacement for growth hormone in adult patients with growth hormone deficiency.[L15661] | Somapacitan stimulates the growth hormone receptor.[L15661] Somapacitan has a long duration of action as it is given once weekly.[L15661] It has a moderately wide therapeutic window as an acute overdose may cause hypoglycemia followed by hyperglycemia.[L15661] Patients should be counselled regarding the risk of increased mortality in patients with critical illness, risk of neoplasms, glucose intolerance in diabetes mellitus, intracranial hypertension, hypersensitivity, fluid retention, hypoadrenalism, hypothyroidism, pancreatitis, lipohypertrophy, and lipoatrophy.[L15661] | Somapacitan binds to the growth hormone receptor and induces intracellular signalling to up-regulate insulin-like growth factor I (IGF-1).[A219096,L15661] IGF-1 causes growth in bones and muscle tissue.[A219096] Growth hormones more directly cause the fusion of myoblasts and myotubes to cause muscle fibre growth, activate neural stem cells, and induce chondrocyte proliferation.[A219096] | Patients experiencing an acute overdose of somapacitan may present with fluid retention.[L15661] Chronic overdose may resemble gigantism or acromegaly.[L15661] Treat patients with symptomatic and supportive measures to minimize the permanent effects.[A219141] | Studies in humans and rats show that somapacitan is metabolized through cleavage of the albumin-binding moiety and linker sidechain before further non-specific mechanisms.[A219096,L15661] | A 0.02mg/kg single dose of somapacitan reaches a Cmax of 14.4 ng/mL, with a Tmax of 11.1 hours, and an AUC of 475 ng | The approximate volume of distribution of somapacitan is 14.6 L.[L15661] | The apparent maximum rate of saturable elimination is estimated to be 0.268 ± 0.03 mg/h.[A219126] | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | Growth hormone receptor | NA | NA | NA | NA | NA | NA | NA | NA | NA | (2S)-5-[2-[2-[2-[[(2S)-1-amino-6-[[2-[(2R)-2-amino-2-carboxyethyl]sulfanylacetyl]amino]-1-oxohexan-2-yl]amino]-2-oxoethoxy]ethoxy]ethylamino]-2-[[(4S)-4-carboxy-4-[[2-[2-[2-[4-[16-(2H-tetrazol-5-yl)hexadecanoylsulfamoyl]butanoylamino]ethoxy]ethoxy]acetyl]amino]butanoyl]amino]-5-oxopentanoic acid | NA | Link | NA | NA |
| 15764 | Th1624 | Ropeginterferon alfa-2b | >Th1624_Ropeginterferon_alfa-2b PCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE | 60000 | C16H29N3O6(C2H4O)n(C2H4O)n | NA | NA | NA | Ropeginterferon alfa-2b administered to polycythemia vera patients over a dose range of 100-500 µg has a half-life of approximately seven days.[L39170] | Polycythemia vera (PV) is the most common Philadelphia chromosome-negative myeloproliferative neoplasm (MPN), characterized by increased hematocrit and platelet/leukocyte counts, an increased risk for hemorrhage and thromboembolic events, and a long-term propensity for myelofibrosis and leukemia.[A242000, A242005] [Interferon alfa-2b] has been used for decades to treat PV but requires frequent dosing and is not tolerated by all patients.[A242005] Ropeginterferon alfa-2b is a next-generation mono-pegylated type I interferon produced from proline-IFN-a-2b in _Escherichia coli_ that has high tolerability and a long half-life.[A242015, L39170] Ropeginterferon alfa-2b has shown efficacy in PV in _in vitro_ and _in vivo_ models and clinical trials.[A242010, A242015] Ropeginterferon alfa-2b was approved by the FDA on November 12, 2021, and is currently marketed under the trademark BESREMi by PharmaEssentia Corporation.[L39170] | Ropeginterferon alfa-2b is indicated for the treatment of adult patients with polycythemia vera.[L39170] | Ropeginterferon alfa-2b acts through the interferon-alpha/beta receptor to initiate downstream JAK/STAT signalling leading to its therapeutic effects. Like other interferon alfa products, ropeginterferon alfa-2b may cause various toxicities, including endocrine, cardiovascular, pulmonary, ophthalmologic, dental/periodontal, renal, and dermatological toxicity. In addition, interferon alfa has been associated with hepatotoxicity, including increases in serum ALT, AST, GGT, and bilirubin; ropeginterferon alfa-2b is contraindicated in patients with moderate to severe (Child-Pugh B or C) hepatic impairment. Pancreatitis and colitis, including fatal ulcerative/hemorrhagic/ischemic colitis, have occurred in patients treated with interferon alfa. Significant toxicity of any kind may require treatment discontinuation. Interferon alfa treatment has decreased peripheral blood counts, including thrombocytopenia and leukopenia, and altered lipid levels, including hyperlipidemia, hypertriglyceridemia, and dyslipidemia. Hypersensitivity reactions, including anaphylaxis, may occur; ropeginterferon alfa-2b is contraindicated in hypersensitive patients and those with known hypersensitivity to other interferons. Life-threatening or fatal neuropsychiatric reactions may occur, including in patients without prior history; ropeginterferon alfa-2b is contraindicated in patients with a history of severe psychiatric disorders. Finally, ropeginterferon alfa-2b can cause fetal harm and should be used with caution in females of reproductive potential.[L39170] | Polycythemia vera (PV) is the most common Philadelphia chromosome-negative myeloproliferative neoplasm (MPN), which also includes essential thrombocytopenia and myelofibrosis.[A242000, A242005] PV is characterized by increased hematocrit and platelet/leukocyte counts, an increased risk for hemorrhage and thromboembolic events, and a long-term propensity for myelofibrosis and leukemia. The main driver mutation, _JAK2_ V617F, is present in >95% of PV patients and results in constitutive JAK/STAT signalling; other exon 12 mutations in _JAK2_ may also result in PV. PV results in clonal hematopoietic stem cells, such that they form endogenous erythroid colonies (EECs) _in vitro_.[A242000] Interferon alfa-2b has been used for decades in PV despite the lack of formal approval.[A242005] Although the mechanism of action is unclear, interferon alfa-2b is known to bind the interferon-alpha/beta receptor (IFNAR) and activate downstream JAK/STAT signalling.[A242005, L39170] The overall result is a series of anti-proliferative, anti-angiogenic, pro-apoptotic, and immunomodulatory effects, including augmenting T-cell, macrophage, and natural killer cells.[A242005] Interestingly, _in vitro_ studies have revealed that ropeginterferon alfa-2b is specific to some extent for _JAK2_-mutant EECs, a result that is in line with the reduced allelic burden observed in clinical trials.[A242010, A242015] Partial and complete molecular and hematological responses have been achieved with ropeginterferon alfa-2b.[A242015] | Ropeginterferon alfa-2b overdose may present with influenza-like symptoms or other adverse reactions. As there is no known antidote, symptomatic and supportive care should be administered in the result of an overdose. Ropeginterferon alfa-2b is not mutagenic in standard assays but has not been tested for carcinogenic potential.[L39170] | Ropeginterferon alfa-2b is expected to be catabolized by various proteolytic enzymes.[L15811] | In patients with polycythemia vera on a two-week dosing interval, the estimated steady-state Cmin was 1.4-12 ng/mL, Cmax was 4.4-31 ng/mL, and AUC was 1011-7809 ng | Ropeginterferon alfa-2b has an estimated geometric mean apparent volume of distribution (%CV) of 4.8 L (21%) in polycythemia vera patients.[L39170] | Ropeginterferon alfa-2b administered to polycythemia vera patients over a dose range of 100-500 µg has a clearance of 1.7-2.5 L/h.[L39170] | Cytochrome P-450 Enzyme Inhibitors | NA | NA | NA | NA | Interferon alpha/beta receptor (IFNAR) | NA | NA | NA | NA | NA | NA | NA | NA | NA | (2S)-1-[3,7-bis(2-methoxyethoxycarbonylamino)heptyl]pyrrolidine-2-carboxylic acid | NA | Link | NA | NA |
| 15938 | Th1653 | Agalsidase alfa | >Th1653_Agalsidase_alfa LDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL | 45351.6 | C2029H3080N544O587S27 | NA | NA | NA | The elimination half life was 108 ± 17 minutes for males and 89 ± 28 minutes for females.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A similar to [agalsidase beta]. While patients generally do not experience a clinically significant difference in outcomes between the two drugs, some patients may experience greater benefit with agalsidase beta.[A220228,A220233] Use of agalsidase beta has decreased in Europe, in favor of agalsidase alfa, after a contamination event in 2009.[A220343] Agalsidase alfa was granted EMA approval on 3 August 2001.[L16413] | Agalsidase alfa is indicated in the treatment of Fabry disease.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A used as enzyme replacement therapy in the treatment of Fabry disease.[L16398] It has a long duration of action and a wide therapeutic index.[L16398] Patients should be counselled regarding the risk of infusion related reactions and hypersensitivity.[L16398] | a-galactosidase A is uptaken by cells via the mannose 6 phosphate receptor.[A220323] Agalsidase alfa hydrolyzes globotriaosylceramide and other glycosphingolipids that would normally be hydrolyzed by endogenous a-galactosidase A.[L16398] Preventing the accumulation of glycosphingolipids prevents or reduces the severity of manifestations of Fabry disease such as renal failure, cardiomyopathy, or cerebrovascular events.[L16398] | Data regarding overdoses of agalsidase alfa are not readily available.[L16398] Patients experiencing an overdose of agalsidase alfa may experience an increased incidence and severity of adverse effects. Overdose can be managed through the use of symptomatic and supportive measures. | Data regarding the metabolism of agalsidase alfa is not readily available.[L16398] However, protein drugs are expected to be degraded by proteases and other catalytic enzymes to smaller peptides and amino acids.[A182009] | A dose of agalsidase alfa in non end stage renal disease patients reaches a Cmax of 3710 ± 855 U/mL with an AUC of 256,958 ± 63,499 min | The volume of distribution at steady state in non end stage renal disease patients was approximately 17% of body weight regardless of sex.[A220338,L16398] | The clearance for doses of 0.007-0.2 mg/kg were 2.66 mL/min/kg for males and 2.10 mL/min/kg for females.[L16398] | Enzyme Replacement Therapy | NA | NA | NA | NA | Globotriaosylceramide | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15939 | Th1653 | Agalsidase alfa | >Th1653_Agalsidase_alfa LDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL | 45351.6 | C2029H3080N544O587S27 | NA | NA | NA | The elimination half life was 108 ± 17 minutes for males and 89 ± 28 minutes for females.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A similar to [agalsidase beta]. While patients generally do not experience a clinically significant difference in outcomes between the two drugs, some patients may experience greater benefit with agalsidase beta.[A220228,A220233] Use of agalsidase beta has decreased in Europe, in favor of agalsidase alfa, after a contamination event in 2009.[A220343] Agalsidase alfa was granted EMA approval on 3 August 2001.[L16413] | Agalsidase alfa is indicated in the treatment of Fabry disease.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A used as enzyme replacement therapy in the treatment of Fabry disease.[L16398] It has a long duration of action and a wide therapeutic index.[L16398] Patients should be counselled regarding the risk of infusion related reactions and hypersensitivity.[L16398] | a-galactosidase A is uptaken by cells via the mannose 6 phosphate receptor.[A220323] Agalsidase alfa hydrolyzes globotriaosylceramide and other glycosphingolipids that would normally be hydrolyzed by endogenous a-galactosidase A.[L16398] Preventing the accumulation of glycosphingolipids prevents or reduces the severity of manifestations of Fabry disease such as renal failure, cardiomyopathy, or cerebrovascular events.[L16398] | Data regarding overdoses of agalsidase alfa are not readily available.[L16398] Patients experiencing an overdose of agalsidase alfa may experience an increased incidence and severity of adverse effects. Overdose can be managed through the use of symptomatic and supportive measures. | Data regarding the metabolism of agalsidase alfa is not readily available.[L16398] However, protein drugs are expected to be degraded by proteases and other catalytic enzymes to smaller peptides and amino acids.[A182009] | A dose of agalsidase alfa in non end stage renal disease patients reaches a Cmax of 3710 ± 855 U/mL with an AUC of 256,958 ± 63,499 min | The volume of distribution at steady state in non end stage renal disease patients was approximately 17% of body weight regardless of sex.[A220338,L16398] | The clearance for doses of 0.007-0.2 mg/kg were 2.66 mL/min/kg for males and 2.10 mL/min/kg for females.[L16398] | Enzymes | NA | NA | NA | NA | Globotriaosylceramide | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15940 | Th1653 | Agalsidase alfa | >Th1653_Agalsidase_alfa LDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL | 45351.6 | C2029H3080N544O587S27 | NA | NA | NA | The elimination half life was 108 ± 17 minutes for males and 89 ± 28 minutes for females.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A similar to [agalsidase beta]. While patients generally do not experience a clinically significant difference in outcomes between the two drugs, some patients may experience greater benefit with agalsidase beta.[A220228,A220233] Use of agalsidase beta has decreased in Europe, in favor of agalsidase alfa, after a contamination event in 2009.[A220343] Agalsidase alfa was granted EMA approval on 3 August 2001.[L16413] | Agalsidase alfa is indicated in the treatment of Fabry disease.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A used as enzyme replacement therapy in the treatment of Fabry disease.[L16398] It has a long duration of action and a wide therapeutic index.[L16398] Patients should be counselled regarding the risk of infusion related reactions and hypersensitivity.[L16398] | a-galactosidase A is uptaken by cells via the mannose 6 phosphate receptor.[A220323] Agalsidase alfa hydrolyzes globotriaosylceramide and other glycosphingolipids that would normally be hydrolyzed by endogenous a-galactosidase A.[L16398] Preventing the accumulation of glycosphingolipids prevents or reduces the severity of manifestations of Fabry disease such as renal failure, cardiomyopathy, or cerebrovascular events.[L16398] | Data regarding overdoses of agalsidase alfa are not readily available.[L16398] Patients experiencing an overdose of agalsidase alfa may experience an increased incidence and severity of adverse effects. Overdose can be managed through the use of symptomatic and supportive measures. | Data regarding the metabolism of agalsidase alfa is not readily available.[L16398] However, protein drugs are expected to be degraded by proteases and other catalytic enzymes to smaller peptides and amino acids.[A182009] | A dose of agalsidase alfa in non end stage renal disease patients reaches a Cmax of 3710 ± 855 U/mL with an AUC of 256,958 ± 63,499 min | The volume of distribution at steady state in non end stage renal disease patients was approximately 17% of body weight regardless of sex.[A220338,L16398] | The clearance for doses of 0.007-0.2 mg/kg were 2.66 mL/min/kg for males and 2.10 mL/min/kg for females.[L16398] | Enzymes and Coenzymes | NA | NA | NA | NA | Globotriaosylceramide | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15944 | Th1653 | Agalsidase alfa | >Th1653_Agalsidase_alfa LDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL | 45351.6 | C2029H3080N544O587S27 | NA | NA | NA | The elimination half life was 108 ± 17 minutes for males and 89 ± 28 minutes for females.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A similar to [agalsidase beta]. While patients generally do not experience a clinically significant difference in outcomes between the two drugs, some patients may experience greater benefit with agalsidase beta.[A220228,A220233] Use of agalsidase beta has decreased in Europe, in favor of agalsidase alfa, after a contamination event in 2009.[A220343] Agalsidase alfa was granted EMA approval on 3 August 2001.[L16413] | Agalsidase alfa is indicated in the treatment of Fabry disease.[L16398] | Agalsidase alfa is a recombinant human a-galactosidase A used as enzyme replacement therapy in the treatment of Fabry disease.[L16398] It has a long duration of action and a wide therapeutic index.[L16398] Patients should be counselled regarding the risk of infusion related reactions and hypersensitivity.[L16398] | a-galactosidase A is uptaken by cells via the mannose 6 phosphate receptor.[A220323] Agalsidase alfa hydrolyzes globotriaosylceramide and other glycosphingolipids that would normally be hydrolyzed by endogenous a-galactosidase A.[L16398] Preventing the accumulation of glycosphingolipids prevents or reduces the severity of manifestations of Fabry disease such as renal failure, cardiomyopathy, or cerebrovascular events.[L16398] | Data regarding overdoses of agalsidase alfa are not readily available.[L16398] Patients experiencing an overdose of agalsidase alfa may experience an increased incidence and severity of adverse effects. Overdose can be managed through the use of symptomatic and supportive measures. | Data regarding the metabolism of agalsidase alfa is not readily available.[L16398] However, protein drugs are expected to be degraded by proteases and other catalytic enzymes to smaller peptides and amino acids.[A182009] | A dose of agalsidase alfa in non end stage renal disease patients reaches a Cmax of 3710 ± 855 U/mL with an AUC of 256,958 ± 63,499 min | The volume of distribution at steady state in non end stage renal disease patients was approximately 17% of body weight regardless of sex.[A220338,L16398] | The clearance for doses of 0.007-0.2 mg/kg were 2.66 mL/min/kg for males and 2.10 mL/min/kg for females.[L16398] | Hydrolytic Lysosomal Neutral Glycosphingolipid-specific Enzyme | NA | NA | NA | NA | Globotriaosylceramide | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 16002 | Th1661 | Avalglucosidase alfa | >Th1661_Avalglucosidase_alfa QQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPRVHSRAPSPLYSVEFSEEPFGVIVHRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPIEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC | 124000 | C4490H6818N1197O1299S32 | NA | NA | NA | The mean avalglucosidase alfa-ngpt plasma elimination half-life was 1.6 hours in patients with late-onset Pompe disease.[L35155] | Avalglucosidase alfa, or NeoGAA, is a drug for enzyme replacement therapy specifically designed for Pompe disease, a rare inherited neuromuscular disorder caused by the deficiency of the alpha-glucosidase (GAA) enzyme. GAA is an essential enzyme that hydrolyzes glycogen into free glucose for use in cellular functions. In Pompe disease, the GAA enzyme is missing and patients are unable to properly break down glycogen, resulting in the accumulation of glycogen within lysosomes and progressive disruption of cellular function, especially in smooth, cardiac, and skeletal muscle cells. Pompe disease is characterized by progressive muscle weakness and loss of motor function, including respiratory muscle weakness, which leads to premature death and debilitating effects on people’s lives.[A232955] Avalglucosidase alfa is a recombinant form of GAA that restores deficient enzyme levels. First developed by Sanofi Genzyme, avalglucosidase alfa is a chemically modified version of [alglucosidase alfa], where synthetic bis-phosphorylated oligosaccharides were attached to the structure to improve cellular uptake of the drug and better muscle targeting.[A232960] On August 6, 2021, avalglucosidase alfa-ngpt was approved under the market name Nexviazyme to treat patients one year of age and older with late-onset Pompe disease.[L35160] Late-onset Pompe disease is associated with a range of debilitating physical symptoms, such as progressive muscle weakness, including respiratory muscle weakness, and loss of motor function.[A232955] In clinical trials, avalglucosidase alfa improved lung function in patients with Pompe disease.[L35160] Avalglucosidase alfa was approved by Health Canada on November 15, 2021 for the treatment of patients older than 6 months of age with late-onset Pompe disease.[L39205] | Avalglucosidase alfa is a hydrolytic lysosomal glycogen-specific enzyme indicated for the treatment of patients one year of age and older with late-onset Pompe disease (lysosomal acid alpha-glucosidase [GAA] deficiency).[L35155] It is approved for the same indication in Canada for pediatric patients six months and older.[L39357] | Avalglucosidase alfa is a recombinant alpha-glucosidase (GAA) enzyme that catalyzes hydrolysis of glycogen. In clinical trials, avalglucosidase alfa reduced the levels of glycogen excreted in the urine of patients with Pompe disease, indicating that it effectively cleaved excess glycogen.[L35155] Avalglucosidase alfa has significantly higher binding affinity for cation-independent mannose-6-phosphate receptor (CI-MPR) for cellular uptake and better muscle targeting than [alglucosidase alfa]. In GAA-deficient mice, avalglucosidase alfa reduced glycogen with more efficacy than alglucosidase alfa at an equivalent dose.[A232960] | Pompe disease is a genetic glycogen metabolism disorder that is also referred to as acid maltase deficiency or glycogen storage disease type II (GSD II). It is caused by mutations in the GAA gene, which encodes the lysosomal hydrolase acid a-glucosidase (GAA), an enzyme that normally catalyzes hydrolysis of glycogen to release free glucose for absorption and use for cellular functions. GAA deficiency leads to accumulation of glycogen within lysosomes and progressive disruption of cellular function, especially in smooth, cardiac, and skeletal muscle cells.[A232955] Enzyme replacement therapy using avalglucosidase alfa aims to restore the missing GAA enzyme. Avalglucosidase alfa is a hydrolytic lysosomal glycogen-specific recombinant human GAA enzyme that is conjugated with multiple synthetic bis-mannose-6-phosphate (bis-M6P) tetra-mannose glycans for enhanced targeting to skeletal muscles. The M6P of avalglucosidase alfa binds to cation-independent mannose-6-phosphate receptor (CI-MPR) on the cell surface with high affinity, which allows drug uptake into cells. Avalglucosidase alfa is internalized and transported into lysosomes to undergo proteolytic cleavage. It then exerts GAA enzymatic activity to cleave glycogen.[A232955, L35155] | There is limited information on the overdose profile and LD50 values of avalglucosidase alfa. | The metabolic pathway of avalglucosidase alfa-ngpt has not been characterized. The protein portion of avalglucosidase alfa-ngpt is expected to be metabolized into small peptides and amino acids via catabolic pathways.[L35155] | The avalglucosidase alfa-ngpt exposure increases in an approximately proportional manner with increasing doses over a range from 5 to 20 mg/kg. Following intravenous infusion of 20 mg/kg every two weeks in patients with late-onset Pompe disease, the mean ± SD plasma Cmax of avalglucosidase alfa-ngpt was 259 ± 72 µg/mL at week one and 242 ± 81 µg/mL at week 49. The mean ± SD plasma AUC of avalglucosidase alfa-ngpt was 1,290 ± 420 µg·h/mL at week one and 1,250 ± 433 µg·h/mL at week 49.[L35155] | The volume of distribution of avalglucosidase alfa-ngpt was 3.4 L in patients with late-onset Pompe disease. No accumulation was observed following every two weeks-dosing schedules.[L35155] | The mean avalglucosidase alfa-ngpt clearance was 0.9 L/hour in patients with late-onset Pompe disease.[L35155] | Enzyme Replacement Therapy | NA | NA | NA | NA | Cation-independent mannose-6-phosphate receptor | Nexviazyme | Sanofi Aventis | Sanofi Aventis | Intravenous | 100 mg / vial | None. | headache, fatigue, diarrhea, nausea, joint pain, dizziness, muscle aches, itching, vomiting, shortness of breath, skin redness, numbness and tingling, and hives. | Nexviazyme helps replace an enzyme that is missing in people with a genetic disorder called late-onset Pompe disease, (also called GAA deficiency) in children at least 1 year old. Nexviazyme may also be used for purposes not listed in this medication guide. Warnings Tell your caregivers or get emergency... | Nexviazyme is a prescription medicine used to treat the symptoms of Pompe Disease. Nexviazyme may be used alone or with other medications. | NA | Avalglucosidase alfa-ngpt is a hydrolytic lysosomal glycogen-specific recombinant human α-glucosidase enzyme conjugated with multiple synthetic bis-mannose-6-phosphate (bis-M6P)-tetra-mannose glycans resulting in approximately 15 moles of M6P per mole of enzyme (15 M6P) and is produced in Chinese hamster ovary cells (CHO). Avalglucosidase alfa-ngpt has a molecular weight of approximately 124 kDa. | Link | Link | NA |
| 16003 | Th1661 | Avalglucosidase alfa | >Th1661_Avalglucosidase_alfa QQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPRVHSRAPSPLYSVEFSEEPFGVIVHRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPIEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC | 124000 | C4490H6818N1197O1299S32 | NA | NA | NA | The mean avalglucosidase alfa-ngpt plasma elimination half-life was 1.6 hours in patients with late-onset Pompe disease.[L35155] | Avalglucosidase alfa, or NeoGAA, is a drug for enzyme replacement therapy specifically designed for Pompe disease, a rare inherited neuromuscular disorder caused by the deficiency of the alpha-glucosidase (GAA) enzyme. GAA is an essential enzyme that hydrolyzes glycogen into free glucose for use in cellular functions. In Pompe disease, the GAA enzyme is missing and patients are unable to properly break down glycogen, resulting in the accumulation of glycogen within lysosomes and progressive disruption of cellular function, especially in smooth, cardiac, and skeletal muscle cells. Pompe disease is characterized by progressive muscle weakness and loss of motor function, including respiratory muscle weakness, which leads to premature death and debilitating effects on people’s lives.[A232955] Avalglucosidase alfa is a recombinant form of GAA that restores deficient enzyme levels. First developed by Sanofi Genzyme, avalglucosidase alfa is a chemically modified version of [alglucosidase alfa], where synthetic bis-phosphorylated oligosaccharides were attached to the structure to improve cellular uptake of the drug and better muscle targeting.[A232960] On August 6, 2021, avalglucosidase alfa-ngpt was approved under the market name Nexviazyme to treat patients one year of age and older with late-onset Pompe disease.[L35160] Late-onset Pompe disease is associated with a range of debilitating physical symptoms, such as progressive muscle weakness, including respiratory muscle weakness, and loss of motor function.[A232955] In clinical trials, avalglucosidase alfa improved lung function in patients with Pompe disease.[L35160] Avalglucosidase alfa was approved by Health Canada on November 15, 2021 for the treatment of patients older than 6 months of age with late-onset Pompe disease.[L39205] | Avalglucosidase alfa is a hydrolytic lysosomal glycogen-specific enzyme indicated for the treatment of patients one year of age and older with late-onset Pompe disease (lysosomal acid alpha-glucosidase [GAA] deficiency).[L35155] It is approved for the same indication in Canada for pediatric patients six months and older.[L39357] | Avalglucosidase alfa is a recombinant alpha-glucosidase (GAA) enzyme that catalyzes hydrolysis of glycogen. In clinical trials, avalglucosidase alfa reduced the levels of glycogen excreted in the urine of patients with Pompe disease, indicating that it effectively cleaved excess glycogen.[L35155] Avalglucosidase alfa has significantly higher binding affinity for cation-independent mannose-6-phosphate receptor (CI-MPR) for cellular uptake and better muscle targeting than [alglucosidase alfa]. In GAA-deficient mice, avalglucosidase alfa reduced glycogen with more efficacy than alglucosidase alfa at an equivalent dose.[A232960] | Pompe disease is a genetic glycogen metabolism disorder that is also referred to as acid maltase deficiency or glycogen storage disease type II (GSD II). It is caused by mutations in the GAA gene, which encodes the lysosomal hydrolase acid a-glucosidase (GAA), an enzyme that normally catalyzes hydrolysis of glycogen to release free glucose for absorption and use for cellular functions. GAA deficiency leads to accumulation of glycogen within lysosomes and progressive disruption of cellular function, especially in smooth, cardiac, and skeletal muscle cells.[A232955] Enzyme replacement therapy using avalglucosidase alfa aims to restore the missing GAA enzyme. Avalglucosidase alfa is a hydrolytic lysosomal glycogen-specific recombinant human GAA enzyme that is conjugated with multiple synthetic bis-mannose-6-phosphate (bis-M6P) tetra-mannose glycans for enhanced targeting to skeletal muscles. The M6P of avalglucosidase alfa binds to cation-independent mannose-6-phosphate receptor (CI-MPR) on the cell surface with high affinity, which allows drug uptake into cells. Avalglucosidase alfa is internalized and transported into lysosomes to undergo proteolytic cleavage. It then exerts GAA enzymatic activity to cleave glycogen.[A232955, L35155] | There is limited information on the overdose profile and LD50 values of avalglucosidase alfa. | The metabolic pathway of avalglucosidase alfa-ngpt has not been characterized. The protein portion of avalglucosidase alfa-ngpt is expected to be metabolized into small peptides and amino acids via catabolic pathways.[L35155] | The avalglucosidase alfa-ngpt exposure increases in an approximately proportional manner with increasing doses over a range from 5 to 20 mg/kg. Following intravenous infusion of 20 mg/kg every two weeks in patients with late-onset Pompe disease, the mean ± SD plasma Cmax of avalglucosidase alfa-ngpt was 259 ± 72 µg/mL at week one and 242 ± 81 µg/mL at week 49. The mean ± SD plasma AUC of avalglucosidase alfa-ngpt was 1,290 ± 420 µg·h/mL at week one and 1,250 ± 433 µg·h/mL at week 49.[L35155] | The volume of distribution of avalglucosidase alfa-ngpt was 3.4 L in patients with late-onset Pompe disease. No accumulation was observed following every two weeks-dosing schedules.[L35155] | The mean avalglucosidase alfa-ngpt clearance was 0.9 L/hour in patients with late-onset Pompe disease.[L35155] | Hydrolytic Lysosomal Glycogen-specific Enzyme | NA | NA | NA | NA | Cation-independent mannose-6-phosphate receptor | Nexviazyme ngpt | Genzyme Corporation | Genzyme Corporation | Intravenous | 100 mg/10mL | NA | Back pain bluish lips or skin blurred vision chest discomfort or tightness chills confusion cough diarrhea difficulty swallowing dizziness, faintness, or lightheadedness when getting up suddenly from a lying or sitting position fast, pounding, or irregular heartbeat or pulse feeling of warmth fever general feeling of discomfort or illness headache hives, itching, skin rash joint pain loss of appetite muscle aches and pains nausea nervousness pounding in the ears puffiness or swelling of the eyelids or around the eyes, face, lips, or tongue redness of the face, neck, arms, and occasionally, upper chest runny nose shakiness in the legs, arms, hands, or feet shivering slow or fast heartbeat sore throat sweating trembling or shaking of the hands or feet trouble breathing trouble sleeping unusual tiredness or weakness vomiting | NA | NA | NA | NA | Link | Link | NA |
| 16102 | Th1678 | Tyrosinase | >Th1678_Tyrosinase MESTTVLLAASTLLLVLHASYGQFPRACSTAQVLLSKECCPVWPGDNSSCGEVSGRGVCQDVVPSNSPVGAQFPFSGIDDRENWPIVFYNRTCQCQGNFMGYNCGECRFGYTGPNCTVRRNMIRKEIFRMTTAEKDKFIAYLNLAKRTISQDYVISTGTYEQMNNGSNPMFADINVYDLFVWLHYYASRDAFLEDGSVWANIDFAHEAPGFPPWHRFFLLLWEREIQKVAADDNFTIPFWDWRDAQQCDLCTDEFFGGTHPTSNNLLSPASFFSSWQVICSQPEEYNRLRIICNGTNEGPLLRSPGRHDRNRTPRLPTSADVEACLSLTDYETGAMDRFANFSFRNTLEGYAVPASGIANRSQSNMHNSLHVFMNGSMSNVQGSANDPIFVLHHAFVDSLFEQWLRRHQPSLDVYPEANAPVGHNREYNMVPFIPLFTNGEFFVQSRDLGYDYDYLAESGSIEDFLLPYLEQARQIWQWLLGAAVVGGLVTAVIATIISLTCRRKRRTKTSEETRPLLMEAEDYHATYQSNL | NA | NA | NA | NA | NA | NA | Tyrosinase is a multi-copper-containing multifunctional metalloenzyme with 4 possible oxidation states.[A231829, A231834, A231839] It is responsible for producing melanin pigment across the phylogenetic spectrum.[A231829, A231834, A231839] Within mammals, tyrosinase is found specifically in melanocytes in a glycosylated form and plays a critical role in regulating the process of melanin biosynthesis (also known as melanogenesis).[A231829, A231839] It is recognized as being the main enzyme responsible for enzymatic browning and melanogenesis in mammals, thus causing undesired browning of fruits and vegetables and diseases resulting from melanin overproduction.[A231829] | NA | NA | During melanogenesis, tyrosinase acts as a rate-limiting enzyme.[A231829] | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 16103 | Th1678 | Tyrosinase | >Th1678_Tyrosinase MESTTVLLAASTLLLVLHASYGQFPRACSTAQVLLSKECCPVWPGDNSSCGEVSGRGVCQDVVPSNSPVGAQFPFSGIDDRENWPIVFYNRTCQCQGNFMGYNCGECRFGYTGPNCTVRRNMIRKEIFRMTTAEKDKFIAYLNLAKRTISQDYVISTGTYEQMNNGSNPMFADINVYDLFVWLHYYASRDAFLEDGSVWANIDFAHEAPGFPPWHRFFLLLWEREIQKVAADDNFTIPFWDWRDAQQCDLCTDEFFGGTHPTSNNLLSPASFFSSWQVICSQPEEYNRLRIICNGTNEGPLLRSPGRHDRNRTPRLPTSADVEACLSLTDYETGAMDRFANFSFRNTLEGYAVPASGIANRSQSNMHNSLHVFMNGSMSNVQGSANDPIFVLHHAFVDSLFEQWLRRHQPSLDVYPEANAPVGHNREYNMVPFIPLFTNGEFFVQSRDLGYDYDYLAESGSIEDFLLPYLEQARQIWQWLLGAAVVGGLVTAVIATIISLTCRRKRRTKTSEETRPLLMEAEDYHATYQSNL | NA | NA | NA | NA | NA | NA | Tyrosinase is a multi-copper-containing multifunctional metalloenzyme with 4 possible oxidation states.[A231829, A231834, A231839] It is responsible for producing melanin pigment across the phylogenetic spectrum.[A231829, A231834, A231839] Within mammals, tyrosinase is found specifically in melanocytes in a glycosylated form and plays a critical role in regulating the process of melanin biosynthesis (also known as melanogenesis).[A231829, A231839] It is recognized as being the main enzyme responsible for enzymatic browning and melanogenesis in mammals, thus causing undesired browning of fruits and vegetables and diseases resulting from melanin overproduction.[A231829] | NA | NA | During melanogenesis, tyrosinase acts as a rate-limiting enzyme.[A231829] | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 16160 | Th1685 | Plasminogen | >Th1685_Plasminogen MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN | NA | NA | NA | NA | NA | The mean half-life of Ryplazim at steady-state is approximately 39.2 hours.[L34620] | Plasminogen is a pro-enzyme (i.e. a zymogen) which is cleaved to form plasmin - also known as [fibrinolysin] - as part of the fibrinolytic pathway that breaks down fibrin blood clots.[A236035] This pathway is activated when a clot is no longer needed or to prevent a clot from extending beyond the site of injury.[L34635] In June 2021, the FDA approved a plasma-derived plasminogen (Ryplazim, human plasminogen-tvmh)[L34620] for the treatment of type 1 plasminogen deficiency (hypoplasminogenemia).[L34615] It is the first and only FDA-approved treatment for this condition, which causes wood-like lesions to form on the mucous membranes of patients, providing an unmet medical need for patients with this rare congenital disease. | Plasma-derived human plasminogen, marketed under the brand name Ryplazim, is indicated for the treatment of patients with plasminogen deficiency type 1 (hypoplasminogenemia).[L34620] | The intravenous administration of plasminogen temporarily increases levels of plasminogen in the blood, allowing for the reduction or resolution of the lignous lesions associated with plasminogen deficiency.[L34620] Therapy is administered periodically, every 2 to 4 days, to prevent any significant build-up of these lesions between doses. Plasminogen administration can lead to tissue sloughing at mucosal sites where lignous lesions have built up, which may lead to organ or airway obstruction depending on the site of the lesion(s). Patients should be monitored for at least 4 hours post-administration, especially patients with evidence of airway involvement, to ensure airway management and respiratory support is readily available.[L34620] | Plasminogen is a zymogen produced in the liver which, when cleaved into its active form, breaks down fibrin blood clots.[A236035] This active form, called plasmin or fibrinolysin, is generated when tissue plasminogen activator (tPA) or urokinase-like plasminogen activator (uPA) cleave plasminogen to begin the fibrinolytic pathway.[L34635] Blood clots are broken down by plasmin into soluble fibrin and fibrinogen degradation products when the clot is no longer needed.[L34635] Type 1 plasminogen deficiency, also called hypoplasminogenemia, is a congenital disorder in which patients are deficient in plasminogen. Interestingly, this disease does not increase the risk of clotting, but rather results in the formation of lignous pseudomembranous lesions on the mucous membranes of the body.[L34625] Lesions range in location and severity but can lead to severe long-term consequences if left untreated. For example, lignous conjunctivitis, the most common manifestation of type 1 plasminogen deficiency, may lead to corneal tearing and blindness.[A236040] Human plasminogen is administered topically (e.g. in eye drops) or intravenously (i.e. [Ryplazim](https://www.fda.gov/media/149806/download)) in order to temporarily increase local or serum levels of fibrinogen. When this therapy is administered every 2 to 4 days, it prevents the build-up of lignous lesions and allows existing lesions to be shed. | There are no data regarding overdose of intravenously administered human plasminogen. | Plasminogen is a zymogen which is converted into the active fibrinolytic plasmin, or fibrinolysin, by tissue plasminogen activator (tPA) or urokinase-like plasminogen activator (uPA).[L34635,A236035] | Following 12 weeks of intravenous administration every 2 to 4 days, the mean AUCinf of Ryplazim was 5731.8 hr*% and its Cmax was approximately 125% of the mean physiological level (normal: 70-130%).[L34620] After 12 weeks of therapy, physiological plasminogen levels were sustained for approximately 24 hours post-dose and patients maintained a 10% absolute increase in plasminogen concentration for up to 96 hours after administration.[L34620] | The mean steady-state volume of distribution of Ryplazim is approximately 49.3 mL/kg.[L34620] | The clearance of Ryplazim appears to slow with extended use. Following the first intravenous dose the mean clearance of Ryplazim was 1.4 mL/hr/kg, while following an intravenous dose at week 12 the mean clearance was 0.9 mL/hr/kg.[L34620] | Enzyme Precursors | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 16161 | Th1685 | Plasminogen | >Th1685_Plasminogen MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN | NA | NA | NA | NA | NA | The mean half-life of Ryplazim at steady-state is approximately 39.2 hours.[L34620] | Plasminogen is a pro-enzyme (i.e. a zymogen) which is cleaved to form plasmin - also known as [fibrinolysin] - as part of the fibrinolytic pathway that breaks down fibrin blood clots.[A236035] This pathway is activated when a clot is no longer needed or to prevent a clot from extending beyond the site of injury.[L34635] In June 2021, the FDA approved a plasma-derived plasminogen (Ryplazim, human plasminogen-tvmh)[L34620] for the treatment of type 1 plasminogen deficiency (hypoplasminogenemia).[L34615] It is the first and only FDA-approved treatment for this condition, which causes wood-like lesions to form on the mucous membranes of patients, providing an unmet medical need for patients with this rare congenital disease. | Plasma-derived human plasminogen, marketed under the brand name Ryplazim, is indicated for the treatment of patients with plasminogen deficiency type 1 (hypoplasminogenemia).[L34620] | The intravenous administration of plasminogen temporarily increases levels of plasminogen in the blood, allowing for the reduction or resolution of the lignous lesions associated with plasminogen deficiency.[L34620] Therapy is administered periodically, every 2 to 4 days, to prevent any significant build-up of these lesions between doses. Plasminogen administration can lead to tissue sloughing at mucosal sites where lignous lesions have built up, which may lead to organ or airway obstruction depending on the site of the lesion(s). Patients should be monitored for at least 4 hours post-administration, especially patients with evidence of airway involvement, to ensure airway management and respiratory support is readily available.[L34620] | Plasminogen is a zymogen produced in the liver which, when cleaved into its active form, breaks down fibrin blood clots.[A236035] This active form, called plasmin or fibrinolysin, is generated when tissue plasminogen activator (tPA) or urokinase-like plasminogen activator (uPA) cleave plasminogen to begin the fibrinolytic pathway.[L34635] Blood clots are broken down by plasmin into soluble fibrin and fibrinogen degradation products when the clot is no longer needed.[L34635] Type 1 plasminogen deficiency, also called hypoplasminogenemia, is a congenital disorder in which patients are deficient in plasminogen. Interestingly, this disease does not increase the risk of clotting, but rather results in the formation of lignous pseudomembranous lesions on the mucous membranes of the body.[L34625] Lesions range in location and severity but can lead to severe long-term consequences if left untreated. For example, lignous conjunctivitis, the most common manifestation of type 1 plasminogen deficiency, may lead to corneal tearing and blindness.[A236040] Human plasminogen is administered topically (e.g. in eye drops) or intravenously (i.e. [Ryplazim](https://www.fda.gov/media/149806/download)) in order to temporarily increase local or serum levels of fibrinogen. When this therapy is administered every 2 to 4 days, it prevents the build-up of lignous lesions and allows existing lesions to be shed. | There are no data regarding overdose of intravenously administered human plasminogen. | Plasminogen is a zymogen which is converted into the active fibrinolytic plasmin, or fibrinolysin, by tissue plasminogen activator (tPA) or urokinase-like plasminogen activator (uPA).[L34635,A236035] | Following 12 weeks of intravenous administration every 2 to 4 days, the mean AUCinf of Ryplazim was 5731.8 hr*% and its Cmax was approximately 125% of the mean physiological level (normal: 70-130%).[L34620] After 12 weeks of therapy, physiological plasminogen levels were sustained for approximately 24 hours post-dose and patients maintained a 10% absolute increase in plasminogen concentration for up to 96 hours after administration.[L34620] | The mean steady-state volume of distribution of Ryplazim is approximately 49.3 mL/kg.[L34620] | The clearance of Ryplazim appears to slow with extended use. Following the first intravenous dose the mean clearance of Ryplazim was 1.4 mL/hr/kg, while following an intravenous dose at week 12 the mean clearance was 0.9 mL/hr/kg.[L34620] | Enzymes and Coenzymes | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |