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.
Tabular representation:
| 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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 10577 | Th1118 | Sulodexide | NA | 5000-8000 | NA | NA | NA | NA | elimination half-life was 11.7 ± 2.0 h by IV route | A mixture of glycosaminoglycans (GAGs), composed of dermatan sulfate (DS) and fast moving heparin (FMH). | For the treatment of thrombosis. Also investigated for use/treatment in diabetic kidney disease, and neuropathy (diabetic). | The low molecular weight of both sulodexide fractions allows for extensive oral absorption compared to unfractionated heparin. The pharmacological effects of sulodexide differ substantially from other glycosaminoglycans and are mainly characterized by a prolonged half-life and reduced effect on global coagulation and bleeding parameters. Due to the presence of both glycosaminoglycan fractions, sulodexide potentiates the antiprotease activities of both antithrombin III and heparin cofactor II simultaneously. | Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, heparin cofactor II (HCII) catalysis by dermatan sulfate and antithrombin-III catalysis by fast moving heparin (FMH). | Sulodexide seems to be well tolerated. Most adverse effects reported are related to the GI system and seem to be transient in nature. Among others adverse reactions are diarrhea, epigastralgia, dyspepsia, heartburn and dizziness. Allergic reactions, such as skin rash, have also been reported but are very rare. | It is mainly metabolized in the liver. | Sulodexide can be administered via the oral route, IV and IM routes. After oral dosing, the absorption rate being equivalent, the bioavailability is 40-60%. either calculated from the fast-moving heparin fraction or from the dermatan fraction. Bioavailability following IM administration is approximately 90%. After a rapid absorption in the intestine, the dermatan and heparin components start to appear in the plasma. Sulodexide is degraded after ingestion and loses its sulfate groups and both sulfated and unsulfated groups circulate in the blood for up to 24hours. AUC=22.83+/-4.44mg.h/L. | Cmax=516+/-77.54ng/mL, Tmax=1.33+/-0.58h, Vd=71.24+/-14.06L (b phase). Sulodexide reaches high concentrations in the plasma and is widely distributed in the endothelial layer. Binding to endothelial cell receptors in arteries and veins contributes to its rapid distribution profile. | 2.70+/-0.58L/h | Antithrombins and Fibrinolytic Agents and Hypoglycemic Agents and Anticoagulants and Hypolipidemic Agents | NA | NA | NA | NA | Heparin cofactor 2,Antithrombin-III | SULODEXIDE | Syntex S.A | Syntex S.A | Antithrombotic and antithrombin activity is of great pharmacologic interest and makes sulodexide a suitable drug for the prophylaxis and treatment of arterial and venous peripheral diseases | NA | NA | NA | NA | NA | NA | NA | 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 |
| 11856 | 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 | Fibrinolytic Agents | NA | NA | NA | NA | Plasminogen | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12067 | 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 | Fibrinolysin, antagonists & inhibitors | 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 |
| 12068 | 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 | Fibrinolytic Agents | 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 |
| 13063 | Th1378 | Fibrinogen human | >Th1378_Fibrinogen_human MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ | NA | NA | NA | NA | NA | 78.7 hours | Fibrinogen concentrate (human) is a hematological agent. It works by replacing a certain protein in the blood that helps with blood clotting. Fibrinogen (factor I) is a soluble plasma glycoprotein with a molecular weight of about 340 kDa. It is a physiological substrate for three enzymes: plasmin, factor XIIIa and thrombin. It is indicated for the treatment of acute bleeding episodes in patients with congenital fibrinogen deficiency, including afibrinogenemia and hypofibrinogenemia. | For the treatment of acute bleeding episodes in patients with congenital fibrinogen deficiency, including afibrinogenemia and hypofibrinogenemia. | Fibrinogen replaces the missing, or low coagulation factor. | Fibrinogen (factor I) is a soluble plasma glycoprotein with a molecular weight of about 340 kDa. The native molecule is a dimer and consists of three pairs of polypeptide chains (Aa, Bß and | NA | NA | Cmax is 140 mg/dL | Mean volume of distribution is 52.7 mL/kg. | 0.59 mL/h/kg | Fibrinogen | NA | NA | NA | NA | NA | Evicel | Omrix Biopharmaceuticals Ltd | Omrix Biopharmaceuticals Ltd | Topical | NA | Do not use EVICEL®Directly into the circulatory system. Intravascular application of EVICEL® may result in life-threatening thromboembolic events [see WARNINGS AND PRECAUTIONS and ADVERSE REACTIONS].In individuals known to have anaphylactic or severe systemic reaction to human blood products [see ADVERSE REACTIONS].For brisk arterial bleeding.For spraying in endoscopic or laparoscopic procedures in those instances where the minimum recommended distance from the applicator tip to the target site cannot be ensured. [see DOSAGE AND ADMINISTRATION]. | slow heart rate, nausea, low blood potassium, insomnia, low blood pressure (hypotension), fever, graft infection, vascular graft occlusion, swelling of extremities, and constipation | EVICEL® is manufactured from pooled human plasma. EVICEL® is provided as a single use kit consisting of two packages: One package contains one vial of Biological Active Component 2 (BAC2) and one vial of Thrombin. The second package contains a sterile spray application device. | Evicel is a prescription medicine used as a Wound Sealant to control bleeding during surgery. Evicel may be used alone or with other medications. | NA | EVICEL® is manufactured from pooled human plasma. EVICEL® is provided as a single use kit consisting of two packages: One package contains one vial of Biological Active Component 2 (BAC2) and one vial of Thrombin. The second package contains a sterile spray application device. The two components (BAC2 and Thrombin) should be mixed and applied topically as described in the Dosage and Administration Section (2). | Link | Link | NA |
| 13302 | 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 | Fibrinolytic Agents | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 13957 | 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 | Antifibrinolytic Agents | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 14678 | 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 | Fibrinolytic Agents | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 16163 | 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] | Fibrinolytic Agents | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |