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Th1047 details
Primary information
ID10331
Therapeutic IDTh1047
Protein NameAlpha-1-proteinase inhibitor
Sequence>Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting point59
Half-lifeNA
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-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.
ToxicityNA
MetabolismNA
AbsorptionNA
5632 ± 2006 mL [ARALAST NP]
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesAcute-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
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNeutrophil elastase
Brand NameAralast
CompanyBaxter
Brand DescriptionBaxter
Prescribed ForIts 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
Chemical NameNA
FormulationARALAST NP is available as a lyophilized powder in single dose vials containing 0.5 gram or 1 gram of functional Alpha 1 -Protenase inhibitor
Physical Appearance Lyophilized powder
Route of AdministrationIntravenous infusion
Recommended DosageRecommended dose is 60 mg/kg of body weight, administered once in a week.
ContraindicationARALAST NP is contraindicated in immunoglobulin A deficient patients with antibodies against IgA, due to the risk of severe hypersensitivity.
Side EffectsFever, 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.
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID10332
Therapeutic IDTh1047
Protein NameAlpha-1-proteinase inhibitor
Sequence>Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting point59
Half-lifeNA
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-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.
ToxicityNA
MetabolismNA
AbsorptionNA
5618 ± 1618 mL [Aralast]
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesAcute-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
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameGlassia
CompanyTakeda, Baxalta US Inc.
Brand DescriptionTakeda, Baxalta US Inc.
Prescribed Fortreat the symptoms of Alpha-1 Antitrypsin Deficiency.
Chemical NameNA
FormulationGLASSIA 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.
Physical Appearance sterile, ready to use, liquid preparation of purified human alpha1 -proteinase inhibitor
Route of Administrationintravenous
Recommended DosageAdminister 60 mg/kg body weight of GLASSIA once weekly by intravenous infusion.
ContraindicationGLASSIA 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.
Side Effectshives, 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
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID10333
Therapeutic IDTh1047
Protein NameAlpha-1-proteinase inhibitor
Sequence>Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting point59
Half-lifeNA
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-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.
ToxicityNA
MetabolismNA
AbsorptionNA
NA
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesAcute-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
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameRespreeza
CompanyCsl Behring
Brand DescriptionCsl Behring
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID10334
Therapeutic IDTh1047
Protein NameAlpha-1-proteinase inhibitor
Sequence>Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting point59
Half-lifeNA
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-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.
ToxicityNA
MetabolismNA
AbsorptionNA
NA
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesAcute-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
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameProlastin
CompanyTalecris Biotherapeutics C formerly Bayer
Brand DescriptionTalecris Biotherapeutics C formerly Bayer
Prescribed ForIt is used to treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema.
Chemical NameNA
FormulationThe 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,
Physical Appearance Lyophilized powder
Route of AdministrationIntravenous infusion
Recommended DosageProlastin (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.
ContraindicationIndividuals 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.
Side EffectsFever, 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.
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID10335
Therapeutic IDTh1047
Protein NameAlpha-1-proteinase inhibitor
Sequence>Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting point59
Half-lifeNA
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-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.
ToxicityNA
MetabolismNA
AbsorptionNA
NA
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesAcute-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
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameZemaira
CompanyCsl Behring
Brand DescriptionCsl Behring
Prescribed Forto treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema.
Chemical NameNA
FormulationZemaira 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.
Physical Appearance sterile, white, lyophilized preparation of purified Alpha1-Proteinase Inhibitor
Route of Administrationintravenous
Recommended DosageThe recommended dose of ZEMAIRA is 60 mg/kg body weight administered once weekly.
ContraindicationZEMAIRA 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
Side EffectsNausea, 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.
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID10336
Therapeutic IDTh1047
Protein NameAlpha-1-proteinase inhibitor
Sequence>Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting point59
Half-lifeNA
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-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.
ToxicityNA
MetabolismNA
AbsorptionNA
NA
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesAcute-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
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameNA
CompanyNA
Brand DescriptionNA
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA