Detailed description page of ThPDB2
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Th1012 details |
| Primary information | |
|---|---|
| ID | 10067 |
| Therapeutic ID | Th1012 |
| Protein Name | Reteplase |
| Sequence | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP |
| Molecular Weight | 39589.6 |
| Chemical Formula | C1736H2671N499O522S22 |
| Isoelectric Point | 6.86 |
| Hydrophobicity | -0.435 |
| Melting point | 60 |
| Half-life | NA |
| Description | 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). |
| Indication/Disease | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. |
| Pharmacodynamics | 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. |
| Mechanism of Action | 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. |
| Toxicity | NA |
| Metabolism | NA |
| Absorption | NA |
| NA | |
| Clearance | NA |
| Categories | 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 |
| Patents Number | CA2107476 |
| Date of Issue | 18-Dec-2007 |
| Date of Expiry | 15-Apr-2012 |
| Drug Interaction | Additive anticoagulant/antiplatelet effects may increase bleed risk. Concomitant therapy should be avoided with Ginkgo biloba |
| Target | Plasminogen,Fibrinogen alpha chain,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1 |
| Brand Name | Retavase |
| Company | Centocor |
| Brand Description | Centocor |
| Prescribed For | Improves heart function and reduces long-term effects of a heart attack. |
| Chemical Name | NA |
| Formulation | 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 |
| Physical Appearance | Sterile, white, lyophilized powder |
| Route of Administration | Intravenous Injection |
| Recommended Dosage | 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. |
| Contraindication | Allergic, or you have an aneurysm, heart or blood vessel defects, bleeding disorders |
| Side Effects | Rash; hives; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue. |
| Useful Link 1 | Link |
| Useful Link 2 | NA |
| Remarks | NA |
| Primary information | |
|---|---|
| ID | 10068 |
| Therapeutic ID | Th1012 |
| Protein Name | Reteplase |
| Sequence | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP |
| Molecular Weight | 39589.6 |
| Chemical Formula | C1736H2671N499O522S22 |
| Isoelectric Point | 6.86 |
| Hydrophobicity | -0.435 |
| Melting point | 60 |
| Half-life | NA |
| Description | 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). |
| Indication/Disease | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. |
| Pharmacodynamics | 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. |
| Mechanism of Action | 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 |
| Toxicity | NA |
| Metabolism | NA |
| Absorption | NA |
| NA | |
| Clearance | NA |
| Categories | 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 |
| Patents Number | NA |
| Date of Issue | NA |
| Date of Expiry | NA |
| Drug Interaction | Increased bleeding risk. Monitor for signs of bleeding when given in combination with Ticlopidine |
| Target | NA |
| Brand Name | NA |
| Company | KR Therapeutics Inc. |
| Brand Description | KR Therapeutics Inc. |
| Prescribed For | NA |
| Chemical Name | NA |
| Formulation | NA |
| Physical Appearance | NA |
| Route of Administration | NA |
| Recommended Dosage | NA |
| Contraindication | Severe uncontrolled high blood pressure |
| Side Effects | Black, tarry stools; bleeding at the injection site |
| Useful Link 1 | Link |
| Useful Link 2 | NA |
| Remarks | NA |
| Primary information | |
|---|---|
| ID | 10069 |
| Therapeutic ID | Th1012 |
| Protein Name | Reteplase |
| Sequence | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP |
| Molecular Weight | 39589.6 |
| Chemical Formula | C1736H2671N499O522S22 |
| Isoelectric Point | 6.86 |
| Hydrophobicity | -0.435 |
| Melting point | 60 |
| Half-life | NA |
| Description | 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). |
| Indication/Disease | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. |
| Pharmacodynamics | 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. |
| Mechanism of Action | 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 |
| Toxicity | NA |
| Metabolism | NA |
| Absorption | NA |
| NA | |
| Clearance | NA |
| Categories | 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 |
| Patents Number | NA |
| Date of Issue | NA |
| Date of Expiry | NA |
| Drug Interaction | NA |
| Target | NA |
| Brand Name | NA |
| Company | Hospira Inc. |
| Brand Description | Hospira Inc. |
| Prescribed For | NA |
| Chemical Name | NA |
| Formulation | NA |
| Physical Appearance | NA |
| Route of Administration | NA |
| Recommended Dosage | NA |
| Contraindication | If you have had brain or spinal surgery; or you have suffered recent trauma |
| Side Effects | Vomiting blood or material that looks like coffee grounds |
| Useful Link 1 | Link |
| Useful Link 2 | NA |
| Remarks | NA |
| Primary information | |
|---|---|
| ID | 10070 |
| Therapeutic ID | Th1012 |
| Protein Name | Reteplase |
| Sequence | >Th1012_Reteplase SYQGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP |
| Molecular Weight | 39589.6 |
| Chemical Formula | C1736H2671N499O522S22 |
| Isoelectric Point | 6.86 |
| Hydrophobicity | -0.435 |
| Melting point | 60 |
| Half-life | NA |
| Description | 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). |
| Indication/Disease | For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction. |
| Pharmacodynamics | 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. |
| Mechanism of Action | 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 |
| Toxicity | NA |
| Metabolism | NA |
| Absorption | NA |
| NA | |
| Clearance | NA |
| Categories | 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 |
| Patents Number | NA |
| Date of Issue | NA |
| Date of Expiry | NA |
| Drug Interaction | NA |
| Target | NA |
| Brand Name | NA |
| Company | PDL BioPharma Inc. |
| Brand Description | PDL BioPharma Inc. |
| Prescribed For | NA |
| Chemical Name | NA |
| Formulation | NA |
| Physical Appearance | NA |
| Route of Administration | NA |
| Recommended Dosage | NA |
| Contraindication | A history of stroke, or internal bleeding |
| Side Effects | Chest pain; severe bleeding; sudden, severe headache; trouble breathing |
| Useful Link 1 | NA |
| Useful Link 2 | NA |
| Remarks | NA |