Browse result page of ThPDB2
This is the result page of the browse module of ThPDB2. This page gives the information about the query submitted by the user as per the browse category. Further details of the entries can be seen by clicking on the ID or THPP_ID. Further the user can sort the entries on the basis of various fields by clicking on the respective headers. The user can also download the results in various formats.
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| ID | THPP_ID | Therapeutic Name | Sequence | Molecular Weight | Chemical Formula | Isoelectric Point | Hydrophobicity | Melting Point | Half Life | Description | Disease/Indication | Pharmacodynamics | Mechanism of Action | Toxicity | Metabolism | Absorption | Volume of Distribution | Clearance | Categories | Patent Number | Date of Issue | Date of Expiry | Drug Interaction | Target | Brand Name | Company | Brand Description | Prescribed for | Chemical Name | Formulation | Physical Appearance | Route of Administation | Recommended Dosage | Contraindication | Side Effects | Useful Links 1 | Useful Links 2 | Remarks |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 10234 | Th1032 | Coagulation factor VIIa | >Th1032_Coagulation_factor_VIIa ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 | NA | Recombinant human coagulation Factor VIIa is intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues, cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | To treat bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | 121 ± 30 mL/kg [adults] | 33 - 37 mL/h x kg [healthy] | Amino Acids, Peptides, and Proteins, Biological Factors, Blood and Blood Forming Organs, Blood Coagulation Factors, Blood Proteins, Endopeptidases, Enzymes, Enzymes and Coenzymes, Factor VII, Factor VIIa, antagonists & inhibitors, Hemostatics, Hydrolases, Increased Coagulation Factor IX Activity, Increased Coagulation Factor X Activity, Peptide Hydrolases, Proteins, Serine Endopeptidases, Serine Proteases | NA | NA | NA | Autoplex T (anti-inhibitor coagulant complex) | Coagulation factor X,Serine protease hepsin,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NovoSeven | Novo Nordisk | Novo Nordisk | For treatment and prevention of bleeding in surgeries and procedures in adults and children with hemophilia A or B with inhibitors, congenital Factor VII (FVII) deficiency, and people with Glanzmann’s thrombasthenia who have a decreased or absent response | NA | Each vial contains approximately 0. 6 mg/mL NovoSeven (coagulation factor viia recombinant) (corresponding to 600 _g/mL). The reconstituted vials have a pH of approximately 5. 5 in sodium chloride (3 mg/mL), calcium chloride dihydrate (1. 5 mg/mL), glycyl | Sterile, white lyophilized powder | Injection | For bleeding episodes, the recommended dose of NovoSeven (coagulation factor viia (recombinant)) for hemophilia A or B patients with inhibitors is 90 _g/kg given every two hours by bolus infusion until hemostasis is achieved, or until thehemostasis has been acheived. | Hypersensitivity | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; bleeding at the injection site; bloody stools; calf or stomach pain, tenderness, or swelling; chest pain; confusion; dizziness; fainting; numbness. | Link | NA | NA |
| 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 |
| 10742 | Th1171 | C1 Esterase Inhibitor (Human) | NA | 68000 | NA | NA | NA | NA | Following intravenous administration of a single dose, the half-life was 56 ± 36 hours.3 Subcutaneous administration produces a half-life of 199.6 hours | Recombinant human C1 esterase inhibitor is a human protein developed through Pharming’s proprietary technology where the human protein is expressed in milk of transgenic rabbits. Hereditary Angioedema (HAE) is a human genetic disorder caused by a shortage of C1 inhibitor activity and results in an overreaction of the immune system. The disease is characterized by acute attacks of painful and in some cases fatal swelling of several soft tissues (edema), which may last up to five days when untreated. | For routine prophylaxis against angioedema attacks in adolescent and adult patients with Hereditary Angioedema (HAE). | In clinical studies, intravenous administration demonstrated an increase in plasma levels of C1 inhibitor within approximately one hour or less of administration. | C1 inhibitor is a normal constituent of human blood and is one of the serine proteinase inhibitors (serpins). The primary function of C1 inhibitor is to regulate the activation of the complement and intrinsic coagulation (contact system) pathway. C1 inhibitor also regulates the fibrinolytic system. Regulation of these systems is performed through the formation of complexes between the proteinases and the inhibitor, resulting in inactivation of both and consumption of the C1 inhibitor. HAE patients have low levels of endogenous or functional C1 inhibitor. Although the events that induce attacks of angioedema in HAE patients are not well defined, it is thought by some that increased vascular permeability and the clinical manifestation of HAE attacks are primarily mediated through contact system activation. Suppression of contact system activation by C1 inhibitor through the inactivation of plasma kallikrein and factor XIIa is thought to modulate this vascular permeability by preventing the generation of bradykinin1. Administration of C1 Esterase Inhibitor increases plasma levels of C1 inhibitor activity. | NA | NA | NA | NA | NA | NA | NA | NA | NA | Cyproterone acetate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Danazol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Desogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Dienogest may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Drospirenone may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estropipate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethinyl Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethynodiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Etonogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human). | Plasma protease C1 inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA |
| 10743 | Th1171 | C1 Esterase Inhibitor (Human) | NA | 68000 | NA | NA | NA | NA | Following intravenous administration of a single dose, the half-life was 56 ± 36 hours.3 Subcutaneous administration produces a half-life of 199.6 hours | Recombinant human C1 esterase inhibitor is a human protein developed through Pharming’s proprietary technology where the human protein is expressed in milk of transgenic rabbits. Hereditary Angioedema (HAE) is a human genetic disorder caused by a shortage of C1 inhibitor activity and results in an overreaction of the immune system. The disease is characterized by acute attacks of painful and in some cases fatal swelling of several soft tissues (edema), which may last up to five days when untreated. | For routine prophylaxis against angioedema attacks in adolescent and adult patients with Hereditary Angioedema (HAE). | In clinical studies, intravenous administration demonstrated an increase in plasma levels of C1 inhibitor within approximately one hour or less of administration. | C1 inhibitor is a normal constituent of human blood and is one of the serine proteinase inhibitors (serpins). The primary function of C1 inhibitor is to regulate the activation of the complement and intrinsic coagulation (contact system) pathway. C1 inhibitor also regulates the fibrinolytic system. Regulation of these systems is performed through the formation of complexes between the proteinases and the inhibitor, resulting in inactivation of both and consumption of the C1 inhibitor. HAE patients have low levels of endogenous or functional C1 inhibitor. Although the events that induce attacks of angioedema in HAE patients are not well defined, it is thought by some that increased vascular permeability and the clinical manifestation of HAE attacks are primarily mediated through contact system activation. Suppression of contact system activation by C1 inhibitor through the inactivation of plasma kallikrein and factor XIIa is thought to modulate this vascular permeability by preventing the generation of bradykinin1. Administration of C1 Esterase Inhibitor increases plasma levels of C1 inhibitor activity. | NA | NA | NA | NA | NA | NA | NA | NA | NA | Cyproterone acetate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Danazol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Desogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Dienogest may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Drospirenone may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estropipate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethinyl Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethynodiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Etonogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human). | Plasma protease C1 inhibitor | Berinert 1500 | Csl Behring Canada Inc | Csl Behring Canada Inc | Berinert is a plasma-derived concentrate of C1 Esterase Inhibitor (Human) indicated for the treatment of acute abdominal, facial, or laryngeal attacks of hereditary angioedema (HAE) in adult and adolescent patients. | NA | 1500 unit | kit; powder for solution | IV | Administer Berinert at a dose of 20 International Units (IU) per kg body weight by intravenous injection. Doses lower than 20 IU/kg body weight should not be administered. Berinert is provided as a freeze-dried powder for reconstitution with the Sterile Water for Injection, USP provided. Store the vial in the original carton in order to protect from light. Do not freeze. | Berinert is contraindicated in individuals who have experienced life-threatening hypersensitivity reactions, including anaphylaxis, to C1 esterase inhibitor preparations. | The most serious adverse reaction reported in subjects enrolled in clinical studies who received Berinert was an increase in the severity of pain associated with HAE. The most common adverse reaction reported in greater than 4% of the subjects and greater than placebo among subjects who received Berinert in the placebo-controlled clinical trial was dysgeusia. | Link | NA | NA |
| 10744 | Th1171 | C1 Esterase Inhibitor (Human) | NA | 68000 | NA | NA | NA | NA | Following intravenous administration of a single dose, the half-life was 56 ± 36 hours.3 Subcutaneous administration produces a half-life of 199.6 hours | Recombinant human C1 esterase inhibitor is a human protein developed through Pharming’s proprietary technology where the human protein is expressed in milk of transgenic rabbits. Hereditary Angioedema (HAE) is a human genetic disorder caused by a shortage of C1 inhibitor activity and results in an overreaction of the immune system. The disease is characterized by acute attacks of painful and in some cases fatal swelling of several soft tissues (edema), which may last up to five days when untreated. | For routine prophylaxis against angioedema attacks in adolescent and adult patients with Hereditary Angioedema (HAE). | In clinical studies, intravenous administration demonstrated an increase in plasma levels of C1 inhibitor within approximately one hour or less of administration. | C1 inhibitor is a normal constituent of human blood and is one of the serine proteinase inhibitors (serpins). The primary function of C1 inhibitor is to regulate the activation of the complement and intrinsic coagulation (contact system) pathway. C1 inhibitor also regulates the fibrinolytic system. Regulation of these systems is performed through the formation of complexes between the proteinases and the inhibitor, resulting in inactivation of both and consumption of the C1 inhibitor. HAE patients have low levels of endogenous or functional C1 inhibitor. Although the events that induce attacks of angioedema in HAE patients are not well defined, it is thought by some that increased vascular permeability and the clinical manifestation of HAE attacks are primarily mediated through contact system activation. Suppression of contact system activation by C1 inhibitor through the inactivation of plasma kallikrein and factor XIIa is thought to modulate this vascular permeability by preventing the generation of bradykinin1. Administration of C1 Esterase Inhibitor increases plasma levels of C1 inhibitor activity. | NA | NA | NA | NA | NA | NA | NA | NA | NA | Cyproterone acetate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Danazol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Desogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Dienogest may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Drospirenone may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estropipate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethinyl Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethynodiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Etonogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human). | Plasma protease C1 inhibitor | Berinert 500 | Csl Behring Canada Inc | Csl Behring Canada Inc | Berinert is a plasma-derived concentrate of C1 Esterase Inhibitor (Human) indicated for the treatment of acute abdominal, facial, or laryngeal attacks of hereditary angioedema (HAE) in adult and adolescent patients. | NA | 500 unit | kit; powder for solution | IV | Administer Berinert at a dose of 20 International Units (IU) per kg body weight by intravenous injection. Doses lower than 20 IU/kg body weight should not be administered. Berinert is provided as a freeze-dried powder for reconstitution with the Sterile Water for Injection, USP provided. Store the vial in the original carton in order to protect from light. Do not freeze. | Berinert is contraindicated in individuals who have experienced life-threatening hypersensitivity reactions, including anaphylaxis, to C1 esterase inhibitor preparations. | The most serious adverse reaction reported in subjects enrolled in clinical studies who received Berinert was an increase in the severity of pain associated with HAE. The most common adverse reaction reported in greater than 4% of the subjects and greater than placebo among subjects who received Berinert in the placebo-controlled clinical trial was dysgeusia. | Link | NA | NA |
| 10745 | Th1171 | C1 Esterase Inhibitor (Human) | NA | 68000 | NA | NA | NA | NA | Following intravenous administration of a single dose, the half-life was 56 ± 36 hours.3 Subcutaneous administration produces a half-life of 199.6 hours | Recombinant human C1 esterase inhibitor is a human protein developed through Pharming’s proprietary technology where the human protein is expressed in milk of transgenic rabbits. Hereditary Angioedema (HAE) is a human genetic disorder caused by a shortage of C1 inhibitor activity and results in an overreaction of the immune system. The disease is characterized by acute attacks of painful and in some cases fatal swelling of several soft tissues (edema), which may last up to five days when untreated. | For routine prophylaxis against angioedema attacks in adolescent and adult patients with Hereditary Angioedema (HAE). | In clinical studies, intravenous administration demonstrated an increase in plasma levels of C1 inhibitor within approximately one hour or less of administration. | C1 inhibitor is a normal constituent of human blood and is one of the serine proteinase inhibitors (serpins). The primary function of C1 inhibitor is to regulate the activation of the complement and intrinsic coagulation (contact system) pathway. C1 inhibitor also regulates the fibrinolytic system. Regulation of these systems is performed through the formation of complexes between the proteinases and the inhibitor, resulting in inactivation of both and consumption of the C1 inhibitor. HAE patients have low levels of endogenous or functional C1 inhibitor. Although the events that induce attacks of angioedema in HAE patients are not well defined, it is thought by some that increased vascular permeability and the clinical manifestation of HAE attacks are primarily mediated through contact system activation. Suppression of contact system activation by C1 inhibitor through the inactivation of plasma kallikrein and factor XIIa is thought to modulate this vascular permeability by preventing the generation of bradykinin1. Administration of C1 Esterase Inhibitor increases plasma levels of C1 inhibitor activity. | NA | NA | NA | NA | NA | NA | NA | NA | NA | Cyproterone acetate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Danazol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Desogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Dienogest may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Drospirenone may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Estropipate may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethinyl Estradiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Ethynodiol may increase the thrombogenic activities of C1 Esterase Inhibitor (Human); Etonogestrel may increase the thrombogenic activities of C1 Esterase Inhibitor (Human). | Plasma protease C1 inhibitor | Cinryze | Viropharma Biologics Inc | Viropharma Biologics Inc | CINRYZE is a C1 esterase inhibitor indicated for routine prophylaxis against angioedema attacks in adolescent and adult patients with Hereditary Angioedema (HAE). | NA | 500 unit | powder for solution | IV | A dose of 1,000 Units CINRYZE can be administered every 3 or 4 days for routine prophylaxis against angioedema attacks in HAE patients. CINRYZE is administered at an injection rate of 1 mL per minute. | CINRYZE is contraindicated in patients who have manifested life-threatening immediate hypersensitivity reactions, including anaphylaxis to the product. | The only serious adverse reaction observed in clinical studies of CINRYZE was cerebrovascular accident. The most common adverse reactions observed were headache, nausea, rash, and vomiting. | Link | NA | NA |
| 11387 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Amino Acids, Peptides, and Proteins | NA | NA | NA | Catridecacog,Aminocaproic acid,Alpha-1-proteinase inhibitor,Menadione,Tranexamic acid,Aprotinin,Hydrogen peroxide,Aminomethylbenzoic acid,Camostat,Menadione bisulfite,Monteplase,Lepirudin,Bivalirudin,Alteplase,Urokinase,Reteplase,Anistreplase,Tenecteplase,Abciximab,Drotrecogin alfa,Streptokinase,Dicoumarol,Argatroban,Ardeparin,Phenindione,Fondaparinux,Warfarin,Pentosan polysulfate,Phenprocoumon,Dipyridamole,Heparin,Enoxaparin,Epoprostenol,Acenocoumarol,4-hydroxycoumarin,Coumarin,Ximelagatran,Desmoteplase,Defibrotide,Ancrod,Beraprost,Fibrinolysin,Prasugrel,Rivaroxaban,Sulodexide,Idraparinux,Cangrelor,Astaxanthin,Apixaban,Otamixaban,Amediplase,Dabigatran etexilate,Danaparoid,Dalteparin,Tinzaparin,Ferulic acid,(R)-warfarin,Ethyl biscoumacetate,Nadroparin,Triflusal,Ticagrelor,Ditazole,Vorapaxar,Edoxaban,Potassium citrate,Sodium citrate,Dextran,Bemiparin,Parnaparin,Desirudin,Zinc citrate,Antithrombin Alfa,Protein C,Antithrombin III human,Letaxaban,Darexaban,Betrixaban,Nafamostat,Gabexate,Fluindione,Protein S human,Brinase,Clorindione,Diphenadione,Tioclomarol,Melagatran,Saruplase,(S)-Warfarin,Tocopherylquinone,Edetate calcium disodium anhydrous,Dabigatran,Semuloparin,Troxerutin,Edetic acid,Reviparin,Dermatan sulfate,SR-123781A,Dociparstat sodium | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase | Novo Nordisk | Novo Nordisk | Intravenous | 1.2 mg / vial | NA | NA | NA | NA | NA | NA | Link | Link | NA |
| 11388 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Biological Factors | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase | Novo Nordisk | Novo Nordisk | Intravenous | 2.4 mg / vial | NA | NA | NA | NA | NA | NA | Link | Link | NA |
| 11389 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Blood and Blood Forming Organs | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase | Novo Nordisk | Novo Nordisk | Intravenous | 4.8 mg / vial | NA | NA | NA | NA | NA | NA | Link | Link | NA |
| 11390 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Blood Coagulation Factors | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase RT | Novo Nordisk | Novo Nordisk | Intravenous | 1 mg / vial | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11391 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Blood Proteins | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase RT | Novo Nordisk | Novo Nordisk | Intravenous | 2 mg / vial | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11392 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Endopeptidases | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase RT | Novo Nordisk | Novo Nordisk | Intravenous | 5 mg / vial | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11393 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Enzyme Precursors | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Niastase RT | Novo Nordisk | Novo Nordisk | Intravenous | 8 mg / vial | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11394 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Enzymes | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Novoseven | Novo Nordisk | Novo Nordisk | Intravenous | 50 KIU | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | fever, headache, injection site reactions (pain, redness, or irritation), dizziness, nausea, or vomiting. | NovoSeven RT with MixPro is a man-made protein similar to a natural protein in the body that helps the blood to clot. NovoSeven RT with MixPro is used to treat or prevent bleeding in people with hemophilia A or hemophilia B, or factor VII deficiency. NovoSeven RT with MixPro may also be used for purposes... | NovoSeven (coagulation factor viia (recombinant)) is indicated for: | NA | REFERENCES | Link | Link | NA |
| 11395 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Enzymes and Coenzymes | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Novoseven | Novo Nordisk | Novo Nordisk | Intravenous | 100 KIU | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | fever, headache, injection site reactions (pain, redness, or irritation), dizziness, nausea, or vomiting. | NovoSeven RT with MixPro is a man-made protein similar to a natural protein in the body that helps the blood to clot. NovoSeven RT with MixPro is used to treat or prevent bleeding in people with hemophilia A or hemophilia B, or factor VII deficiency. NovoSeven RT with MixPro may also be used for purposes... | NovoSeven (coagulation factor viia (recombinant)) is indicated for: | NA | REFERENCES | Link | Link | NA |
| 11396 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Factor VII | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Novoseven | Novo Nordisk | Novo Nordisk | Intravenous | 250 KIU | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | fever, headache, injection site reactions (pain, redness, or irritation), dizziness, nausea, or vomiting. | NovoSeven RT with MixPro is a man-made protein similar to a natural protein in the body that helps the blood to clot. NovoSeven RT with MixPro is used to treat or prevent bleeding in people with hemophilia A or hemophilia B, or factor VII deficiency. NovoSeven RT with MixPro may also be used for purposes... | NovoSeven (coagulation factor viia (recombinant)) is indicated for: | NA | REFERENCES | Link | Link | NA |
| 11397 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Hemostatics | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Novoseven | Novo Nordisk | Novo Nordisk | Intravenous | 400 KIU | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | fever, headache, injection site reactions (pain, redness, or irritation), dizziness, nausea, or vomiting. | NovoSeven RT with MixPro is a man-made protein similar to a natural protein in the body that helps the blood to clot. NovoSeven RT with MixPro is used to treat or prevent bleeding in people with hemophilia A or hemophilia B, or factor VII deficiency. NovoSeven RT with MixPro may also be used for purposes... | NovoSeven (coagulation factor viia (recombinant)) is indicated for: | NA | REFERENCES | Link | Link | NA |
| 11398 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Hydrolases | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NovoSeven RT | Novo Nordisk | Novo Nordisk | Intravenous | 1 mg/1mL | NovoSeven Coagulation Factor VIIa (Recombinant) should not be administered to patients with known hypersensitivity to NovoSeven (coagulation factor viia (recombinant)) or any of the components of NovoSeven (coagulation factor viia (recombinant)) . NovoSeven (coagulation factor viia (recombinant)) is contraindicated in patients with known hypersensitivity to mouse, hamster, or bovine proteins. | Bloating or swelling of the face, hands, lower legs, or feet bluish color of the hands or feet blurred vision changes in facial color chest pain chills cold sweats confusion continuing thirst cough dizziness excessive sweating faintness fast heartbeat hives, itching, or skin rash large flat blue or purplish patches on the skin lightheadedness when getting up suddenly from a lying or sitting position persistent bleeding or oozing from puncture sites or mucous membranes (bowel, mouth, nose, or urinary bladder) puffiness or swelling of the eyelids or around the eyes shakiness slow or irregular heartbeat (less than 50 beats per minute) slurred speech sneezing sore throat sudden decrease in the amount of urine swelling of the face, fingers, feet, or lower legs troubled breathing, tightness in the chest unusual tiredness or weakness unusual weight gain | NA | NA | NA | NA | Link | Link | NA |
| 11399 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Increased Coagulation Factor IX Activity | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Sevenfact | Laboratoire Français du Fractionnement et des Biotechnologies Société Anonyme (LFB S.A.) | Laboratoire Français du Fractionnement et des Biotechnologies Société Anonyme (LFB S.A.) | Intravenous | 1 mg/1mL | SEVENFACT is contraindicated in known allergy to rabbits or rabbit proteins. Exposure to SEVENFACT in these patients can result in severe hypersensitivity reaction. patients with severe hypersensitivity reaction to SEVENFACT or any of its components. Exposure to SEVENFACT in these patients can result in severe hypersensitivity reaction. | headache, dizziness, infusion-site discomfort, infusion-site bleeding, infusion-related reactions, and fever | Coagulation factor VIIa-jncw is used to treat and prevent bleeding episodes in patients with Hemophilia A or B. Factor VIIa-jncw is a man-made protein produced to replicate the naturally occurring activated factor VII (factor VIIa) in the body. It is used to stop bleeding of injuries for patients with... | Sevenfact [coagulation factor VIIa (recombinant)-jncw] is a coagulation factor VIIa concentrate indicated for the treatment and control of bleeding episodes occurring in adults and adolescents (12 years of age and older) with hemophilia A or B with inhibitors. | NA | NA | Link | Link | NA |
| 11400 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Increased Coagulation Factor X Activity | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | Sevenfact | Laboratoire Français du Fractionnement et des Biotechnologies Société Anonyme (LFB S.A.) | Laboratoire Français du Fractionnement et des Biotechnologies Société Anonyme (LFB S.A.) | Intravenous | 5 mg/1mL | SEVENFACT is contraindicated in known allergy to rabbits or rabbit proteins. Exposure to SEVENFACT in these patients can result in severe hypersensitivity reaction. patients with severe hypersensitivity reaction to SEVENFACT or any of its components. Exposure to SEVENFACT in these patients can result in severe hypersensitivity reaction. | headache, dizziness, infusion-site discomfort, infusion-site bleeding, infusion-related reactions, and fever | Coagulation factor VIIa-jncw is used to treat and prevent bleeding episodes in patients with Hemophilia A or B. Factor VIIa-jncw is a man-made protein produced to replicate the naturally occurring activated factor VII (factor VIIa) in the body. It is used to stop bleeding of injuries for patients with... | Sevenfact [coagulation factor VIIa (recombinant)-jncw] is a coagulation factor VIIa concentrate indicated for the treatment and control of bleeding episodes occurring in adults and adolescents (12 years of age and older) with hemophilia A or B with inhibitors. | NA | NA | Link | Link | NA |
| 11401 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Peptide Hydrolases | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11402 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Proteins | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11403 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Serine Endopeptidases | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 11404 | Th1246 | Coagulation factor VIIa Recombinant Human | >Th1246_Coagulation_factor_VIIa_Recombinant_Human ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP | 45079.1 | C1972H3076N560O597S28 | 6.09 | -0.311 | 58 °C | NA | Recombinant human coagulation Factor VIIa (rFVIIa), intended for promoting hemostasis by activating the extrinsic pathway of the coagulation cascade. NovoSeven is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. Cloned and expressed in hamster kidney cells, the protein is catalytically active in a two-chain form. | For treatment of hemorrhagic complications in hemophilia A and B. | Used in the treatment of bleeding episodes in hemophilia A or B. NovoSeven is recombinant Factor VIIa and, when complexed with tissue factor can activate coagulation Factor X to Factor Xa, as well as coagulation Factor IX to Factor IXa. Factor Xa, in complex with other factors, then converts prothrombin to thrombin, which leads to the formation of a hemostatic plug by converting fibrinogen to fibrin and thereby inducing local clotting. | NovoSeven activates the coagulation or clotting cascade by cleaving Factor IX and Factor X, which activates them and then leads to activation of thrombin and fibrin. | NA | NA | NA | * 121 ± 30 mL/kg [adults] * 153 ± 29 mL/kg [children] * 280 to 290 mL/kg [congenital Factor VII deficiency] | * 33 - 37 mL/h x kg [healthy] * 1375 +/- 396 mL/hr [severe hemophilia A male children] * 57.3 +/- 9.5 mL/hr/kg [severe hemophilia A male children] * 2767 +/- 385 mL/hr [severe hemophilia A men] * 37.6 +/- 13.1 mL/hr/kg [severe hemophilia A men] | Serine Proteases | NA | NA | NA | NA | Coagulation factor X,Tissue factor pathway inhibitor,Vitamin K-dependent gamma-carboxylase,Coagulation factor VII,Tissue factor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12060 | 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 | Anticoagulants | 2624691 | 06-01-1953 | 06-01-1980 | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12061 | 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 | Blood and Blood Forming Organs | 3136703 | 09-06-1964 | 09-06-1981 | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12062 | 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 | Cardiovascular Agents | 3234106 | 08-02-1966 | 08-02-1983 | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12063 | 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 | Endopeptidases | 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 |
| 12064 | Th1283 | Fibrinolysin | >Th1283_Fibrinolysin DLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGR | 88411.4 | C3848H5912N1096O1185S60 | NA | NA | NA | Almost completely inactivated after 24 hours. | Fibrinolysin consists of two polypeptide chains, one light and one heavy, linked by a disulfide bond. The light chain has a molecular weight of approximately 27,000 Da and contains the active center of Fibrinolysin; the heavy chain has a molecular weight of approximately 57,000 Da. Fibrinolysin is used as a local healing ointment when combined together with the enzyme deoxyribonuclease I (extracted from bovine pancreas). Fibrinolysin and deoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) Fibrinolysin and 666 BUs desoxyribonuclease per gram. The ointment is marketed by Pfizer under the brand name Fibrolan in a variety of countries (e.g. Switzerland). It is currently not approved in the USA. | Fibrinolysin assists with the healing of minor burns, superficial wounds, ulcers, surgical wounds, and superficial hematomas. | NA | Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living tissue. | NA | local inactivation | NA | NA | NA | Enzymes | NA | NA | NA | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12065 | Th1283 | Fibrinolysin | >Th1283_Fibrinolysin DLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAENSKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSPEKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAKTMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDIPRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNLEENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYHGNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPCQEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCESSFDCGKPKVEPKKCSGR | 88411.4 | C3848H5912N1096O1185S60 | NA | NA | NA | Almost completely inactivated after 24 hours. | Fibrinolysin consists of two polypeptide chains, one light and one heavy, linked by a disulfide bond. The light chain has a molecular weight of approximately 27,000 Da and contains the active center of Fibrinolysin; the heavy chain has a molecular weight of approximately 57,000 Da. Fibrinolysin is used as a local healing ointment when combined together with the enzyme deoxyribonuclease I (extracted from bovine pancreas). Fibrinolysin and deoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) Fibrinolysin and 666 BUs desoxyribonuclease per gram. The ointment is marketed by Pfizer under the brand name Fibrolan in a variety of countries (e.g. Switzerland). It is currently not approved in the USA. | Fibrinolysin assists with the healing of minor burns, superficial wounds, ulcers, surgical wounds, and superficial hematomas. | NA | Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living tissue. | NA | local inactivation | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Plasminogen activator inhibitor 1,Urokinase-type plasminogen activator | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12066 | 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 | Fibrin Modulating 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 |
| 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 |
| 12069 | 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 | Hematologic 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 |
| 12070 | 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 | Hydrolases | 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 |
| 12071 | 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 | Peptide Hydrolases | 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 |
| 12072 | 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 | Serine Endopeptidases | 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 |
| 12073 | 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 | Serine Proteases | 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 |
| 12635 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Agents causing angioedema | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12636 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Amino Acids, Peptides, and Proteins | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12637 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Biological Factors | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12638 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Blood Proteins | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12639 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Endopeptidases | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12640 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Enzymes | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12641 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Enzymes and Coenzymes | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12642 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Hydrolases | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12643 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Peptide Hydrolases | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12644 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Plasminogen Activators | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12645 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Proteins | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12646 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Serine Endopeptidases | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 12647 | Th1341 | Lanoteplase | >Th1341_Lanoteplase GARSYQVIDTRATCYEDQGISYRGTWSTAESGAECTNWQSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHMLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | NA | NA | NA | NA | NA | NA | 0 | Investigated for use/treatment in myocardial infarction. | NA | Lanoteplase is a second generation derivative of alteplase, and a third generation recombinant plasminogen activator made from a deletion and point mutant of tissue type-plasminogen activator (t-PA). Lanoteplase has a longer half life than alteplase. Lanoteplase is a serine protease that binds to fibrin in a thrombus (blood clot)and cleaves the Arg-Val bond in plasminogen, producing active plasmin. Plasmin is an enzyme that degrades plasma proteins such as fibrin clots to clear blocked blood vessels that cause myocardial infarction (heart attack) or stroke. | NA | NA | NA | NA | NA | Serine Proteases | NA | NA | NA | NA | Urokinase plasminogen activator surface receptor,Fibrinogen alpha chain,Kallikrein-1,Laminin subunit alpha-5,Coagulation factor X,Fibronectin,Plasminogen activator inhibitor 2,Tetranectin,Keratin, type II cytoskeletal 8,Annexin A2,Laminin subunit beta-1,Laminin subunit gamma-1,Laminin subunit alpha-1,Calreticulin,Calnexin,Prolow-density lipoprotein receptor-related protein 1,Laminin subunit alpha-3 | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15506 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Amino Acids, Peptides, and Proteins | NA | NA | NA | NA | Tissue factor pathway inhibitor | Andexxa | Alexion Pharmaceuticals, Inc. | Alexion Pharmaceuticals, Inc. | Intravenous | 100 mg/10mL | None. | urinary tract infections (UTIs), pneumonia, and infusion-related reactions | Andexxa is a protein that reverses the effects of certain anticoagulant medications that are used to treat or prevent blood clots. Reversing anticoagulant medicine is necessary if you have uncontrolled or life-threatening bleeding as a result of how that medicine works. Andexxa is used to treat uncontrolled... | ANDEXXA® (coagulation factor Xa (recombinant), inactivated-zhzo) Lyophilized Powder for Solution For Intravenous Injection | NA | NA | Link | Link | NA |
| 15507 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Antidotes | NA | NA | NA | NA | Tissue factor pathway inhibitor | Andexxa | Alexion Pharmaceuticals, Inc. | Alexion Pharmaceuticals, Inc. | Intravenous | 200 mg/20mL | None. | urinary tract infections (UTIs), pneumonia, and infusion-related reactions | Andexxa is a protein that reverses the effects of certain anticoagulant medications that are used to treat or prevent blood clots. Reversing anticoagulant medicine is necessary if you have uncontrolled or life-threatening bleeding as a result of how that medicine works. Andexxa is used to treat uncontrolled... | ANDEXXA® (coagulation factor Xa (recombinant), inactivated-zhzo) Lyophilized Powder for Solution For Intravenous Injection | NA | NA | Link | Link | NA |
| 15508 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Biological Factors | NA | NA | NA | NA | Tissue factor pathway inhibitor | Ondexxya | Alexion Europe Sas | Alexion Europe Sas | Intravenous | 200 mg | NA | Based on studies in healthy volunteers, the most common side effects with Ondexxya (which may affect more than 1 in 10 people) are flushing, feeling hot, both of which are related to infusing the medicine, and a short-lived increase in levels of certain proteins indicating blood clotting. In patients who were bleeding, the most common side effects (affecting around 1 in 10 people) were thromboembolism (problems due to clots in blood vessels such as blocked veins, heart attack and stroke) and fever. | Andexanet alfa, the active substance in Ondexxya, acts as a decoy target for anticoagulants called factor Xa inhibitors such as apixaban and rivaroxaban. These anticoagulants work by blocking factor Xa, a natural protein that helps the blood to clot. When Ondexxya is given, the anticoagulants attach to andexanet alfa instead, and they are no longer available to block factor Xa. As a result, the excessive bleeding caused by the anticoagulants is reduced. | used for stopping life-threatening or uncontrolled bleeding in adults taking the anticoagulant medicines apixaban or rivaroxaban. | NA | NA | Link | Link | NA |
| 15509 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Blood Coagulation Factors | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15510 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Blood Proteins | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15511 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Coagulants | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15512 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Endopeptidases | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15513 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Enzymes | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15514 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Enzymes and Coenzymes | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15515 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Factor X | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15516 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Hydrolases | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15517 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Peptide Hydrolases | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15518 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Proteins | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15519 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Serine Endopeptidases | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 15520 | Th1604 | Andexanet alfa | >Th1604_Andexanet_alfa ANSFLFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRRKRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDAGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | NA | NA | NA | NA | NA | The elimination half-life ranges from 5 to 7 hours [L3725]. | Andexanet alfa is a recombinant human coagulation Factor Xa that promotes blood coagulation. It was developed by Portola Pharmaceuticals and was approved in in May 2018. It is marketed as Andexxa for intravenous injection or infusion and is indicated for the reversal of anticoagulation in combination with [rivaroxaban] and [apixaban] in cases of life-threatening or uncontrolled bleeding. Rivaroxaban and apixaban are Factor Xa inhibitors that promote anticoagulation in situations where blood clotting is unfavourable, such as in deep vein thrombosis and pulmonary embolism. However, the use of these agents is associated with a risk for uncontrollable bleeding episodes that can lead to can cause serious or fatal bleeding. Andexanet alfa is currently under regulatory review by the European Union and is undergoing clinical development in Japan [A35518]. Andexanet alfa works by binding to Factor Xa inhibitors and prevent them from interacting with endogenous Factor Xa. It displayed high affinity (0.53–1.53 nmol/L) to apixaban, betrixaban, edoxaban and rivaroxaban [A35518]. However, the effectiveness of andexanet alfa on treating bleeding related to any FXa inhibitors other than apixaban and rivaroxaban was not demonstrated, thus such use is limited [L3725]. Its pharmacokinetic properties are not reported to be affected by factor Xa inhibitors [A35518]. Andexanet alfa retains the structural similarity to that of endogenous human factor Xa, but exists in its mature functional form without the need for activation via the intrinsic or extrinsic coagulation pathways [A35558] and remains catalytically inactive due to structural modification [A35518]. The procoagulation potential of andexanet alfa is eliminated through the removal of a 34-residue fragment containing Gla: via this truncation, andexanet alfa is unable to bind to membrane surfaces and assemble the prothrombinase complex [A35558]. It also prevents andexanet alfa from taking up space on phospholipid surface membranes, so that native FXa may bind and assemble the prothrominase complex [A35558]. The amino acid residue modification from serine to alanine in the binding site of the catalytic domain allows more effective binding to FXa inhibitors and deters the andexanet alfa from converting prothrombin to thrombin [A35558]. | Andexanet alfa is indicated for patients treated with [rivaroxaban] and [apixaban], when reversal of anticoagulation is needed due to life-threatening or uncontrolled bleeding [L3725]. Andexxa has not been shown to be effective for, and is not indicated for, the treatment of bleeding related to any Factor Xa inhibitors other than apixaban and rivaroxaban [L3725]. | _In vitro_, andexanet alfa was shown to dose-dependently reverse the activity of apixaban, betrixaban, edoxaban, rivaroxaban, enoxaparin and fondaparinux on Factor Xa in human and rat plasma [A35518]. In a randomized placebo-controlled study of healthy elderly volunteers, co-administration of andexanet alfa bolus with 5 mg of apixaban twice daily resulted in a reduction of anti-factor Xa activity by 94% compared to 21% among those who received placebo, and thrombin generation was fully restored in 100% [A35519]. The anti-factor Xa activity was reduced by 92% and thrombin generation was fully restored in 96% of the subjects upon andexanet alfa bolus administration in subjects receiving 20 mg of rivaroxaban daily [A35519]. A multicenter, prospective, open-label, single-group study involving elderly patients with acute major bleeding within 18 hours after the administration of a factor Xa inhibitor was performed. In this study, the median anti-factor Xa activity in patients receiving rivaroxaban and apixaban was reduced by 89% and 93%, respectively, upon administration of andexanet alfa infusion [A35520]. In dose-ranging studies of healthy volunteers, the anti-FXa activity activity was observed within two minutes after the completion of the bolus administration. Elevation of Tissue Factor (TF)-initiated thrombin generation above the baseline range (prior to anticoagulation) occurred within two minutes following a bolus administration of andexanet alfa and was maintained throughout the duration of the continuous infusion [L3725]. The anti-FXa activity returned to the placebo levels approximately 2 hours after completion of a bolus or continuous infusion [L3725]. In contrast, TFPI activity in plasma was sustained for at least 22 hours following andexanet alfa administration [L3725]. | Factor Xa inhibitors promote anticoagulation by binding to both free Factor Xa in plasma and Factor Xa attached to the prothrombinase complex. This ultimately leads to the blockade of thrombin generation or clot formation [A27288]. Andexanet alfa is a factor Xa decoy that binds to factor Xa inhibitors such as apixaban and rivaroxaban with high affinity and prevents them from binding to endogenous factor Xa. It was also shown to sequester factor Xa inhibitors, leading to reversing their anticoagulant effects and restoring the activity of endogenous factor Xa [A35518]. Andexanet alfa may also achieve procoagulation via binding and inhibiting the activity of Tissue Factor Pathway Inhibitor (TFPI), which is an endogenous inhibitor of Factor Xa [A35518]. Inhibition of TFPI by andexanet alfa resulted in a transient increase in the level of prothrombin fragments 1 and 2, thrombin-antithrombin complex and D-dimer [A35518]. Subsequently, this may result in increased tissue factor-initiated thrombin generation [L3725]. Since it is a genetically modified variant of human factor Xa, andexanet alfa is not able to cleave and activate prothrombin nor assemble into the prothrombinase complex [A35518]. | NA | There is limited information regarding the metabolism of andexanet alfa [A35558]. | Following intravenous administration of bolus doses > 30 mg in healthy subjects, the exposure of andexanet alfa increased in a dose-dependent manner. | The volume of distribution (Vd) for andexanet alfa is approximately equivalent to the blood volume of 5 L [L3725]. | Clearance for andexanet alfa is approximately 4.3 L/hr [L3725]. | Serine Proteases | NA | NA | NA | NA | Tissue factor pathway inhibitor | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | NA | Link | NA | NA |
| 16384 | Th1894 | Tirzepatide | >Th1894_Tirzepatide YXEGTFTSDYSIXLDKIAQKAFVQWLIAGGPSSGAPPPS | 4810.52 Da | C225H348N48O68 | NA | NA | NA | ,The half-life is approximately five days. | Tirzepatide is a novel dual glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) receptor agonist. Dual GIP/GLP-1 agonists gained increasing attention as new therapeutic agents for glycemic and weight control as they demonstrated better glucose control and weight loss compared to selective GLP-1 receptor agonists in preclinical and clinical trials. | Tirzepatide is a dual GIP and GLP-1 receptor agonist used for the treatment of type II diabetes in adults as an adjunct to diet and exercise. | Tirzepatide is a synthetic peptide with glucose-lowering effects. It works to stimulate first- and second-phase insulin secretion, and reduces glucagon levels, both in a glucose-dependent manner. Tirzepatide was also shown to delay gastric emptying, lower fasting and postprandial glucose concentration, decrease food intake,4 and reduce body weight in patients with type 2 diabetes. Tirzepatide can increase insulin sensitivity. | Glucagon-like peptide-1 (GLP-1) receptors (GLP-1R) are expressed throughout the body, including pancreatic beta-cells and the gastrointestinal tract. They have been implicated in the pathophysiology of type II diabetes mellitus as GLP-1R signalling is involved in glucose control by enhancing glucose-stimulated insulin secretion, delaying gastric transit, decreasing plasma glucagon levels, and reducing body weight by activating anorexigenic pathways in the brain. Both glucose-dependent insulinotropic polypeptide (GIP) and GLP-1 are peptide hormones involved in glucose homeostasis: they promote glucose-stimulated insulin secretion from the pancreatic beta-cells. However, GIP is the main incretin hormone that exerts insulinotropic effects in response to food intake. | There is limited information regarding the LD50 and overdose of tirzepatide. In case of an overdosage, appropriate supportive treatment should be initiated with a sufficient amount of time for observation and treatment, as tirzepatide has a long half-life. | Tirzepatide is metabolized by proteolytic cleavage of the peptide backbone, beta-oxidation of the C20 fatty diacid moiety, and amide hydrolysis. | Over the dose range of 1-5 mg, the Cmax of tirzepatide ranged from 108 to 397 ng/mL.The mean absolute bioavailability of tirzepatide following subcutaneous administration is 80%. Following subcutaneous administration, the Tmax ranged from eight to 72 hours. The steady-state plasma concentrations were achieved following four weeks of once-weekly subcutaneous administration. | Following subcutaneous administration, the mean steady-state volume of distribution was 9.5 L. The mean apparent steady-state volume of distribution of tirzepatide following subcutaneous administration in patients with type 2 diabetes mellitus was approximately 10.3 L. | The apparent population mean clearance of tirzepatide is 0.061 L/h.4 The mean steady-state apparent clearance of tirzepatide was 0.056 L/h. | Amino Acids, Peptides, and Proteins,Blood Glucose Lowering Agents,Gastrointestinal Hormones,GLP-1 Agonists,Hormones,Hormones, Hormone Substitutes, and Hormone Antagonists,Incretins,Nerve Tissue Proteins,Neuropeptides,Peptide Hormones,Peptides,Proteins | NA | NA | NA | NA | Glucagon-like peptide 1 receptor, Gastric inhibitory polypeptide | Mounjaro | Eli Lilly and Company | Eli Lilly and Company | Subcutaneous | 12.5 mg/0.5mL | MOUNJARO is contraindicated in patients with: A personal or family history of medullary thyroid carcinoma (MTC) or in patients with Multiple Endocrine Neoplasia syndrome type 2 | hives, difficulty breathing, swelling of your face, lips, tongue, or throat, dizziness, fast heart rate, shaking, sweating, nervousness, anxiety, irritability, confusion, dizziness, hunger, pain in the upper right side of your abdomen, pain spreading to your back or below the shoulder blade, nausea, vomiting, fever, yellowing of the skin and eyes (jaundice), clay-colored stools, and bloating of the abdomen | MOUNJARO (tirzepatide) injection, for subcutaneous use, contains tirzepatide, a once weekly GIP receptor and GLP-1 receptor agonist. It is a 39-amino-acid modified peptide based on the GIP sequence. Tirzepatide contains 2 non-coded amino acids (aminoisobutyric acid, Aib) in positions 2 and 13, a C-terminal amide, and Lys residue at position 20 that is attached to 1,20-eicosanedioic acid via a linker. | Mounjaro (tirzepatide) Injection is a prescription medicine used to treat the symptoms of Type 2 Diabetes Mellitus. | NA | MOUNJARO is a clear, colorless to slightly yellow, sterile, preservative-free solution for subcutaneous use. Each singledose pen contains a 0.5 mL solution of 2.5 mg, 5 mg, 7.5 mg, 10 mg, 12.5 mg, or 15 mg of tirzepatide and the following excipients: sodium chloride (4.1 mg), sodium phosphate dibasic heptahydrate (0.7 mg), and water for injection. Hydrochloric acid solution and/or sodium hydroxide solution may have been added to adjust the pH. MOUNJARO has a pH of 6.5 – 7.5. | Link | Link | NA |