Identification
- Summary
Moroctocog alfa is a recombinant Factor VIII used to treat hemophilia A to control bleeding.
- Brand Names
- Refacto AF, Xyntha
- Generic Name
- Moroctocog alfa
- DrugBank Accession Number
- DB13999
- Background
Moroctocog alfa, also known as BDDrFVIII (B domain deleted recombinant factor VIII), is a recombinant DNA-based drug with functional characteristics comparable to those of endogenous coagulation Factor VIII, the essential human blood clotting protein that is impaired in Hemophilia A. Moroctocog alfa is identical in sequence to endogenously produced Factor VIII, but does not contain the B-domain, which has no known biological function. Moroctocog alfa is produced through recombinant DNA technology and purification, resulting in a 1438 amino acid, 170 kDa protein Label. Clinical evaluation has shown that BDDrFVIII is pharmacokinetically equivalent to full-length recombinant FVIII 5,Label.
Also known as Anti-Hemophilic Factor (AHF), endogenous Factor VIII is essential to the clotting process in the body due to its involvement in the clotting cascade where it is responsible for acting as a co-factor to Factor IX. Activation of Factor IX leads to a cascade of signals that results in activation of Factor X, which then results in the conversion of prothrombin to thrombin, and as a result, leads to the conversion of fibrinogen to fibrin, the fibrous protein that creates the scaffold of the clot. Replacement of Factor VIII is essential for the treatment of Hemophilia A, which is caused by mutations in the Factor VIII gene, leading to a functional deficiency or complete loss of protein. Congenital loss or deficiency of Factor VIII results in the physiologic impairment of the coagulation clotting cascade, and as a result, leads to easy bruising and bleeding. Bleeding can range in severity from minor concerns, such as nosebleeds, to more serious events such as hemorrhaging in the joints, brain, or digestive tract 4.
Exogenous replacement of Factor VIII is currently the cornerstone of Hemophilia treatment and is used for the prophylaxis and control of bleeding episodes. Treatment has drastically improved since the 1960s when Factor VIII protein was primarily purified from human plasma, rather than being produced through recombinant DNA technology. Unfortunately, purification of protein from human plasma carries an increased risk of transmission of blood-borne diseases such as HIV and Hepatitis, which in part contributed to the Tainted Blood Scandal in the 1980s 3,2,6. Use of recombinant DNA-derived clotting factor treatments, such as Moroctocog alfa, has reduced this risk.
Other drug products with similar structure and function to Moroctocog alfa include Antihemophilic factor human, which is purified Factor VIII from human pooled blood and contains both A- and B-subunits, and Efmoroctocog alfa, which is a fully recombinant factor VIII-Fc fusion protein which has an extended half-life compared with conventional factor VIII due to conjugation to the dimeric Fc domain of human immunoglobulin G1, a long-lived plasma protein 3.
Moroctocog alfa is approved by Health Canada and by the European Medicines Agency for the control and prevention of hemorrhagic episodes and for routine and surgical prophylaxis in patients with hemophilia A (congenital factor VIII deficiency or classic hemophilia). As it does not contain von Willebrand factor it is not indicated in von Willebrand’s disease Label.
- Type
- Biotech
- Groups
- Approved
- Biologic Classification
- Protein Based Therapies
Blood factors - Protein Chemical Formula
- Not Available
- Protein Average Weight
- 173000.0 Da (glycosylated)
- Sequences
- Not Available
- Synonyms
- Antihemophilic factor (recombinant, B-domain deleted), plasma/albumin free
- Antihemophilic factor recombinant plasma/albumin free
- Antihemphilic factor, recombinant human B-domain deleted
- B-domain deleted recombinant factor VIII
- BDDrFVIII
- Human factor VIII, recombinant B-domain deleted
- Moroctocog alfa
Pharmacology
- Indication
Moroctocog alfa is indicated for use in adults and children with hemophilia A (congenital factor VIII deficiency) for on-demand treatment and control of bleeding episodes, perioperative management, and routine prophylaxis to reduce the frequency of bleeding episodes.7,8,9
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Prophylaxis of Bleeding caused by hemophilia a •••••••••••• Management of Bleeding caused by hemophilia a •••••••••••• Management of Bleeding caused by hemophilia a •••••••••••• - Associated Therapies
- Contraindications & Blackbox Warnings
Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
Antihemophilic Factor binds factor IXa along with calcium and phospholipid, which converts factor X to factor Xa to facilitate the clotting cascade.
- Mechanism of action
Antihemophilic factor (AHF) is a protein found in normal plasma which is necessary for clot formation. The administration of AHF provides an increase in plasma levels of AHF and can temporarily correct the coagulation defect of patients with hemophilia A (classical hemophilia). As factor VIII is the specific clotting factor deficient in patients with hemophilia A, replacement of clotting factor with Moroctocog alfa, also known as BDDrFVIII (B domain deleted recombinant factor VIII), is the cornerstone of the prevention and treatment of bleeding for this disorder.
Target Actions Organism ACoagulation factor X activatorHumans ACoagulation factor IX cofactorHumans Avon Willebrand factor binderHumans UPhytanoyl-CoA dioxygenase, peroxisomal antagonistHumans UAsialoglycoprotein receptor 2 binderHumans U78 kDa glucose-regulated protein chaperoneHumans UCalreticulin chaperoneHumans UCalnexin chaperoneHumans UProtein ERGIC-53 chaperoneHumans UProlow-density lipoprotein receptor-related protein 1 modulatorHumans UMultiple coagulation factor deficiency protein 2 modulatorHumans - Absorption
- Volume of distribution
Mean steady-state volume of distribution = 65.1 (± 35.1) mL/kg Label
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Mean terminal elimination half-life = 11.8 (± 5.1) hours Label Half-life = 11.2 ± 5.0 hours 5
- Clearance
Mean clearance = 4.21 (± 2.08) mL/h•kg Label Clearance = 4.51 ± 2.23 mL/h•kg 5
- Adverse Effects
Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs Browse all" title="About SNP Mediated Effects/ADRs" id="snp-actions-info" class="drug-info-popup" href="javascript:void(0);">
- Not Available
Interactions
- Drug Interactions Learn More" title="About Drug Interactions" id="structured-interactions-info" class="drug-info-popup" href="javascript:void(0);">
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareAbciximab The therapeutic efficacy of Moroctocog alfa can be decreased when used in combination with Abciximab. Acenocoumarol The therapeutic efficacy of Moroctocog alfa can be decreased when used in combination with Acenocoumarol. Alpha-1-proteinase inhibitor Alpha-1-proteinase inhibitor may increase the thrombogenic activities of Moroctocog alfa. Alteplase The therapeutic efficacy of Moroctocog alfa can be decreased when used in combination with Alteplase. Aminocaproic acid The risk or severity of adverse effects can be increased when Aminocaproic acid is combined with Moroctocog alfa. - Food Interactions
- No interactions found.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Brand Name Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Refacto Powder, for solution 1000 unit / vial Intravenous Wyeth Ltd. 2003-02-11 2009-01-23 Canada 
Refacto AF Injection, powder, for solution 2000 IU Intravenous Pfizer Europe Ma Eeig 2016-09-08 Not applicable EU 
Refacto AF Injection, powder, for solution 3000 IU Intravenous Pfizer Europe Ma Eeig 2016-09-08 Not applicable EU Refacto AF Injection, powder, for solution 500 IU Intravenous Pfizer Europe Ma Eeig 2016-09-08 Not applicable EU Refacto AF Injection, powder, for solution 1000 IU Intravenous Pfizer Europe Ma Eeig 2016-09-08 Not applicable EU - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Xyntha Moroctocog alfa (500 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL) Injection, powder, lyophilized, for solution; Kit Intravenous; Topical Wyeth BioPharma Division of Wyeth Pharmaceuticals LLC 2008-08-01 Not applicable US 
Xyntha Moroctocog alfa (2000 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL) Injection, powder, lyophilized, for solution; Kit Intravenous; Topical Wyeth BioPharma Division of Wyeth Pharmaceuticals LLC 2011-08-01 Not applicable US Xyntha Moroctocog alfa (1000 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL) Injection, powder, lyophilized, for solution; Kit Intravenous; Topical Wyeth BioPharma Division of Wyeth Pharmaceuticals LLC 2011-08-01 Not applicable US Xyntha Moroctocog alfa (2000 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL) Injection, powder, lyophilized, for solution; Kit Intravenous; Topical Wyeth BioPharma Division of Wyeth Pharmaceuticals LLC 2008-08-01 Not applicable US Xyntha Moroctocog alfa (250 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL) Injection, powder, lyophilized, for solution; Kit Intravenous; Topical Wyeth BioPharma Division of Wyeth Pharmaceuticals LLC 2008-08-01 Not applicable US
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- Not Available
- Kingdom
- Organic Compounds
- Super Class
- Organic Acids
- Class
- Carboxylic Acids and Derivatives
- Sub Class
- Amino Acids, Peptides, and Analogues
- Direct Parent
- Peptides
- Alternative Parents
- Not Available
- Substituents
- Not Available
- Molecular Framework
- Not Available
- External Descriptors
- Not Available
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 113E3Z3CJJ
- CAS number
- 284036-24-4
References
- General References
- Titheradge MA, Coore HG: Initial rates of pyruvate transport in mitochondria determined by an "inhibitor-stop" technique. Biochem J. 1975 Sep;150(3):553-6. [Article]
- Santagostino E: A new recombinant factor VIII: from genetics to clinical use. Drug Des Devel Ther. 2014 Dec 12;8:2507-15. doi: 10.2147/DDDT.S73241. eCollection 2014. [Article]
- Frampton JE: Efmoroctocog Alfa: A Review in Haemophilia A. Drugs. 2016 Sep;76(13):1281-1291. doi: 10.1007/s40265-016-0622-z. [Article]
- Franchini M, Mannucci PM: Hemophilia A in the third millennium. Blood Rev. 2013 Jul;27(4):179-84. doi: 10.1016/j.blre.2013.06.002. Epub 2013 Jun 28. [Article]
- Recht M, Nemes L, Matysiak M, Manco-Johnson M, Lusher J, Smith M, Mannucci P, Hay C, Abshire T, O'Brien A, Hayward B, Udata C, Roth DA, Arkin S: Clinical evaluation of moroctocog alfa (AF-CC), a new generation of B-domain deleted recombinant factor VIII (BDDrFVIII) for treatment of haemophilia A: demonstration of safety, efficacy, and pharmacokinetic equivalence to full-length recombinant factor VIII. Haemophilia. 2009 Jul;15(4):869-80. doi: 10.1111/j.1365-2516.2009.02027.x. Epub 2009 Apr 9. [Article]
- Have we forgotten the lessons of the tainted blood scandal? - The Globe and Mail [Link]
- DailyMed Label: XYNTHA SOLOFUSE (antihemophilic factor [recombinant]) for intravenous injection [Link]
- Summary of Product Characteristics: ReFacto AF (moroctocog alfa) Intravenous Injection [Link]
- Health Canada Product Monograph: Xyntha [Antihemophilic Factor (Recombinant)] For Intravenous Injection [Link]
- External Links
- KEGG Drug
- D08232
- ChEMBL
- CHEMBL2109137
- RxList
- RxList Drug Page
- Drugs.com
- Drugs.com Drug Page
- Wikipedia
- Moroctocog_alfa
- FDA label
- Download (985 KB)
Clinical Trials
- Clinical Trials Learn More" title="About Clinical Trials" id="clinical-trials-info" class="drug-info-popup" href="javascript:void(0);">
Phase Status Purpose Conditions Count 4 Completed Treatment Hemophilia A 3 4 Terminated Treatment Hemophilia A 2 3 Completed Treatment Hemophilia A 5 3 Terminated Treatment Hemophilia A 1 1 Completed Not Available Hemophilia A 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Powder, for solution Intravenous 1000 unit / vial Injection, powder, for solution Intravenous 3000 IU Injection, solution Intravenous 1000 iu Injection, solution Intravenous 2000 iu Injection, solution Intravenous 250 iu Injection, solution Intravenous 500 iu Injection, powder, lyophilized, for solution; kit Intravenous; Topical Kit; powder, for solution Intravenous 1000 unit / vial Kit; powder, for solution Intravenous 2000 unit / vial Kit; powder, for solution Intravenous 250 unit / vial Kit; powder, for solution Intravenous 500 unit / vial Injection, powder, lyophilized, for solution Intravenous 1000 IU Injection, powder, lyophilized, for solution Intravenous 500 IU Injection, powder, for solution Intravenous Injection, powder, for solution Intravenous 1000 IU Injection, powder, for solution Intravenous 2000 IU Injection, powder, for solution Intravenous 250 IU Injection, powder, for solution Intravenous 500 IU Powder, for solution Intravenous 1000 unit / syr Powder, for solution Intravenous 2000 unit / syr Powder, for solution Intravenous 250 unit / syr Powder, for solution Intravenous 3000 unit / syr Powder, for solution Intravenous 500 unit / syr Injection, powder, lyophilized, for solution Intravenous 2000 IU Injection, powder, lyophilized, for solution Intravenous 250 IU - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
- Not Available
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Activator
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
- Gene Name
- F10
- Uniprot ID
- P00742
- Uniprot Name
- Coagulation factor X
- Molecular Weight
- 54731.255 Da
References
- BLATRIX C, SOULIER JP: [Preparation of a fraction rich in prothrombin, proconvertin, Stuart factor and antihemophilic factor B (P.P.B. fraction)]. Pathol Biol (Paris). 1959 Dec;7:2477-86. [Article]
- LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF STUART FACTOR (FACTOR X) BY ACTIVATED ANTIHEMOPHILIC FACTOR (ACTIVATED FACTOR 8). Biochemistry. 1965 Jan;4:113-20. [Article]
- Radnoff OD, Saito H: Inhibition of Hageman factor, plasma thromboplastin antecedent, thrombin and other clotting factors by phenylglyoxal hydrate (38500). Proc Soc Exp Biol Med. 1975 Jan;148(1):177-82. [Article]
- Orthner CL: Characterization of proteases in AHF concentrates: effect on factor VIII:von Willebrand protein as assessed by high-pressure gel permeation chromatography. J Lab Clin Med. 1984 Nov;104(5):816-28. [Article]
- Freedman J, Mody M, Lazarus AH, Dewar L, Song S, Blanchette VS, Garvey MB, Ofosu FA: Platelet activation and hypercoagulability following treatment with porcine factor VIII (HYATE:C). Am J Hematol. 2002 Mar;69(3):192-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Cofactor
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholi...
- Gene Name
- F9
- Uniprot ID
- P00740
- Uniprot Name
- Coagulation factor IX
- Molecular Weight
- 51778.11 Da
References
- Hule V: [Factor IX inhibitor (antihemophilic factor B, PTC) in a woman]. Vnitr Lek. 1975 Mar;21(3):274-7. [Article]
- Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K: Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry. 1985 Jul 2;24(14):3736-50. [Article]
- LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF ANTIHEMOPHILIC FACTOR (FACTOR 8) BY ACTIVATED CHRISTMAS FACTOR (ACTIVATED FACTOR9 9). Biochemistry. 1964 Nov;3:1720-5. [Article]
- Hoofnagle JH, Gerety RJ, Thiel J, Barker LF: The prevalence of hepatitis B surface antigen in commercially prepared plasma products. J Lab Clin Med. 1976 Jul;88(1):102-13. [Article]
- Prince AM, Horowitz B, Brotman B, Huima T, Richardson L, van den Ende MC: Inactivation of hepatitis B and Hutchinson strain non-A, non-B hepatitis viruses by exposure to Tween 80 and ether. Vox Sang. 1984;46(1):36-43. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Binder
- General Function
- Protein n-terminus binding
- Specific Function
- Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surf...
- Gene Name
- VWF
- Uniprot ID
- P04275
- Uniprot Name
- von Willebrand factor
- Molecular Weight
- 309261.83 Da
References
- Shord SS, Lindley CM: Coagulation products and their uses. Am J Health Syst Pharm. 2000 Aug 1;57(15):1403-17; quiz 1418-20. [Article]
- Lillicrap D, Poon MC, Walker I, Xie F, Schwartz BA: Efficacy and safety of the factor VIII/von Willebrand factor concentrate, haemate-P/humate-P: ristocetin cofactor unit dosing in patients with von Willebrand disease. Thromb Haemost. 2002 Feb;87(2):224-30. [Article]
- Gill JC, Ewenstein BM, Thompson AR, Mueller-Velten G, Schwartz BA: Successful treatment of urgent bleeding in von Willebrand disease with factor VIII/VWF concentrate (Humate-P): use of the ristocetin cofactor assay (VWF:RCo) to measure potency and to guide therapy. Haemophilia. 2003 Nov;9(6):688-95. [Article]
- Smith KJ, Lusher JM, Cohen AR, Salzman P: Initial clinical experience with a new pasteurized monoclonal antibody purified factor VIIIC. Semin Hematol. 1990 Apr;27(2 Suppl 2):25-9. [Article]
- Altieri DC, Capitanio AM, Mannucci PM: von Willebrand factor contaminating porcine factor VIII concentrate (Hyate:C) causes platelet aggregation. Br J Haematol. 1986 Aug;63(4):703-11. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Antagonist
- General Function
- Phytanoyl-coa dioxygenase activity
- Specific Function
- Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
- Gene Name
- PHYH
- Uniprot ID
- O14832
- Uniprot Name
- Phytanoyl-CoA dioxygenase, peroxisomal
- Molecular Weight
- 38538.065 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Chen C, Wang Q, Fang X, Xu Q, Chi C, Gu J: Roles of phytanoyl-CoA alpha-hydroxylase in mediating the expression of human coagulation factor VIII. J Biol Chem. 2001 Dec 7;276(49):46340-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Binder
- General Function
- Carbohydrate binding
- Specific Function
- Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-...
- Gene Name
- ASGR2
- Uniprot ID
- P07307
- Uniprot Name
- Asialoglycoprotein receptor 2
- Molecular Weight
- 35092.04 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Bovenschen N, Rijken DC, Havekes LM, van Vlijmen BJ, Mertens K: The B domain of coagulation factor VIII interacts with the asialoglycoprotein receptor. J Thromb Haemost. 2005 Jun;3(6):1257-65. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Chaperone
- General Function
- Unfolded protein binding
- Specific Function
- Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded protein...
- Gene Name
- HSPA5
- Uniprot ID
- P11021
- Uniprot Name
- 78 kDa glucose-regulated protein
- Molecular Weight
- 72332.425 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Chaperone
- General Function
- Zinc ion binding
- Specific Function
- Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently wit...
- Gene Name
- CALR
- Uniprot ID
- P27797
- Uniprot Name
- Calreticulin
- Molecular Weight
- 48141.2 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Pipe SW, Morris JA, Shah J, Kaufman RJ: Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 1998 Apr 3;273(14):8537-44. [Article]
- Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol. 2008 Feb;87(2):107-12. Epub 2007 Sep 26. [Article]
- Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Chaperone
- General Function
- Poly(a) rna binding
- Specific Function
- Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembl...
- Gene Name
- CANX
- Uniprot ID
- P27824
- Uniprot Name
- Calnexin
- Molecular Weight
- 67567.695 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Pipe SW, Morris JA, Shah J, Kaufman RJ: Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 1998 Apr 3;273(14):8537-44. [Article]
- Becker S, Simpson JC, Pepperkok R, Heinz S, Herder C, Grez M, Seifried E, Tonn T: Confocal microscopy analysis of native, full length and B-domain deleted coagulation factor VIII trafficking in mammalian cells. Thromb Haemost. 2004 Jul;92(1):23-35. [Article]
- Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol. 2008 Feb;87(2):107-12. Epub 2007 Sep 26. [Article]
- Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Chaperone
- General Function
- Unfolded protein binding
- Specific Function
- Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or...
- Gene Name
- LMAN1
- Uniprot ID
- P49257
- Uniprot Name
- Protein ERGIC-53
- Molecular Weight
- 57548.665 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Cunningham MA, Pipe SW, Zhang B, Hauri HP, Ginsburg D, Kaufman RJ: LMAN1 is a molecular chaperone for the secretion of coagulation factor VIII. J Thromb Haemost. 2003 Nov;1(11):2360-7. [Article]
- Miao HZ, Sirachainan N, Palmer L, Kucab P, Cunningham MA, Kaufman RJ, Pipe SW: Bioengineering of coagulation factor VIII for improved secretion. Blood. 2004 May 1;103(9):3412-9. Epub 2004 Jan 15. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Modulator
- General Function
- Receptor activity
- Specific Function
- Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance...
- Gene Name
- LRP1
- Uniprot ID
- Q07954
- Uniprot Name
- Prolow-density lipoprotein receptor-related protein 1
- Molecular Weight
- 504601.695 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Franchini M, Montagnana M: Low-density lipoprotein receptor-related protein 1: new functions for an old molecule. Clin Chem Lab Med. 2011 Jun;49(6):967-70. doi: 10.1515/CCLM.2011.154. Epub 2011 Mar 11. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Modulator
- General Function
- Calcium ion binding
- Specific Function
- The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.
- Gene Name
- MCFD2
- Uniprot ID
- Q8NI22
- Uniprot Name
- Multiple coagulation factor deficiency protein 2
- Molecular Weight
- 16390.175 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Zhang B, Kaufman RJ, Ginsburg D: LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J Biol Chem. 2005 Jul 8;280(27):25881-6. Epub 2005 May 10. [Article]
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Activator
- General Function
- Thrombospondin receptor activity
- Specific Function
- Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostas...
- Gene Name
- F2
- Uniprot ID
- P00734
- Uniprot Name
- Prothrombin
- Molecular Weight
- 70036.295 Da
References
- Alberio L, Safa O, Clemetson KJ, Esmon CT, Dale GL: Surface expression and functional characterization of alpha-granule factor V in human platelets: effects of ionophore A23187, thrombin, collagen, and convulxin. Blood. 2000 Mar 1;95(5):1694-702. [Article]
- Ratnoff OD, Lewis JH: Heckathorn's disease: variable functional dificiency of antihemophilic factor (factor VIII). Blood. 1975 Aug;46(2):161-73. [Article]
- Anderson DM, Shelley S, Crick N, Buraglio M: No effect of the novel antidiabetic agent nateglinide on the pharmacokinetics and anticoagulant properties of warfarin in healthy volunteers. J Clin Pharmacol. 2002 Dec;42(12):1358-65. [Article]
- Piet MP, Chin S, Prince AM, Brotman B, Cundell AM, Horowitz B: The use of tri(n-butyl)phosphate detergent mixtures to inactivate hepatitis viruses and human immunodeficiency virus in plasma and plasma's subsequent fractionation. Transfusion. 1990 Sep;30(7):591-8. [Article]
- Lazarchick J, Ashby MA, Lazarchick JJ, Sens DA: Mechanism of factor VIII inactivation by human antibodies. IV. Antibody binding prevents factor VIII proteolysis by thrombin. Ann Clin Lab Sci. 1986 Nov-Dec;16(6):497-501. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inactivator
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts ...
- Gene Name
- PROC
- Uniprot ID
- P04070
- Uniprot Name
- Vitamin K-dependent protein C
- Molecular Weight
- 52070.82 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Bereczky Z, Kovacs KB, Muszbek L: Protein C and protein S deficiencies: similarities and differences between two brothers playing in the same game. Clin Chem Lab Med. 2010 Dec;48 Suppl 1:S53-66. doi: 10.1515/CCLM.2010.369. Epub 2010 Nov 5. [Article]
Drug created at March 20, 2018 17:53 / Updated at February 20, 2024 23:54