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IdentificationPharmacologyInteractionsReferencesTrialsEconomicsPropertiesSpectraTaxonomyAntihemophilic factor, human recombinant
Identification
- Name
- Antihemophilic factor, human recombinant
- Accession Number
- DB00025 (BTD00029, BIOD00029, DB13162, DBSALT002413)
- Type
- Biotech
- Groups
- Approved, Investigational
- Biologic Classification
- Protein Based Therapies
Blood factors - Description
Human recombinant antihemophilic factor (AHF) or Factor VIII, 2332 residues, glycosylated, produced by CHO cells
- Protein structure
- Protein chemical formula
- C11794H18314N3220O3553S83
- Protein average weight
- 264725.5 Da
- Sequences
>DB00025 sequence ATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFN IAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQ REKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCR EGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNR SLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLL MDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRF DDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIG RKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGI TDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNME RDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAG VQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKH KMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYE DSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMP KIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQ LHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDN TSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSW GKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSL LIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQK KEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEG QNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEK KETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNR TKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRL PLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSI PQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKK NNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHI YQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSK LLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKP EIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIY DEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTD GSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGA EPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHT NTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHA INGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYP GVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITAS GQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQ FIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRS TLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWR PQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKV KVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY
Download FASTA Format- Synonyms
- Antihemophilic factor (recombinant)
- Antihemophilic factor recombinant
- Antihemophilic factor, human recombinant
- Antihemophilic factor, recombinant
- Factor VIII (rDNA)
- Factor VIII (Recombinant)
- Factor VIII recombin
- Factor VIII, recombinant
- Human Factor VIII (Recombinant)
- Human factor VIII recombinant
- Octocog alfa
- rAHF
- Recombinant antihemophilic factor VIII
- External IDs
- BAY 14-2222 / BAY 81-8973 / BAY W 6240 / BAY-14-2222 / BAY-81-8973 / BAY-W-6240 / BAY81-8973
- Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Unlock Additional DataAdvate Powder, for solution 500 unit Intravenous Shire Pharma Canada Ulc 2012-03-05 Not applicable Canada 
Advate Injection, powder, for solution 1000 IU Intravenous Baxter Ag 2004-03-02 Not applicable EU 
Advate Powder, for solution 3000 unit Intravenous Shire Pharma Canada Ulc Not applicable Not applicable Canada Advate Injection, powder, for solution 250 IU Intravenous Baxter Ag 2004-03-02 Not applicable EU Advate Powder, for solution 500 unit Intravenous Baxter Healthcare Corporation 2006-10-06 2013-10-08 Canada Advate Injection, powder, for solution 500 IU Intravenous Baxter Ag 2004-03-02 Not applicable EU Advate Powder, for solution 2000 unit Intravenous Shire Pharma Canada Ulc Not applicable Not applicable Canada Advate Powder, for solution 250 unit Intravenous Shire Pharma Canada Ulc 2012-01-16 Not applicable Canada Advate Powder, for solution 3000 unit Intravenous Shire Pharma Canada Ulc 2010-01-05 Not applicable Canada Advate Injection, powder, for solution 250 IU Intravenous Baxter Ag 2004-03-02 Not applicable EU Additional Data Available- Application NumberApplication Number
A unique ID assigned by the FDA when a product is submitted for approval by the labeller.
Learn more - Product CodeProduct Code
A governmentally-recognized ID which uniquely identifies the product within its regulatory market.
Learn more
- International/Other Brands
- Bioclate / Helixate / Hyate:C / Koate-HP / Kogenate / Monarc-M / ReFacto
- Categories
- UNII
- P89DR4NY54
- CAS number
- 139076-62-3
Pharmacology
- Indication
For the treatment of hemophilia A, von Willebrand disease and Factor XIII deficiency.
- Associated Conditions
- Pharmacodynamics
Antihemophilic Factor binds factor IXa along with calcium and phospholipid, This complex converts factor X to factor Xa to facilitate 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).
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
- Not Available
- Volume of distribution
- Not Available
- Protein binding
- Not Available
- Metabolism
- Not Available
- Route of elimination
- Not Available
- Half life
8.4-19.3 hrs
- Clearance
- 4.1 mL/h•kg [Previously treated pediatric patients]
- Toxicity
- Not Available
- Affected organisms
- Humans and other mammals
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Unlock Additional Data
Additional Data Available
Adverse Effects
Comprehensive structured data on known drug adverse effects with statistical prevalence. MedDRA and ICD10 ids are provided for adverse effect conditions and symptoms.
Learn more Additional Data Available
Contraindications
Structured data covering drug contraindications. Each contraindication describes a scenario in which the drug is not to be used. Includes restrictions on co-administration, contraindicated populations, and more.
Learn more Additional Data Available
Blackbox Warnings
Structured data representing warnings from the black box section of drug labels. These warnings cover important and dangerous risks, contraindications, or adverse effects.
Learn moreInteractions
- Drug Interactions
- 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 Unlock Additional Data(R)-warfarin The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with (R)-warfarin. (S)-Warfarin The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with (S)-Warfarin. 4-hydroxycoumarin The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with 4-hydroxycoumarin. Abciximab The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with Abciximab. Acenocoumarol The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with Acenocoumarol. Acetylsalicylic acid The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with Acetylsalicylic acid. Alpha-1-proteinase inhibitor Alpha-1-proteinase inhibitor may increase the thrombogenic activities of Antihemophilic factor, human recombinant. Alteplase The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with Alteplase. Amediplase The therapeutic efficacy of Antihemophilic factor, human recombinant can be decreased when used in combination with Amediplase. Aminocaproic acid The risk or severity of adverse effects can be increased when Aminocaproic acid is combined with Antihemophilic factor, human recombinant. Additional Data Available- Extended DescriptionExtended Description
Extended description of the mechanism of action and particular properties of each drug interaction.
Learn more - Severity
- Evidence Level
- ActionAction
An effect category for each drug interaction. Know how this interaction affects the subject drug.
Learn more
- Food Interactions
- Not Available
References
- Synthesis Reference
James W. Bloom, "Warm ethanol method for preparation of low fibrinogen antihemophilic factor." U.S. Patent US4478825, issued June, 1955.
US4478825- 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. [PubMed:2157]
- External Links
- UniProt
- P00451
- Genbank
- M14113
- PubChem Substance
- 46506209
- RxNav
- 1300486
- ChEMBL
- CHEMBL2108175
- PharmGKB
- PA164750168
- RxList
- RxList Drug Page
- Drugs.com
- Drugs.com Drug Page
- Wikipedia
- Antihemophilic_Factor
- ATC Codes
- B02BD02 — Coagulation factor viii
- AHFS Codes
- 20:28.16 — Hemostatics
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 1 Completed Basic Science Hemophilia A 2 1 Completed Other Hemophilia A 1 1 Completed Treatment Congenital Hematological Disorder / Hemophilia A 1 1 Completed Treatment Hemophilia A 4 1 Not Yet Recruiting Treatment Hemophilia A 1 1, 2 Completed Other Hemophilia A 1 2 Completed Prevention Hemophilia A 1 2 Completed Treatment Hemophilia A 2 2 Terminated Treatment Hemophilia 1 2 Terminated Treatment Hemophilia A 1 2, 3 Completed Prevention Hemophilia A 1 2, 3 Completed Treatment Hemophilia A 4 3 Active Not Recruiting Treatment Hemophilia A 1 3 Completed Treatment Bone Diseases / Hemophilia 1 3 Completed Treatment Disorders, Blood Coagulation / Hemophilia A 1 3 Completed Treatment Hemophilia 1 3 Completed Treatment Hemophilia A 5 3 Completed Treatment Severe Hemophilia A 1 3 Completed Treatment Von Willebrand's Disease 1 3 Recruiting Prevention Von Willebrand's Disease 2 3 Recruiting Treatment Von Willebrand's Disease 1 3 Suspended Treatment Hemophilia A 1 3 Terminated Prevention Hemophilia A 1 4 Completed Basic Science Hemophilia A 1 4 Completed Prevention Hemophilia A 1 4 Completed Treatment Hematologic Diseases / Hemophilia A 1 4 Completed Treatment Hemophilia A 8 4 Completed Treatment Severe Hemophilia A 1 4 Recruiting Other Hemophilia A 1 4 Terminated Supportive Care Hemophilia A 1 4 Unknown Status Diagnostic Severe Haemophilia A 1 4 Withdrawn Treatment Hemophilia A 1 Not Available Active Not Recruiting Not Available Hemophilia 1 Not Available Active Not Recruiting Prevention Severe Hemophilia A 1 Not Available Completed Not Available Acquired Hemophilia A 1 Not Available Completed Not Available Congenital Factor VIII (FVIII) Deficiency / Hemophilia A 1 Not Available Completed Not Available Disorders, Blood Coagulation / Hemophilia A 1 Not Available Completed Not Available Hemophilia A 12 Not Available Completed Not Available Hemophilia A / Hemophilia B 1 Not Available Completed Treatment Hemophilia A 1 Not Available Recruiting Not Available Acquired Hemophilia A 1 Not Available Recruiting Not Available Factor VIII Deficiency / Hemophilia / Hemophilia A 1 Not Available Recruiting Not Available Hemophilia A 4 Not Available Recruiting Not Available Hemophilia A, Congenital 1 Not Available Terminated Not Available Hemophilia A / Hemophilia B 1 Not Available Unknown Status Treatment Hemophilia A 2
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Baxter International Inc.
- Bayer Healthcare
- CSL Behring LLC
- GlaxoSmithKline Inc.
- Grifols SA
- Ipsen Pharmaceuticals Inc.
- Octapharma USA
- Talecris Biotherapeutics
- Wyeth Pharmaceuticals
- Dosage forms
Form Route Strength Injection, powder, for solution Intravenous 1000 IU Injection, powder, for solution Intravenous 1500 IU Injection, powder, for solution Intravenous 2000 IU Injection, powder, for solution Intravenous 250 IU Injection, powder, for solution Intravenous 3000 IU Injection, powder, for solution Intravenous 500 IU Kit Intravenous 125 [iU]/1mL Kit Intravenous 200 [iU]/1mL Kit Intravenous 250 [iU]/1mL Kit Intravenous 300 [iU]/1mL Kit Intravenous 400 [iU]/1mL Kit Intravenous 500 [iU]/1mL Kit Intravenous 600 [iU]/1mL Kit Intravenous 750 [iU]/1mL Kit Intravenous 800 [iU]/1mL Powder, for solution Intravenous 1500 unit Powder, for solution Intravenous 3000 unit Kit Intravenous 1000 [iU]/5mL Kit Intravenous 1000 [iU]/2mL Kit Intravenous 1500 [iU]/2mL Kit Intravenous 1500 [iU]/5mL Kit Intravenous 250 [iU]/5mL Kit Intravenous 250 [iU]/2mL Kit Intravenous 500 [iU]/5mL Kit Intravenous 500 [iU]/2mL Kit Intravenous 750 [iU]/5mL Kit Intravenous 750 [iU]/2mL Kit Intravenous 1000 [iU]/2.5mL Kit Intravenous 2000 [iU]/5mL Kit Intravenous 250 [iU]/2.5mL Kit Intravenous 3000 [iU]/5mL Kit Intravenous 500 [iU]/2.5mL Powder, for solution Intravenous 1000 unit Powder, for solution Intravenous 2000 unit Powder, for solution Intravenous 250 unit Powder, for solution Intravenous 500 unit Kit; powder, for solution Intravenous 1000 unit Kit; powder, for solution Intravenous 2000 unit Kit; powder, for solution Intravenous 250 unit Kit; powder, for solution Intravenous 3000 unit Kit; powder, for solution Intravenous 500 unit Kit Intravenous 375 [iU]/1mL Kit Intravenous 62.5 [iU]/1mL Kit Intravenous 100 [iU]/1mL Kit Intravenous 25 [iU]/1mL Kit Intravenous 50 [iU]/1mL Powder, for solution Intravenous - Prices
Unit description Cost Unit Advate 1201-1800 unit vial 1.68USD vial Advate 1801-2400 unit vial 1.68USD vial Advate 200-400 unit vial 1.68USD vial Advate 2400-3600 unit vial 1.68USD vial Advate 401-800 unit vial 1.68USD vial Advate 801-1200 unit vial 1.68USD vial Kogenate fs 1000 unit vial 1.68USD vial Kogenate fs 250 unit vial 1.68USD vial Kogenate fs 3000 unit vial 1.68USD vial Kogenate fs 500 unit vial 1.68USD vial Xyntha 1000 unit kit 1.66USD kit Xyntha 2000 unit kit 1.66USD kit Xyntha 250 unit kit 1.66USD kit Xyntha 500 unit kit 1.66USD kit Helixate fs 1000 unit vial 1.56USD vial Helixate fs 250 unit vial 1.56USD vial Helixate fs 3000 unit vial 1.56USD vial Helixate fs 500 unit vial 1.56USD vial Wilate 450-450 unit kit 1.38USD kit Wilate 900-900 unit kit 1.38USD kit Hemofil m 1701-2000 unit vial 1.34USD vial Hemofil m 220-400 unit vial 1.34USD vial Hemofil m 401-800 unit vial 1.34USD vial Hemofil m 801-1700 unit vial 1.34USD vial Koate-dvi 1000 unit kit 1.31USD kit Koate-dvi 250 unit kit 1.31USD kit Koate-dvi 500 unit kit 1.31USD kit Refacto 1000 unit vial 1.31USD vial Refacto 2000 unit vial 1.31USD vial Refacto 250 unit vial 1.31USD vial Refacto 500 unit vial 1.31USD vial Alphanate 1000-1500 unit vial 1.2USD vial Alphanate 250-500 unit vial 1.2USD vial Humate-p 1000 unit kit 1.2USD kit Humate-p 1200 unit kit 1.2USD kit Humate-p 2000 unit kit 1.2USD kit Humate-p 2400 unit kit 1.2USD kit Humate-p 500 unit kit 1.2USD kit Humate-p 600 unit kit 1.2USD kit Monoclate-p 1000 unit kit 1.01USD kit Monoclate-p 1500 unit kit 1.01USD kit Monoclate-p 250 unit kit 1.01USD kit Monoclate-p 500ahfu kit 1.01USD kit DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.- Patents
Patent Number Pediatric Extension Approved Expires (estimated) Unlock Additional DataCA2124690 No 2007-09-11 2013-10-01 Canada CA1339477 No 1997-09-23 2014-09-23 Canada Additional Data Available- Filed On
Properties
- State
- Solid
- Experimental Properties
Property Value Source hydrophobicity -0.533 Not Available isoelectric point 6.97 Not Available
Taxonomy
- 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
Targets
- 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. [PubMed:13801371]
- LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF STUART FACTOR (FACTOR X) BY ACTIVATED ANTIHEMOPHILIC FACTOR (ACTIVATED FACTOR 8). Biochemistry. 1965 Jan;4:113-20. [PubMed:14285227]
- 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. [PubMed:236567]
- 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. [PubMed:6436416]
- 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. [PubMed:11891806]
- 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. [PubMed:1119107]
- 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. [PubMed:2994716]
- LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF ANTIHEMOPHILIC FACTOR (FACTOR 8) BY ACTIVATED CHRISTMAS FACTOR (ACTIVATED FACTOR9 9). Biochemistry. 1964 Nov;3:1720-5. [PubMed:14240634]
- 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. [PubMed:932529]
- 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. [PubMed:6422634]
- 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. [PubMed:10938981]
- 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. [PubMed:11858481]
- 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. [PubMed:14750934]
- 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. [PubMed:2128855]
- 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. [PubMed:2942172]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:11574539]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:15946216]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:9607108]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:9525969]
- 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. [PubMed:17899080]
- 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. [PubMed:9607108]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:9525969]
- 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. [PubMed:15213841]
- 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. [PubMed:17899080]
- 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. [PubMed:9607108]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:14629470]
- 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. [PubMed:14726380]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:21391865]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:15886209]
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. [PubMed:10688826]
- Ratnoff OD, Lewis JH: Heckathorn's disease: variable functional dificiency of antihemophilic factor (factor VIII). Blood. 1975 Aug;46(2):161-73. [PubMed:1139038]
- 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. [PubMed:12463731]
- 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. [PubMed:2402772]
- 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. [PubMed:3099625]
- 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. [PubMed:17139284]
- 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. [PubMed:17016423]
- 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. [PubMed:21054189]
Drug created on June 13, 2005 07:24 / Updated on April 09, 2020 00:00
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