IDPharmacologyInteractionsReferencesTrialsEconomicsPropertiesTaxonomy
Targets (11)Enzymes (2)
Targets (11)Enzymes (2)Biointeractions (7)

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Identification
NameAntihemophilic factor, human recombinant
Accession NumberDB00025  (BTD00029, BIOD00029, DB13162)
TypeBiotech
GroupsApproved, Investigational
Description

Human recombinant antihemophilic factor (AHF) or Factor VIII, 2332 residues, glycosylated, produced by CHO cells

Protein structureDb00025
Related Articles
Protein chemical formulaC11794H18314N3220O3553S83
Protein average weight264725.5 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), Plasma/Albumin-Free Method
Antihemophilic factor recombinant
Antihemophilic factor, recombinant
Antihemophilic factor,recombinant
Factor VIII (rDNA)
Factor VIII (Recombinant)
Factor VIII recombin
Factor VIII, recombinant
Human Factor VIII (Recombinant)
Human factor VIII recombinant
rAHF
Recombinant antihemophilic factor VIII
External IDs Not Available
Product Ingredients
IngredientUNIICASInChI KeyDetails
Lonoctocog alfaVQ723R7O8R 1388129-63-2Not applicableDetails
Moroctocog alfa113E3Z3CJJ 284036-24-4Not applicableDetails
Octocog alfaNot Available139076-62-3Not applicableDetails
Approved Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing End
AdvateInjection, powder, for solution2000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution250 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution250 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution3000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution250 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution3000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution250 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution2000 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AdvateInjection, powder, for solution1500 IUIntravenousBaxter Ag2004-03-02Not applicableEu
AfstylaKit; Powder, for solution2000 unitIntravenousCsl BehringNot applicableNot applicableCanada
AfstylaKit; Powder, for solution250 unitIntravenousCsl BehringNot applicableNot applicableCanada
AfstylaKit; Powder, for solution1500 unitIntravenousCsl BehringNot applicableNot applicableCanada
AfstylaKit; Powder, for solution2500 unitIntravenousCsl BehringNot applicableNot applicableCanada
AfstylaKit; Powder, for solution500 unitIntravenousCsl BehringNot applicableNot applicableCanada
AfstylaKit; Powder, for solution1000 unitIntravenousCsl BehringNot applicableNot applicableCanada
AfstylaKit; Powder, for solution3000 unitIntravenousCsl BehringNot applicableNot applicableCanada
AntiveninKitMerck Sharp & Dohme Limited2014-12-01Not applicableUs
Hemofil MKitBaxalta Canada Corporation1988-02-23Not applicableUs
Hemofil MKitBaxalta Canada Corporation1988-02-23Not applicableUs
Hemofil MKitBaxalta Canada Corporation1988-02-23Not applicableUs
Hemofil MKitBaxalta Canada Corporation1988-02-23Not applicableUs
Monoclate-PKitCsl Behring1990-05-30Not applicableUs
Monoclate-PKitCsl Behring1990-05-30Not applicableUs
Monoclate-PKitCsl Behring2004-03-04Not applicableUs
Monoclate-PKitCsl Behring1990-05-30Not applicableUs
RecombinateKitBaxter Laboratories1992-12-10Not applicableUs
RecombinateKitBaxter Laboratories2010-03-10Not applicableUs
RecombinateKitBaxter Laboratories2010-03-10Not applicableUs
RecombinateKitBaxter Laboratories2010-02-08Not applicableUs
RecombinateKitBaxter Laboratories1992-12-10Not applicableUs
RecombinateKitBaxter Laboratories2010-02-08Not applicableUs
RecombinateKitBaxter Laboratories1992-12-10Not applicableUs
RecombinateKitBaxter Laboratories2010-02-08Not applicableUs
RefactoPowder, for solution1000 unitIntravenousWyeth Ltd.2003-02-112009-01-23Canada
Refacto AFInjection, powder, for solution500 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution250 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution3000 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution2000 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution1000 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution500 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution250 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution2000 IUIntravenousPfizer1999-04-13Not applicableEu
Refacto AFInjection, powder, for solution1000 IUIntravenousPfizer1999-04-13Not applicableEu
XynthaKit; Powder, for solution1000 unitIntravenousPfizer2009-01-23Not applicableCanada
XynthaKit; Powder, for solution250 unitIntravenousPfizer2009-01-23Not applicableCanada
XynthaKit; Powder, for solution2000 unitIntravenousPfizer2009-01-23Not applicableCanada
XynthaKit; Powder, for solution500 unitIntravenousPfizer2009-01-23Not applicableCanada
Xyntha SolofusePowder, for solution2000 unitIntravenousPfizer2012-05-08Not applicableCanada
Xyntha SolofusePowder, for solution250 unitIntravenousPfizerNot applicableNot applicableCanada
Xyntha SolofusePowder, for solution3000 unitIntravenousPfizer2012-05-08Not applicableCanada
Xyntha SolofusePowder, for solution500 unitIntravenousPfizerNot applicableNot applicableCanada
Xyntha SolofusePowder, for solution1000 unitIntravenousPfizer2012-04-13Not applicableCanada
Approved Generic Prescription ProductsNot Available
Approved Over the Counter ProductsNot Available
Unapproved/Other Products Not Available
International Brands
NameCompany
BioclateNot Available
HelixateNot Available
Hyate:CNot Available
Koate-HPNot Available
KogenateNot Available
Monarc-MNot Available
ReFactoNot Available
Brand mixtures
NameLabellerIngredients
AdvateBaxter Laboratories
  1. Antihemophilic factor, human recombinant
Helixate FSCsl Behring
  1. Antihemophilic factor, human recombinant
Wilate - Von Willebrand Factor/coagulation Factor Viii Complex (human)Octapharma Pharmazeutika Produktionsgesellschaft M.B.H.
  1. Antihemophilic factor, human recombinant
  2. Von Willebrand Factor Human
Categories
UNIIP89DR4NY54
CAS number139076-62-3
Pharmacology
Indication

For the treatment of hemophilia A, von Willebrand disease and Factor XIII deficiency.

Structured Indications
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).

TargetKindPharmacological actionActionsOrganismUniProt ID
Coagulation factor XProteinyes
activator
HumanP00742 details
Coagulation factor IXProteinyes
cofactor
HumanP00740 details
von Willebrand factorProteinyes
binder
HumanP04275 details
Phytanoyl-CoA dioxygenase, peroxisomalProteinunknown
antagonist
HumanO14832 details
Asialoglycoprotein receptor 2Proteinunknown
binder
HumanP07307 details
78 kDa glucose-regulated proteinProteinunknown
chaperone
HumanP11021 details
CalreticulinProteinunknown
chaperone
HumanP27797 details
CalnexinProteinunknown
chaperone
HumanP27824 details
Protein ERGIC-53Proteinunknown
chaperone
HumanP49257 details
Prolow-density lipoprotein receptor-related protein 1Proteinunknown
modulator
HumanQ07954 details
Multiple coagulation factor deficiency protein 2Proteinunknown
modulator
HumanQ8NI22 details
Related Articles
AbsorptionNot Available
Volume of distributionNot Available
Protein bindingNot Available
MetabolismNot Available
Route of eliminationNot Available
Half life

8.4-19.3 hrs

Clearance
  • 4.1 mL/h•kg [Previously treated pediatric patients]
ToxicityNot Available
Affected organisms
  • Humans and other mammals
PathwaysNot Available
Pharmacogenomic Effects/ADRs Not Available
Interactions
Drug Interactions No interactions found.
Food InteractionsNot 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
  1. 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
ATC CodesB02BD02 — Coagulation factor viii
AHFS Codes
  • 20:28.16
PDB Entries
FDA labelNot Available
MSDSNot Available
Clinical Trials
Clinical Trials
PhaseStatusPurposeConditionsCount
1CompletedNot AvailableHemophilia A2
1CompletedBasic ScienceHemophilia A1
1CompletedTreatmentCongenital Hematological Disorder / Hemophilia A1
1CompletedTreatmentHemophilia A4
1Not Yet RecruitingTreatmentHemophilia A1
2CompletedTreatmentHemophilia A1
2RecruitingTreatmentHemophilia1
2, 3CompletedPreventionHemophilia A1
2, 3CompletedTreatmentHemophilia A1
3Active Not RecruitingTreatmentHemophilia A1
3CompletedTreatmentDisorders, Blood Coagulation / Hemophilia A1
3CompletedTreatmentHemophilia1
3CompletedTreatmentHemophilia A6
3CompletedTreatmentSevere Hemophilia A1
3CompletedTreatmentVon Willebrand 's disease Type 11
3Not Yet RecruitingPreventionVon Willebrand 's disease Type 11
3Not Yet RecruitingTreatmentVon Willebrand 's disease Type 11
3RecruitingTreatmentBone Diseases / Hemophilia1
3RecruitingTreatmentHemophilia A1
3TerminatedPreventionHemophilia A1
3TerminatedTreatmentHemophilia A1
4CompletedBasic ScienceHemophilia A1
4CompletedPreventionHemophilia A1
4CompletedTreatmentHematologic Diseases / Hemophilia A1
4CompletedTreatmentHemophilia A7
4TerminatedSupportive CareHemophilia A1
4TerminatedTreatmentHemophilia A1
4Unknown StatusDiagnosticSevere Haemophilia A1
Not AvailableActive Not RecruitingNot AvailableHemophilia A1
Not AvailableActive Not RecruitingPreventionSevere Hemophilia A1
Not AvailableCompletedNot AvailableCongenital Factor VIII (FVIII) Deficiency / Hemophilia A1
Not AvailableCompletedNot AvailableDisorders, Blood Coagulation / Hemophilia A1
Not AvailableCompletedNot AvailableHemophilia A9
Not AvailableCompletedNot AvailableHemophilia A / Hereditary factor IX deficiency1
Not AvailableCompletedTreatmentHemophilia A1
Not AvailableNot Yet RecruitingNot AvailableFactor VIII Deficiency / Hemophilia / Hemophilia A1
Not AvailableRecruitingNot AvailableAcquired Hemophilia A1
Not AvailableRecruitingNot AvailableHemophilia1
Not AvailableRecruitingNot AvailableHemophilia A3
Not AvailableRecruitingNot AvailableHemophilia A, Congenital1
Not AvailableUnknown StatusTreatmentHemophilia A2
Pharmacoeconomics
ManufacturersNot Available
Packagers
Dosage forms
FormRouteStrength
Injection, powder, for solutionIntravenous1500 IU
Kit
Kit; powder, for solutionIntravenous1500 unit
Kit; powder, for solutionIntravenous2500 unit
Kit; powder, for solutionIntravenous3000 unit
Kit
Injection, powder, for solutionIntravenous1000 IU
Injection, powder, for solutionIntravenous2000 IU
Injection, powder, for solutionIntravenous250 IU
Injection, powder, for solutionIntravenous3000 IU
Injection, powder, for solutionIntravenous500 IU
Powder, for solutionIntravenous
Kit; powder, for solutionIntravenous1000 unit
Kit; powder, for solutionIntravenous2000 unit
Kit; powder, for solutionIntravenous250 unit
Kit; powder, for solutionIntravenous500 unit
Powder, for solutionIntravenous1000 unit
Powder, for solutionIntravenous2000 unit
Powder, for solutionIntravenous250 unit
Powder, for solutionIntravenous3000 unit
Powder, for solutionIntravenous500 unit
Prices
Unit descriptionCostUnit
Advate 1201-1800 unit vial1.68USD vial
Advate 1801-2400 unit vial1.68USD vial
Advate 200-400 unit vial1.68USD vial
Advate 2400-3600 unit vial1.68USD vial
Advate 401-800 unit vial1.68USD vial
Advate 801-1200 unit vial1.68USD vial
Kogenate fs 1000 unit vial1.68USD vial
Kogenate fs 250 unit vial1.68USD vial
Kogenate fs 3000 unit vial1.68USD vial
Kogenate fs 500 unit vial1.68USD vial
Xyntha 1000 unit kit1.66USD kit
Xyntha 2000 unit kit1.66USD kit
Xyntha 250 unit kit1.66USD kit
Xyntha 500 unit kit1.66USD kit
Helixate fs 1000 unit vial1.56USD vial
Helixate fs 250 unit vial1.56USD vial
Helixate fs 3000 unit vial1.56USD vial
Helixate fs 500 unit vial1.56USD vial
Wilate 450-450 unit kit1.38USD kit
Wilate 900-900 unit kit1.38USD kit
Hemofil m 1701-2000 unit vial1.34USD vial
Hemofil m 220-400 unit vial1.34USD vial
Hemofil m 401-800 unit vial1.34USD vial
Hemofil m 801-1700 unit vial1.34USD vial
Koate-dvi 1000 unit kit1.31USD kit
Koate-dvi 250 unit kit1.31USD kit
Koate-dvi 500 unit kit1.31USD kit
Refacto 1000 unit vial1.31USD vial
Refacto 2000 unit vial1.31USD vial
Refacto 250 unit vial1.31USD vial
Refacto 500 unit vial1.31USD vial
Alphanate 1000-1500 unit vial1.2USD vial
Alphanate 250-500 unit vial1.2USD vial
Humate-p 1000 unit kit1.2USD kit
Humate-p 1200 unit kit1.2USD kit
Humate-p 2000 unit kit1.2USD kit
Humate-p 2400 unit kit1.2USD kit
Humate-p 500 unit kit1.2USD kit
Humate-p 600 unit kit1.2USD kit
Monoclate-p 1000 unit kit1.01USD kit
Monoclate-p 1500 unit kit1.01USD kit
Monoclate-p 250 unit kit1.01USD kit
Monoclate-p 500ahfu kit1.01USD kit
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
Patent NumberPediatric ExtensionApprovedExpires (estimated)
CA1339477 No1997-09-232014-09-23Canada
CA2124690 No2007-09-112013-10-01Canada
Properties
StateSolid
Experimental Properties
PropertyValueSource
hydrophobicity-0.533Not Available
isoelectric point6.97Not Available
Taxonomy
DescriptionNot Available
KingdomOrganic Compounds
Super ClassOrganic Acids
ClassCarboxylic Acids and Derivatives
Sub ClassAmino Acids, Peptides, and Analogues
Direct ParentPeptides
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkNot Available
External DescriptorsNot Available

Targets

Details
1. Coagulation factor X
Kind
Protein
Organism
Human
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
Molecular Weight:
54731.255 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
Details
2. Coagulation factor IX
Kind
Protein
Organism
Human
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, phospholipids, and factor VIIIa.
Gene Name:
F9
Uniprot ID:
P00740
Molecular Weight:
51778.11 Da
References
  1. Hule V: [Factor IX inhibitor (antihemophilic factor B, PTC) in a woman]. Vnitr Lek. 1975 Mar;21(3):274-7. [PubMed:1119107 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
Details
3. von Willebrand factor
Kind
Protein
Organism
Human
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-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clea...
Gene Name:
VWF
Uniprot ID:
P04275
Molecular Weight:
309261.83 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
Details
4. Phytanoyl-CoA dioxygenase, peroxisomal
Kind
Protein
Organism
Human
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
Molecular Weight:
38538.065 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
Details
5. Asialoglycoprotein receptor 2
Kind
Protein
Organism
Human
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-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor...
Gene Name:
ASGR2
Uniprot ID:
P07307
Molecular Weight:
35092.04 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
Details
6. 78 kDa glucose-regulated protein
Kind
Protein
Organism
Human
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 proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.
Gene Name:
HSPA5
Uniprot ID:
P11021
Molecular Weight:
72332.425 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
Details
7. Calreticulin
Kind
Protein
Organism
Human
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 with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression ...
Gene Name:
CALR
Uniprot ID:
P27797
Molecular Weight:
48141.2 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
Details
8. Calnexin
Kind
Protein
Organism
Human
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 unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes...
Gene Name:
CANX
Uniprot ID:
P27824
Molecular Weight:
67567.695 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
  6. 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 ]
Details
9. Protein ERGIC-53
Kind
Protein
Organism
Human
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 both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.
Gene Name:
LMAN1
Uniprot ID:
P49257
Molecular Weight:
57548.665 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
Details
10. Prolow-density lipoprotein receptor-related protein 1
Kind
Protein
Organism
Human
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 of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellula...
Gene Name:
LRP1
Uniprot ID:
Q07954
Molecular Weight:
504601.695 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
Details
11. Multiple coagulation factor deficiency protein 2
Kind
Protein
Organism
Human
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
Molecular Weight:
16390.175 Da
References
  1. 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 ]
  2. 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 ]
  3. 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

Details
1. Prothrombin
Kind
Protein
Organism
Human
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 homeostasis, inflammation and wound healing.
Gene Name:
F2
Uniprot ID:
P00734
Molecular Weight:
70036.295 Da
References
  1. 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 ]
  2. Ratnoff OD, Lewis JH: Heckathorn's disease: variable functional dificiency of antihemophilic factor (factor VIII). Blood. 1975 Aug;46(2):161-73. [PubMed:1139038 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
Details
2. Vitamin K-dependent protein C
Kind
Protein
Organism
Human
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 a protective effect on the endothelial cell barrier function (PubMed:25651845).
Gene Name:
PROC
Uniprot ID:
P04070
Molecular Weight:
52070.82 Da
References
  1. 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 ]
  2. 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 ]
  3. 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 June 22, 2017 09:31