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References

Trials

Economics

Properties

Spectra

Taxonomy

Antihemophilic factor, human recombinant

Targets (11)Enzymes (2)

Identification

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	Labeller	Marketing Start	Marketing End
Advate	Kit	125 [iU]/1mL	Baxalta US Inc.	2011-12-15	Not applicable
Advate	Kit	250 [iU]/1mL	Baxalta US Inc.	2011-12-15	Not applicable
Advate	Kit	500 [iU]/1mL	Baxalta US Inc.	2011-12-15	Not applicable
Advate	Kit	750 [iU]/1mL	Baxalta US Inc.	2011-12-15	Not applicable
Advate	Kit	400 [iU]/1mL	Baxalta US Inc.	2006-04-12	Not applicable
Advate	Kit	600 [iU]/1mL	Baxalta US Inc.	2007-07-03	Not applicable
Advate	Kit	400 [iU]/1mL	Baxalta Canada Corporation	2006-04-12	Not applicable
Advate	Kit	800 [iU]/1mL	Baxalta US Inc.	2012-07-12	Not applicable
Advate	Kit	600 [iU]/1mL	Baxalta Canada Corporation	2007-07-03	Not applicable
Advate	Kit	800 [iU]/1mL	Baxalta Canada Corporation	2012-07-12	Not applicable

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	activator	Humans
ACoagulation factor IX	cofactor	Humans
Avon Willebrand factor	binder	Humans
UPhytanoyl-CoA dioxygenase, peroxisomal	antagonist	Humans
UAsialoglycoprotein receptor 2	binder	Humans
U78 kDa glucose-regulated protein	chaperone	Humans
UCalreticulin	chaperone	Humans
UCalnexin	chaperone	Humans
UProtein ERGIC-53	chaperone	Humans
UProlow-density lipoprotein receptor-related protein 1	modulator	Humans
UMultiple coagulation factor deficiency protein 2	modulator	Humans

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

Interactions

Drug Interactions

Drug	Interaction
(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.

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
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	Not Available	Hemophilia A	1
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
2	Completed	Treatment	Hemophilia A	1
2	Recruiting	Treatment	Hemophilia	1
2, 3	Completed	Prevention	Hemophilia A	1
2, 3	Completed	Treatment	Hemophilia A	1
3	Completed	Treatment	Disorders, Blood Coagulation / Hemophilia A	1
3	Completed	Treatment	Hemophilia	1
3	Completed	Treatment	Hemophilia A	7
3	Completed	Treatment	Severe Hemophilia A	1
3	Completed	Treatment	Von Willebrand 's disease Type 1	1
3	Not Yet Recruiting	Prevention	Von Willebrand 's disease Type 1	1
3	Not Yet Recruiting	Treatment	Severe Hemophilia A	1
3	Recruiting	Prevention	Von Willebrand 's disease Type 1	1
3	Recruiting	Treatment	Bone Diseases / Hemophilia	1
3	Recruiting	Treatment	Hemophilia A	1
3	Recruiting	Treatment	Von Willebrand 's disease Type 1	1
3	Terminated	Prevention	Hemophilia A	1
3	Terminated	Treatment	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	6
4	Recruiting	Treatment	Community Acquired Pneumonia (CAP)	1
4	Terminated	Supportive Care	Hemophilia A	1
4	Terminated	Treatment	Hemophilia A	1
4	Unknown Status	Diagnostic	Severe Haemophilia A	1
4	Withdrawn	Treatment	Hemophilia A	1
Not Available	Active Not Recruiting	Prevention	Severe 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	11
Not Available	Completed	Not Available	Hemophilia A / Hereditary factor IX deficiency	1
Not Available	Completed	Treatment	Hemophilia A	1
Not Available	Not Yet Recruiting	Not Available	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	1
Not Available	Recruiting	Not Available	Hemophilia A	4
Not Available	Recruiting	Not Available	Hemophilia A, Congenital	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		125 [iU]/1mL
Kit		200 [iU]/1mL
Kit		250 [iU]/1mL
Kit		300 [iU]/1mL
Kit		400 [iU]/1mL
Kit		500 [iU]/1mL
Kit		600 [iU]/1mL
Kit		750 [iU]/1mL
Kit		800 [iU]/1mL
Powder, for solution	Intravenous	1500 unit
Powder, for solution	Intravenous	3000 unit
Kit		1000 [iU]/2mL
Kit		1000 [iU]/5mL
Kit		1500 [iU]/5mL
Kit		1500 [iU]/2mL
Kit		250 [iU]/2mL
Kit		250 [iU]/5mL
Kit		500 [iU]/5mL
Kit		500 [iU]/2mL
Kit		750 [iU]/2mL
Kit		750 [iU]/5mL
Kit		1000 [iU]/2.5mL
Kit		2000 [iU]/5mL
Kit		250 [iU]/2.5mL
Kit		3000 [iU]/5mL
Kit		500 [iU]/2.5mL
Powder, for solution	Intravenous	2000 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		375 [iU]/1mL
Kit		62.5 [iU]/1mL
Kit		100 [iU]/1mL
Kit		25 [iU]/1mL
Kit		50 [iU]/1mL
Powder, for solution	Intravenous	1000 unit
Powder, for solution	Intravenous	250 unit
Powder, for solution	Intravenous	500 unit

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)
CA2124690	No	2007-09-11	2013-10-01
CA1339477	No	1997-09-23	2014-09-23

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

Details1. Coagulation factor X

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]

Details2. Coagulation factor IX

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]

Details3. von Willebrand factor

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]

Details4. Phytanoyl-CoA dioxygenase, peroxisomal

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]

Details5. Asialoglycoprotein receptor 2

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]

Details6. 78 kDa glucose-regulated protein

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]

Details7. Calreticulin

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]

Details8. Calnexin

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]

Details9. Protein ERGIC-53

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]

Details10. Prolow-density lipoprotein receptor-related protein 1

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]

Details11. Multiple coagulation factor deficiency protein 2

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

Details1. Prothrombin

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]

Details2. Vitamin K-dependent protein C

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 21, 2019 05:00