Coagulation Factor IX (Recombinant)

Identification

Summary

Coagulation Factor IX (Recombinant) is a form of recombinant human coagulation Factor IX used to treat hemophilia B.

Brand Names
Benefix, Idelvion, Ixinity, Rixubis
Generic Name
Coagulation Factor IX (Recombinant)
DrugBank Accession Number
DB00100
Background

Recombinant Coagulation Factor IX is a purified Factor IX glycoprotein produced by recombinant DNA technology. It has a primary amino acid sequence that is identical to the Ala148 allelic form of human factor IX, and has structural and functional characteristics similar to those of endogenous factor IX. It is not derived from human blood (unlike human Factor IX complex), and is instead produced by a genetically engineered Chinese hamster ovary (CHO) cell line that secretes recombinant Factor IX into cell medium that is then processed and purified for use as a pharmaceutical agent.

Recombinant Factor IX is indicated for the control and prevention of bleeding episodes in adult and pediatric patients with congenital factor IX deficiency (Hemophilia B).

Type
Biotech
Groups
Approved, Investigational
Biologic Classification
Protein Based Therapies
Blood factors
Protein Structure
Protein Chemical Formula
C2041H3136N558O641S25
Protein Average Weight
46548.2 Da
Sequences
>DB00100 sequence
YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGG
SCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAEN
QKSCEPAVPFPCGRVSVSQTSKLTRAEAVFPDVDYVNSTEAETILDNITQSTQSFNDFTR
VVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEE
TEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFL
KFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDS
CQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Download FASTA Format
Synonyms
  • Coagulation factor IX (recombinant)
  • Coagulation factor IX recombinant human
  • Coagulation factor IX, recombinant
  • Factor IX (Recombinant)
  • nonacog alfa
  • nonacog gamma
  • Recombinant factor IX

Pharmacology

Indication

For treatment of hemophilia (Christmas disease).

Reduce drug development failure rates
Build, train, & validate machine-learning models
with evidence-based and structured datasets.
See how
Build, train, & validate predictive machine-learning models with structured datasets.
See how
Associated Conditions
Indication TypeIndicationCombined Product DetailsApproval LevelAge GroupPatient CharacteristicsDose Form
Prophylaxis ofBleeding••••••••••••••••••••••• •••••
Management ofBleeding••••••••••••••••••••••• •••••• ••••••••••••••••••• •••
Management ofHemophilia b••••••••••••••••••••••••••• •••
Management ofPerioperative bleeding caused by hemophilia b••••••••••••••••••••••• •••••• ••••••••••••••••••• •••
Contraindications & Blackbox Warnings
Prevent Adverse Drug Events Today
Tap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.
Learn more
Avoid life-threatening adverse drug events with our Clinical API
Learn more
Pharmacodynamics

Binds vitamin K and factor VIIIa. Cleaves the Arg-Ile bond in factor X to form active factor Xa. Plays a key role in blood coagulation and clotting. Injections of factor IX are used to treat hemophilia B, which is sometimes called Christmas disease. AlphaNine is injected to increase plasma levels of Factor IX and can temporarily correct this coagulation defect. The activated partial thromboplastin time (aPTT) is prolonged in people with hemophilia B. Treatment with factor IX concentrate may normalize the aPTT by temporarily replacing the factor IX. The administration of BeneFIX increases plasma levels of factor IX, and can temporarily correct the coagulation defect in these patients.

Mechanism of action

Coagulation Factor IX is an important protein in the process of hemostasis and normal blood clotting as it plays a key role within the coagulation cascade. It is located within the blood plasma as a zymogen, an antecedent to enzymatic function, in its inactivated state. Factor IX is dependent on the presence of Vitamin K, and is activated to a serine protease by the function of Coagulation Factor XIa. Factor XIa cleaves the peptide bond associated with protein activation in Factor IX, leaving Factor IX with two exposed chains, a light chain and a heavy chain. These two chains are held together by several disulfide bonds that reinforce the structure of Factor IX's activated form. After being activated, Factor IX forms a complex with calcium ions, membrane phospholipids and Coagulation Factor VIII to activate Coagulation Factor X. The activation of Factor X then performs a similarly integral step in the blood coagulation cascade. The ultimate result of phenotypically normal coagulation factors is the creation of platelets for normal blood clotting.

TargetActionsOrganism
ACoagulation factor X
activator
Humans
ACoagulation factor XI
ligand
Humans
ACoagulation factor VII
ligand
Humans
ACoagulation factor VIII
cofactor
Humans
UProthrombinNot AvailableHumans
UProlow-density lipoprotein receptor-related protein 1Not AvailableHumans
UVitamin K-dependent gamma-carboxylaseNot AvailableHumans
Absorption

Not Available

Volume of distribution

Not Available

Protein binding

Not Available

Metabolism
Not Available
Route of elimination

Not Available

Half-life

18.8 ± 5.4 hours

Clearance

8.62 ± 1.7

Adverse Effects
Improve decision support & research outcomes
With structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!
See the data
Improve decision support & research outcomes with our structured adverse effects data.
See a data sample
Toxicity

Not Available

Pathways
Not Available
Pharmacogenomic Effects/ADRs Browse all" title="About SNP Mediated Effects/ADRs" id="snp-actions-info" class="drug-info-popup" href="javascript:void(0);">
Not Available

Interactions

Drug Interactions Learn More" title="About Drug Interactions" id="structured-interactions-info" class="drug-info-popup" href="javascript:void(0);">
This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
DrugInteraction
AbciximabThe therapeutic efficacy of Coagulation Factor IX (Recombinant) can be decreased when used in combination with Abciximab.
AcenocoumarolThe therapeutic efficacy of Coagulation Factor IX (Recombinant) can be decreased when used in combination with Acenocoumarol.
Alpha-1-proteinase inhibitorAlpha-1-proteinase inhibitor may increase the thrombogenic activities of Coagulation Factor IX (Recombinant).
AlteplaseThe therapeutic efficacy of Coagulation Factor IX (Recombinant) can be decreased when used in combination with Alteplase.
Aminocaproic acidThe risk or severity of adverse effects can be increased when Aminocaproic acid is combined with Coagulation Factor IX (Recombinant).
Food Interactions
No interactions found.

Products

Drug product information from 10+ global regions
Our datasets provide approved product information including:
dosage, form, labeller, route of administration, and marketing period.
Access now
Access drug product information from over 10 global regions.
Access now
Brand Name Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
BenefixInjection, powder, for solution2000 IUIntravenousPfizer Europe Ma Eeig2021-01-27Not applicableEU flag
BenefixInjection, powder, for solution250 IUIntravenousPfizer Europe Ma Eeig2021-01-27Not applicableEU flag
BeneFIXPowder, for solution2000 unit / vialIntravenousPfizer Canada Ulc2008-07-12Not applicableCanada flag
BeneFIXPowder, for solution500 unit / vialIntravenousPfizer Canada Ulc2007-04-14Not applicableCanada flag
BenefixInjection, powder, for solution1500 IUIntravenousPfizer Europe Ma Eeig2021-01-27Not applicableEU flag
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
BeneFIXCoagulation Factor IX (Recombinant) (500 [iU]/5mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC1997-02-01Not applicableUS flag
BeneFIXCoagulation Factor IX (Recombinant) (500 [iU]/5mL) + Isopropyl alcohol (0.42 mL/1)KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals Inc., a subsidiary of Pfizer Inc.1997-02-012010-12-16US flag
BeneFIXCoagulation Factor IX (Recombinant) (3000 [iU]/5mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2012-02-01Not applicableUS flag
BeneFIXCoagulation Factor IX (Recombinant) (1000 [iU]/5mL) + Isopropyl alcohol (0.42 mL/1)KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals Inc., a subsidiary of Pfizer Inc.1997-02-012010-12-16US flag
BeneFIXCoagulation Factor IX (Recombinant) (2000 [iU]/5mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2007-07-06Not applicableUS flag

Categories

Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
Not Available
Kingdom
Organic Compounds
Super Class
Organic Acids
Class
Carboxylic Acids and Derivatives
Sub Class
Amino Acids, Peptides, and Analogues
Direct Parent
Peptides
Alternative Parents
Not Available
Substituents
Not Available
Molecular Framework
Not Available
External Descriptors
Not Available
Affected organisms
  • Humans and other mammals

Chemical Identifiers

UNII
382L14738L
CAS number
181054-95-5

References

Synthesis Reference

Volker Schellenberger, Joshua Silverman, Willem Stemmer, Chia-wei Wang, Benjamin Spink, Nathan Geething, Wayne To, "Coagulation factor IX compositions and methods of making and using same." U.S. Patent US20110046060, issued February 24, 2011.

US20110046060
General References
  1. BIGGS R, DOUGLAS AS, MACFARLANE RG, DACIE JV, PITNEY WR, MERSKEY: Christmas disease: a condition previously mistaken for haemophilia. Br Med J. 1952 Dec 27;2(4799):1378-82. [Article]
  2. Kurachi K, Davie EW: Isolation and characterization of a cDNA coding for human factor IX. Proc Natl Acad Sci U S A. 1982 Nov;79(21):6461-4. [Article]
  3. FDA Approved Drug Products: BeneFIX [coagulation factor IX (recombinant)] lyophilized powder for solution, for intravenous use [Link]
  4. DailyMed Label: IXINITY [coagulation factor IX (recombinant)] Lyophilized Powder for Solution for Intravenous Injection [Link]
UniProt
P00740
Genbank
K02402
KEGG Compound
C03101
PubChem Substance
46508858
RxNav
1300488
Therapeutic Targets Database
DAP000964
PharmGKB
PA164744952
RxList
RxList Drug Page
Drugs.com
Drugs.com Drug Page
Wikipedia
Factor_IX
FDA label
Download (18.9 MB)
MSDS
Download (125 KB)

Clinical Trials

Clinical Trials Learn More" title="About Clinical Trials" id="clinical-trials-info" class="drug-info-popup" href="javascript:void(0);">
PhaseStatusPurposeConditionsCount
4CompletedPreventionCoronavirus Disease 2019 (COVID‑19) / Hemophilia B1
4CompletedTreatmentHemophilia B3
3CompletedPreventionHemophilia B1
3CompletedTreatmentHemophilia B7
3CompletedTreatmentSevere Hemophilia B2

Pharmacoeconomics

Manufacturers
Not Available
Packagers
  • CSL Behring LLC
  • Grifols SA
  • Hospira Inc.
  • Wyeth Pharmaceuticals
Dosage Forms
FormRouteStrength
Injection, powder, for solutionIntravenous1500 IU
Injection, powder, for solutionIntravenous3000 IU
Injection, powder, lyophilized, for solution; kitIntravenous; Topical
Injection, solutionIntravenous1000 IU
Injection, solutionIntravenous250 IU
Injection, solutionIntravenous500 IU
KitIntravenous; Topical
Powder, for solutionIntravenous1000 unit / vial
Powder, for solutionIntravenous1500 unit / vial
Powder, for solutionIntravenous2000 unit / vial
Powder, for solutionIntravenous250 unit / vial
Powder, for solutionIntravenous3000 unit / vial
Powder, for solutionIntravenous500 unit / vial
Kit; liquid; powder, for solutionIntravenous
Injection, powder, for solutionIntravenous
Injection, solutionIntravenous2000 iu
Injection, powder, for solutionIntravenous275 IU/mL
Injection, powder, for solutionIntravenous550 IU/mL
Injection, powder, for solutionIntravenous69 IU/mL
Injection, powder, for solutionIntravenous500 IU
Injection, powder, for solutionIntravenous138 IU/mL
Injection, powder, for solutionIntravenous1000 IU
Injection, powder, for solutionIntravenous2000 IU
Injection, powder, lyophilized, for solutionIntravenous1000 IU
Kit; powder, for solutionIntravenous1000 IU/1
Kit; powder, for solutionIntravenous2000 IU/1
Kit; powder, for solutionIntravenous500 IU/1
Injection, powder, lyophilized, for solutionIntravenous600 IU
Injection, powder, lyophilized, for solution; kitIntravenous1500 [iU]/5mL
KitIntravenous1000 [iU]/5mL
KitIntravenous1500 [iU]/5mL
KitIntravenous2000 [iU]/5mL
KitIntravenous250 [iU]/5mL
KitIntravenous3000 [iU]/5mL
KitIntravenous500 [iU]/5mL
Injection, powder, lyophilized, for solutionIntravenous100000000 IU
Injection, powder, for solutionIntravenous250 IU
Injection, powder, lyophilized, for solutionIntravenous250 IU
Injection, powder, lyophilized, for solutionIntravenous500 IU
Injection, powder, lyophilized, for solution; kitIntravenous125 [iU]/1mL
Injection, powder, lyophilized, for solution; kitIntravenous250 [iU]/1mL
Injection, powder, lyophilized, for solution; kitIntravenous500 [iU]/1mL
Injection, powder, lyophilized, for solution; kitIntravenous750 [iU]/1mL
Injection, powder, lyophilized, for solution; kitIntravenous1000 [iU]/5mL
Injection, powder, lyophilized, for solution; kitIntravenous2000 [iU]/5mL
Injection, powder, lyophilized, for solution; kitIntravenous250 [iU]/5mL
Injection, powder, lyophilized, for solution; kitIntravenous3000 [iU]/5mL
Injection, powder, lyophilized, for solution; kitIntravenous500 [iU]/5mL
Kit; powder, for solutionIntravenous1000 unit / vial
Kit; powder, for solutionIntravenous2000 unit / vial
Kit; powder, for solutionIntravenous250 unit / vial
Kit; powder, for solutionIntravenous3000 unit / vial
Kit; powder, for solutionIntravenous500 unit / vial
SolutionIntravenous2000.00 UI
Prices
Unit descriptionCostUnit
Alphanine sd 250-1500 unit vial1.42USD vial
Mononine 1000 unit vial1.2USD vial
Mononine 500 unit vial1.2USD vial
Benefix 2000 unit vial1.12USD vial
Benefix 1000 unit vial1.0USD vial
Benefix 250 unit vial1.0USD vial
Benefix 500 unit vial1.0USD vial
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
Not Available

Properties

State
Liquid
Experimental Properties
PropertyValueSource
melting point (°C)54 °CLink, R.P., Castellino, F.J. Arch. Biochem. Biophsy. 227:259-265 (1983)
hydrophobicity-0.431Not Available
isoelectric point5.20Not Available

Targets

Build, predict & validate machine-learning models
Use our structured and evidence-based datasets to unlock new
insights and accelerate drug research.
Learn more
Use our structured and evidence-based datasets to unlock new insights and accelerate drug research.
Learn more
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
  1. Worfolk LA, Robinson RA, Tracy PB: Factor Xa interacts with two sites on monocytes with different functional activities. Blood. 1992 Oct 15;80(8):1989-97. [Article]
  2. Jones KC, Mann KG: A model for the tissue factor pathway to thrombin. II. A mathematical simulation. J Biol Chem. 1994 Sep 16;269(37):23367-73. [Article]
  3. Ambrosini G, Plescia J, Chu KC, High KA, Altieri DC: Activation-dependent exposure of the inter-EGF sequence Leu83-Leu88 in factor Xa mediates ligand binding to effector cell protease receptor-1. J Biol Chem. 1997 Mar 28;272(13):8340-5. [Article]
  4. London FS, Walsh PN: Zymogen factor IX potentiates factor IXa-catalyzed factor X activation. Biochemistry. 2000 Aug 15;39(32):9850-8. [Article]
  5. Scandella DH: Properties of anti-factor VIII inhibitor antibodies in hemophilia A patients. Semin Thromb Hemost. 2000;26(2):137-42. [Article]
  6. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
  7. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Ligand
General Function
Serine-type endopeptidase activity
Specific Function
Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.
Gene Name
F11
Uniprot ID
P03951
Uniprot Name
Coagulation factor XI
Molecular Weight
70108.56 Da
References
  1. Sun MF, Zhao M, Gailani D: Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX. J Biol Chem. 1999 Dec 17;274(51):36373-8. [Article]
  2. Gailani D, Ho D, Sun MF, Cheng Q, Walsh PN: Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential. Blood. 2001 May 15;97(10):3117-22. [Article]
  3. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Ligand
General Function
Serine-type peptidase activity
Specific Function
Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, o...
Gene Name
F7
Uniprot ID
P08709
Uniprot Name
Coagulation factor VII
Molecular Weight
51593.465 Da
References
  1. Baker DC, Robbe SL, Jacobson L, Manco-Johnson MJ, Holler L, Lefkowitz J: Hereditary deficiency of vitamin-K-dependent coagulation factors in Rambouillet sheep. Blood Coagul Fibrinolysis. 1999 Mar;10(2):75-80. [Article]
  2. Hertzberg MS, Facey SL, Hogg PJ: An Arg/Ser substitution in the second epidermal growth factor-like module of factor IX introduces an O-linked carbohydrate and markedly impairs activation by factor XIa and factor VIIa/Tissue factor and catalytic efficiency of factor IXa. Blood. 1999 Jul 1;94(1):156-63. [Article]
  3. Butenas S, van't Veer C, Mann KG: "Normal" thrombin generation. Blood. 1999 Oct 1;94(7):2169-78. [Article]
  4. Celie PH, Lenting PJ, Mertens K: Hydrophobic contact between the two epidermal growth factor-like domains of blood coagulation factor IX contributes to enzymatic activity. J Biol Chem. 2000 Jan 7;275(1):229-34. [Article]
  5. Shord SS, Lindley CM: Coagulation products and their uses. Am J Health Syst Pharm. 2000 Aug 1;57(15):1403-17; quiz 1418-20. [Article]
  6. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Cofactor
General Function
Oxidoreductase activity
Specific Function
Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.
Gene Name
F8
Uniprot ID
P00451
Uniprot Name
Coagulation factor VIII
Molecular Weight
267007.42 Da
References
  1. Neels JG, Bovenschen N, van Zonneveld AJ, Lenting PJ: Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation? Trends Cardiovasc Med. 2000 Jan;10(1):8-14. [Article]
  2. Carr ME Jr, Martin EJ, Kuhn JG, Seremetis SV: Effects of recombinant factor VIIa on platelet function and clot structure in blood with deficient prothrombin conversion. Thromb Haemost. 2003 May;89(5):803-11. [Article]
  3. Federici AB: The factor VIII/von Willebrand factor complex: basic and clinical issues. Haematologica. 2003 Jun;88(6):EREP02. [Article]
  4. Kalashnikova LA, Berkovskii AL, Dobrynina LA, Sergeeva EV, Kozlov AA, Aleksandrova EN, Nasonov EL: [Clotting factor VIII in Sneddon syndrome]. Klin Med (Mosk). 2003;81(9):42-5. [Article]
  5. Johansen RF, Sorensen B, Ingerslev J: Acquired haemophilia: dynamic whole blood coagulation utilized to guide haemostatic therapy. Haemophilia. 2006 Mar;12(2):190-7. [Article]
  6. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
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
  1. Butenas S, van't Veer C, Mann KG: "Normal" thrombin generation. Blood. 1999 Oct 1;94(7):2169-78. [Article]
  2. Kohler M: Thrombogenicity of prothrombin complex concentrates. Thromb Res. 1999 Aug 15;95(4 Suppl 1):S13-7. [Article]
  3. Seitz R, Dodt J: Virus safety of prothrombin complex concentrates and factor IX concentrates. Thromb Res. 1999 Aug 15;95(4 Suppl 1):S19-23. [Article]
  4. Samis JA, Ramsey GD, Walker JB, Nesheim ME, Giles AR: Proteolytic processing of human coagulation factor IX by plasmin. Blood. 2000 Feb 1;95(3):943-51. [Article]
  5. Bauer KA, Humphries S, Smillie B, Li L, Cooper JA, Barzegar S, Rosenberg RD, Miller GJ: Prothrombin activation is increased among asymptomatic carriers of the prothrombin G20210A and factor V Arg506Gln mutations. Thromb Haemost. 2000 Sep;84(3):396-400. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
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
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  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. [Article]
  3. Rohlena J, Kolkman JA, Boertjes RC, Mertens K, Lenting PJ: Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein. J Biol Chem. 2003 Mar 14;278(11):9394-401. Epub 2003 Jan 9. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Gamma-glutamyl carboxylase activity
Specific Function
Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vit...
Gene Name
GGCX
Uniprot ID
P38435
Uniprot Name
Vitamin K-dependent gamma-carboxylase
Molecular Weight
87560.065 Da
References
  1. Lin PJ, Straight DL, Stafford DW: Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product. J Biol Chem. 2004 Feb 20;279(8):6560-6. Epub 2003 Dec 2. [Article]
  2. Wu SM, Mutucumarana VP, Geromanos S, Stafford DW: The propeptide binding site of the bovine gamma-glutamyl carboxylase. J Biol Chem. 1997 May 2;272(18):11718-22. [Article]
  3. Rehemtulla A, Roth DA, Wasley LC, Kuliopulos A, Walsh CT, Furie B, Furie BC, Kaufman RJ: In vitro and in vivo functional characterization of bovine vitamin K-dependent gamma-carboxylase expressed in Chinese hamster ovary cells. Proc Natl Acad Sci U S A. 1993 May 15;90(10):4611-5. [Article]
  4. Stanley TB, Wu SM, Houben RJ, Mutucumarana VP, Stafford DW: Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase. Biochemistry. 1998 Sep 22;37(38):13262-8. [Article]
  5. Stanley TB, Stafford DW, Olivera BM, Bandyopadhyay PK: Identification of a vitamin K-dependent carboxylase in the venom duct of a Conus snail. FEBS Lett. 1997 Apr 21;407(1):85-8. [Article]

Drug created at June 13, 2005 13:24 / Updated at January 02, 2024 23:41