Coagulation Factor IX Human



Coagulation Factor IX Human is a coagulation factor used to treat hemophilia B or factor IX hemophilia.

Brand Names
Alphanine Sd, Balfaxar, Beriplex, Immunine Vh, Kcentra, Octaplex
Generic Name
Coagulation Factor IX Human
DrugBank Accession Number

Factor IX (or Christmas factor) is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this protein causes hemophilia B.

Biologic Classification
Protein Based Therapies
Blood factors
Protein Structure
Protein Chemical Formula
Protein Average Weight
46548.2 Da
>DB00100 sequence
Download FASTA Format
  • Antihemophilic factor B
  • Coagulation factor IX (human)
  • Factor IX (Human)
  • Factor IX purificado
  • Human coagulation factor IX



Factor IX is used to treat Christmas disease. Factor IX deficiency is treated by injection factor IX produced from human plasma.

Along with other blood coagulation factors, it is used to reverse acquired coagulation factor deficiency induced by Vitamin K antagonist (VKA, e.g., warfarin) therapy in adult patients with a need for an urgent surgery/invasive procedure.3

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
Used in combination to reverseAcquired coagulation factor deficiency caused by vitamin k antagonistCombination Product in combination with: Coagulation factor X human (DB13148), Prothrombin (DB11311), Protein C (DB11312), Protein S human (DB13149), Coagulation factor VII human (DB13150)•••••••••••••••••
Treatment ofBleeding caused by hemophilia b••••••••••••
Prophylaxis ofBleeding 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

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.

ACoagulation factor X
ACoagulation factor XI
ACoagulation factor VII
ACoagulation factor VIII
UProthrombinNot AvailableHumans
UProlow-density lipoprotein receptor-related protein 1Not AvailableHumans
UVitamin K-dependent gamma-carboxylaseNot AvailableHumans

Not Available

Volume of distribution

Not Available

Protein binding

Not Available

Not Available
Route of elimination

Not Available


18.8 ± 5.4 hours.


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

Not Available

Not Available
Pharmacogenomic Effects/ADRs
Not Available


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.
AbciximabThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Abciximab.
AcenocoumarolThe therapeutic efficacy of Coagulation Factor IX Human 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 Human.
AlteplaseThe therapeutic efficacy of Coagulation Factor IX Human 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 Human.
Food Interactions
No interactions found.


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
BebulinKit30 [iU]/1mLIntravenousBaxalta Incorporated1992-08-192018-11-30US flag
Bebulin VHKit300 [iU]/1mLIntravenousBaxter Laboratories2011-03-162012-09-30US flag
Immunine VhPowder, for solution720 unit / 5 mLIntravenousTakeda1996-10-18Not applicableCanada flag
MononineKit1000 [iU]/10mLIntravenousCSL BEHRING LLC1992-08-202022-01-28US flag
MononineInjection, powder, lyophilized, for solution100 [iU]/1mLIntravenousCSL BEHRING LLC1992-08-202009-04-06US flag
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
AlphaNine SDCoagulation Factor IX Human (1000 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-31Not applicableUS flag
AlphaNine SDCoagulation Factor IX Human (500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-312018-10-21US flag
AlphaNine SDCoagulation Factor IX Human (500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-31Not applicableUS flag
AlphaNine SDCoagulation Factor IX Human (1500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-31Not applicableUS flag
AlphaNine SDCoagulation Factor IX Human (1000 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-312020-03-31US flag
Unapproved/Other Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
REBLENINE VF 500 IU FAKTOR IX FLAKON, 1 ADETCoagulation Factor IX Human (500 IU/10ml)Injection, powder, lyophilized, for solutionIntravenousVİTALİS SAĞLIK ÜRÜNLERİ DANIŞMANLIK VE TİC. A.Ş.2015-09-29Not applicableTurkey flag


ATC Codes
B02BD04 — Coagulation factor ixB02BD01 — Coagulation factor ix, ii, vii and x in combination
Drug Categories
Chemical TaxonomyProvided by Classyfire
Not Available
Organic Compounds
Super Class
Organic Acids
Carboxylic Acids and Derivatives
Sub Class
Amino Acids, Peptides, and Analogues
Direct Parent
Alternative Parents
Not Available
Not Available
Molecular Framework
Not Available
External Descriptors
Not Available
Affected organisms
Not Available

Chemical Identifiers

CAS number


General References
  1. Zogg T, Brandstetter H: Activation mechanisms of coagulation factor IX. Biol Chem. 2009 May-Jun;390(5-6):391-400. doi: 10.1515/BC.2009.057. [Article]
  2. NCBI [Link]
  3. FDA Approved Drug Products: BALFAXAR (prothrombin complex concentrate, human-lans) lyophilized powder for solution, for intravenous use (July 2023) [Link]
PubChem Substance
FDA label
Download (1000 KB)
Download (34.9 KB)

Clinical Trials

Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package
PhaseStatusPurposeConditionsCountStart DateWhy Stopped100+ additional columns
4CompletedNot AvailableHemophilia B1somestatusstop reasonjust information to hide
4CompletedOtherArrhythmia / Blood Platelet Transfusion / Cardiac Diseases / Cardiopulmonary Bypass / Death / Surgery, Cardiac1somestatusstop reasonjust information to hide
4CompletedPreventionCoronavirus Disease 2019 (COVID‑19) / Hemophilia B1somestatusstop reasonjust information to hide
4CompletedTreatmentBleeding / Blood Loss During Surgery / Cardiovascular Surgical Procedures / Fresh Frozen Plasma / Prothrombin Complex Concentrates1somestatusstop reasonjust information to hide
4CompletedTreatmentHemophilia B2somestatusstop reasonjust information to hide


Not Available
Not Available
Dosage Forms
InjectionIntravenous800 UI
Injection, powder, for solutionIntravenous200 UI
Injection, powder, for solutionIntravenous500 UI
Injection, powder, for solutionIntravenous800 UI
Powder, for solutionIntravenous1000 U.I.
Powder, for solutionIntravenous200 U.I./5ML
Powder, for solutionIntravenous500 U.I.
Injection, solutionIntravenous500 IU/10mL
Injection, powder, for solutionIntravenous100 IU
Injection, powder, for solutionIntravenous1500 IU/10ML
Injection, solutionIntravenous1000 U.I.
Injection, solutionIntravenous500 U.I.
Powder, for solutionParenteral1000 U.I.
Powder, for solutionParenteral1500 U.I.
Powder, for solutionParenteral500 U.I.
Injection, powder, lyophilized, for solutionIntravenous50 IU
Injection, powder, for solutionIntravenous1000 IU/10ml vial
Injection, powder, for solutionIntravenous1500 IU/10ml vial
Injection, powder, for solutionIntravenous500 IU/10ml vial
KitIntravenous30 [iU]/1mL
KitIntravenous300 [iU]/1mL
Injection, powder, for solutionIntravenous; Parenteral1500 IU
Injection, powder, for solutionIntravenous; Parenteral250 IU
Injection, powder, for solutionParenteral1000 IU
Injection, powder, for solutionParenteral2000 IU
Injection, powder, for solutionParenteral500 IU
Powder, for solutionIntravenous
SolutionParenteral250 UI
Injection, powder, for solutionParenteral
Injection, powder, lyophilized, for solutionIntravenous500 iu/10ml
Injection, powder, for solutionIntravenous1200 IU
Injection, powder, for solutionParenteral200 U.I.
Injection, powder, for solutionParenteral600 U.I.
Injection, powder, for solutionParenteral100 IU/ml
Injection, powder, for solutionParenteral50 IU/ml
Injection, powder, for solutionParenteral100 I.E./ml
Injection, solutionIntravenous1000 iu/10ml
Injection, solutionIntravenous500 iu/5ml
Injection, powder, for solutionIntravenous; Parenteral3500 UI
Injection, powder, for solutionParenteral1200 I.E.
Injection, powder, for solutionIntravenous120 IU/mL
Injection, powder, for solutionParenteral200 I.E.
Injection, powder, for solutionParenteral600 I.E.
Powder, for solution
Powder, for solutionIntravenous720 unit / 5 mL
Injection, powder, for solutionIntravenous1000 IU/10ML
Powder, for solutionParenteral200 UI/5ML
Powder, for solutionParenteral500 UI/10ML
Injection, powder, lyophilized, for solution; kitIntravenous
Powder, for solutionParenteral
SolutionIntravenous500 UI
Injection, powder, for suspensionParenteral1000 IU
Injection, powder, for solutionIntravenous1000 IU
Injection, powder, for solutionIntravenous250 IU
Injection, powder, for solutionIntravenous500 IU
Injection, powder, lyophilized, for solutionIntravenous100 [iU]/1mL
KitIntravenous1000 [iU]/10mL
KitIntravenous500 [iU]/5mL
SolutionParenteral1000.0 UI
Injection, powder, for solutionParenteral50 I.E./ml
Injection, powder, lyophilized, for solutionIntravenous
Kit; powder, for solutionIntravenous
Injection, powder, for solutionIntravenous drip520 IU/vial
InjectionIntravenous1000 IU/10ml
InjectionIntravenous1500 IU/10ml
InjectionIntravenous500 IU/5ml
Injection, powder, for solutionParenteral
Injection, powder, for solutionIntravenous
Injection, powder, for solutionIntravenous1000 UI
Injection, powder, for solutionIntravenous2000 UI
Injection, powder, for solutionIntravenous3000 UI
SolutionParenteral500.000 UI
Injection, powder, for solutionIntravenous
Injection, powder, for solution50 iu/1vial
Injection, powder, for solutionIntravenous500 iu/vial
Injection, powder, lyophilized, for solutionIntravenous250 IU
Injection, powder, for solution600 iu/1vial
Powder100 iu/1vial
Not Available
Not Available


Experimental Properties
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


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
Pharmacological action
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
Uniprot ID
Uniprot Name
Coagulation factor X
Molecular Weight
54731.255 Da
  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]
Pharmacological action
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
Uniprot ID
Uniprot Name
Coagulation factor XI
Molecular Weight
70108.56 Da
  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]
Pharmacological action
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
Uniprot ID
Uniprot Name
Coagulation factor VII
Molecular Weight
51593.465 Da
  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]
Pharmacological action
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
Uniprot ID
Uniprot Name
Coagulation factor VIII
Molecular Weight
267007.42 Da
  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]
Pharmacological action
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
Uniprot ID
Uniprot Name
Molecular Weight
70036.295 Da
  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]
Pharmacological action
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
Uniprot ID
Uniprot Name
Prolow-density lipoprotein receptor-related protein 1
Molecular Weight
504601.695 Da
  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]
Pharmacological action
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
Uniprot ID
Uniprot Name
Vitamin K-dependent gamma-carboxylase
Molecular Weight
87560.065 Da
  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 November 18, 2016 21:36 / Updated at April 23, 2024 11:38