EC:, Coagulation Factor IX, Plasma Thromboplastin Component, Christmas Factor, Christmas Disease, Factor IX F9, Hemophilia B, EC, F9 P22, THPH8, HEMB, FIX, P19, Factor IX, F9, PTC, EC 3.4.21, Plasma Thromboplastic Component, Factor 9


Coagulation 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 ions, phospholipids, and factor VIIIa.

KO Status


Drug Information

Launched drugs: 21
Drugs in clinical trials: 14
Latest Research Phase: Approved

Drug Name





Clinical Trials

Human prothrombin complex (Guangdong Wellen)


Guangdong Wellen Pharmaceutical Co Ltd


Human prothrombin complex (Octapharma)



Hemorrhage, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma

Human prothrombin complex (Shanghai Xinxing)


Shanghai Xinxing Pharmaceutical Co Ltd


Human prothrombin complex (Sinopharm Shanghai Plasma)


Sinopharm Shanghai Plasma-Derived Biotherapies Co Ltd


Human prothrombin complex (Boya Bio-Pharmaceutical)


Boya Bio-Pharmaceutical Group Co Ltd


Human prothrombin complex (Tonrol Biopharmaceuticals)


Tonrol Bio-Pharmaceutical Co Ltd

Hemophilia B, Hemorrhage

Prothrombin complex concentrat (Taibang Biological Products)


Shandong Taibang Biological Products Co,Ltd

Hemorrhage, Antithrombin III Deficiency

Human Coagulation Factor IX(China Biologic Products)


Shandong Taibang Biological Products Co,Ltd

Hemophilia B

Human prothrombin complex (Hualan Biological Engineering)


Hualan Genetic Engineering Co Ltd

Blood Coagulation Disorders, Hemophilia B, Factor X Deficiency

Eptacog alfa biosimilar (AryoGen Biopharma)


Aryogen Biopharma

Hemophilia A, Hemophilia B, Factor VII Deficiency, Thrombasthenia





Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX

Freedman S.J., Blostein M.D., Baleja J.D., Jacobs M., Furie B.C., Furie B.,

J. Biol. Chem. 271:16227-16236(1996)

Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm

Li L., Darden T.A., Freedman S.J., Furie B.C., Furie B., Baleja J.D., Smith H., Hiskey R.G., Pedersen L.G.,

Biochemistry 36:2132-2138(1997)

Sequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX

Huang L.H., Cheng H., Pardi A., Tam J.P., Sweeney W.V.,

Biochemistry 30:7402-7409(1991)

The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha

Baron M., Norman D.G., Harvey T.S., Handford P.A., Mayhew M., Tse A.G.D., Brownlee G.G., Campbell I.D.C.,

Protein Sci. 1:81-90(1992)

The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions

Rao Z., Handford P., Mayhew M., Knott V., Brownlee G.G., Stuart D.,

Cell 82:131-141(1995)

Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding

Hopfner K.-P., Lang A., Karcher A., Sichler K., Kopetzki E., Brandstetter H., Huber R., Bode W., Engh R.A.,

Structure 7:989-996(1999)

Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody

Huang M., Furie B.C., Furie B.,

J. Biol. Chem. 279:14338-14346(2004)

Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa

Zogg T., Brandstetter H.,

Structure 17:1669-1678(2009)

Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis

Wang S., Beck R., Blench T., Burd A., Buxton S., Malic M., Ayele T., Shaikh S., Chahwala S., Chander C., Holland R., Merette S., Zhao L., Blackney M., Watts A.,

J. Med. Chem. 53:1465-1472(2010)

Structure based drug design: development of potent and selective factor IXa (FIXa) inhibitors

Wang S., Beck R., Burd A., Blench T., Marlin F., Ayele T., Buxton S., Dagostin C., Malic M., Joshi R., Barry J., Sajad M., Cheung C., Shaikh S., Chahwala S., Chander C., Baumgartner C., Holthoff H.P., Giddings A.,

J. Med. Chem. 53:1473-1482(2010)