Coagulation Factor XI Protein & Antibody (FXI, F11)

Coagulation Factor XI Products

Coagulation Factor XI Protein, Recombinant

Molecule	Species	Description	Cat. No
Coagulation Factor XI	Human	Coagulation Factor XI/FXI/F11 Protein, Recombinant	10302-H08H

  10302-H08H: The specific activity is > 200 pmoles / min / µg. Measured by its ability to cleave the fluorogenic peptide substrate, t-butyloxycarbonyl-Ile-Glu-Gly-Arg-7-amido-4-methylcoumarin (Boc-IEGR-AMC).

Coagulation Factor XI Antibody

Molecule	Application	Description	Cat. No
Human Coagulation Factor XI	WB, ELISA	Mouse Monoclonal Antibody	10302-MM04
Human Coagulation Factor XI	WB, ELISA	Rabbit Polyclonal Antibody	10302-RP01
Human Coagulation Factor XI	WB, ELISA	Rabbit Polyclonal Antibody (Antigen Affinity Purified)	10302-RP02

Coagulation Factor XI cDNA Clone

Molecule	Species	Description	Cat. No
Coagulation Factor XI	Human	Homo sapiens Coagulation Factor XI/FXI/F11 cDNA Clone(NM_000128.3)	HG10302-M
Coagulation Factor XI	Mouse	Mus musculus Coagulation Factor XI/FXI/F11 cDNA Clone	MG50237-M

Coagulation Factor XI Related Areas

Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Coagulation Factor XI

Immunology>>Innate Immunity>>Coagulation>>Coagulation Factor XI

Cardiovascular>>Coagulation>>Coagulation Factor XI

Cardiovascular>>Platelet>>Coagulation Factor XI

Coagulation Factor XI Alternative Names

Coagulation Factor XI, FXI, F11, MGC141891 [Homo sapiens]

Coagulation Factor XI, FXI, F11, 1600027G01Rik, AI503996, Cf11 [Mus musculus]

Coagulation Factor XI Background

Factor XI (plasma thromboplastin antecedent) is a plasma glycoprotein, and a zymogen acting as a serine protease which participates in blood coagulation as a catalyst in the conversion of factor IX to factor IXa in the presence of calcium ions. It is an unusual dimeric protease, with structural features that distinguish it from vitamin K-dependent coagulation proteases. The factor XI is synthesized in the liver as a single polypeptide chain with a molecular weight estimated between 125 ~160 kDa and then is processed into a disulfide-bond linked homodimer. FXI is a homodimer, with each subunit containing four apple domains and a protease domain. The apple domains form a disk structure with binding sites for platelets, high molecular weight kininogen, and the substrate factor IX (FIX). FXI is converted to the active protease FXIa by cleavage of the Arg369-Ile370 bond on each subunit. After the activation reaction, Factor XIa is composed of two heavy and two light chains held together by three disulfide bonds. The heavy chains are derived from the amino termini of the zymogen and responsible for the binding of factor XI to high molecular weight kininogen and for the activation of factor IX, while the light chain contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases. FXI deficiency is a disorder characterized by a mild or no bleeding tendency. Severe FXI deficiency is an injury-related bleeding disorder common in Ashkenazi Jews and rare worldwide.

Coagulation Factor XI Related Studies

1. Gailani D, et al. (2009) Structural and functional features of factor XI. J Thromb Haemost. 7 Suppl 1: 75-8.
2. Duga S, et al. (2009) Factor XI Deficiency. Semin Thromb Hemost. 35(4): 416-25.
3. Emsley J, et al. (2010) Structure and function of factor XI. Blood. 115(13): 2569-77.