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Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognize a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: coagulation factor 2; Coagulation factor II; coagulation factor II (thrombin); prepro-coagulation factor II; Prothrombin; prothrombin B-chain; serine protease; thrombin
Gene Aliases: Cf-2; Cf2; F2; FII; PT; RPRGL2; THPH1
UniProt ID: (Mouse) P19221, (Human) P00734
Entrez Gene ID: (Mouse) 14061, (Rat) 29251, (Human) 2147
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