Description
Product Characteristics:
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.
Subcellular location: Secreted, Extracellular matrix
Synonyms: coagulation factor II, prothrombin, F2, Cf-2, Cf2, FII, F 2, coagulation factor II thrombin, Coagulation factor II, Coagulation factor II precursor, F2, Factor II, Factor-II, Prothrombin, prothrombin B-chain, PT, serine protease, THRB, THRB_HUMAN, Thrombin, Thrombin heavy chain.
Target Information: Coagulation factor II is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. F2 also plays a role in maintaining vascular integrity during development and postnatal life. Mutations in F2 leads to various forms of thrombosis and dysprothrombinemia. [provided by RefSeq, Jul 2008]