FA10 (light chain, Cleaved-Arg179) rabbit pAb

Catalytic activity: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. 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. online information: Factor X entry, PTM: N- and O-glycosylated. PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. similarity: Belongs to the peptidase S1 family. similarity: Contains 1 Gla (gamma-carboxy-glutamate) domain. similarity: Contains 1 peptidase S1 domain. similarity: Contains 2 EGF-like domains. subunit: The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. tissue specificity: Plasma; synthesized in the liver.