||Activated protein C (APC) is an anticoagulant serine protease derived from the two chain, vitamin K-dependent zymogen, protein C. A complex between alpha-thrombin and thrombomodulin catalyzes a single cleavage at Arg-12 (Arg-14 in bovine) in the heavy chain of protein C, to generate activated Protein C. Several non-physiologically relevant proteases such as RVV-X activator, trypsin, and PROTAC are also capable of activating protein C. APC functions as an anticoagulant which catalyzes the proteolytic inactivation of the cofactors, factors Va and VIIIa, leading to inhibition of the prothrombinase and factor Xase complexes. The inactivation of factors Va and VIIIa is both Ca2+ and phospholipid dependent. The vitamin K dependent cofactor, protein S, moderately increases this rate of inactivation by forming a 1:1 complex with APC (Kd=6x10-9M).
||20 mM Hepes, 150 mM NaCl, pH 7.4
|Molecular Mass :
||>95% by SDS-PAGE. NOT tissue/cell culture grade. Not tested for endotoxin.
||Extinction coefficient:13.7, Isoelectric point:4.2-4.5, Percent carbohydrate:0.14, Structure:two chains, Mr=35,000 and 21,000, disulfide linked, NH2-terminal gla domain two EGF domains