Anti-APC-AAT Complexes, Neoepitope Antibody

Protein C is a vitamin K-dependent serine protease produced in the liver and made up of 2 polypeptide chains. The 62 kDa proenzyme is activated by thrombin and the active enzyme cleaves factor Va and VIIIa and thus inhibits blood coagulation. The molecular weight of the active enzyme is 55 kDa and the normal concentrations in human plasma is approximately 1-3 ng/ml because of the very fast turnover, the proenzyme concentration is approximately 3 μg/ml. The activated protein C (APC) is inhibited by members of the serine protease inhibitor (serpin) family, of which α1-antitrypsin (AAT) and protein C inhibitor (PCI) are the most important.

PROC, APC, PC, PROC1, THPH3, THPH4, vitamin K-dependent protein C, Protein C-Nagoya, activated protein C, anticoagulant protein C, autoprothrombin IIA, blood coagulation factor XIV, coagulation factor XIV, prepro-protein C, type I protein C

ABS 001-07 is specific for a conformation-dependent neoepitope that is expressed in activated protein C upon complex-formation with α1-antitrypsin. No reaction is seen to non-complexed α1-antitrypsin and only very little cross reaction to protein C zymogen. Note that specificity is calcium dependent.