Mouse monoclonal antibody

JST 001-38 is specific for APC:PCI complex and cleaved PCI but has little reactivity towards native PCI. The dissociation constants (as determined by standard surface plasmon resonance technique) are: Kd= 4x10e-10 M for PCI in complex with APC and 2x10e-10 M for cleaved PCI. The value of Kd for native PCI is too low to measure, i.e. > 10e-5 M.

Mixture of PCI in complex with PSA (approx. 80%) and PCI cleaved from such a complex (approx. 20%).

IgG1/k

The epitope is loctated in the calcium-binding N-terminal EGF domain of protein C.

Available in 200 µL and 1 mL size.1 mg/mL +/- 15%. See Certificate of Analysis for details.

Activated Protein C (APC), a serine proteinase is inhibited by Protein C inhibitor (PCI). PCI belongs to a group of inhibitors sometimes referred to as serpines (serine proteinase inhibitors), and form 1:1 complexes with APC. PCI plasma concentration is approximately 4ug/m1 .The complex formation between APC and PCI proceeds at a slow rate, which is manifested by a long half-life for APC in plasma, wherein t1/2 is about 20 min.However, the rate of complex formation between APC and PCI is increased by heparin.Upon complex formation with APC, the serpin is cleaved in its so-called bait region, whereby a stable intermediate acyl complex is formed. With time, the intermediate acyl complex dissociates, whereby APC is regenerated and a proteolytically modified, i. e. cleaved, inactive serine proteinase inhibitor is formed.