Anti-Prekallikrein Heavy Chain Antibody

The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.

Immunoblotting: use at 1-5ug/mL. Bands of 85kDa and 88kDa are detected <br><br>ELISA: use at 5-10ug/mL with prekallikrein sample bound to ELISA plates. <br><br>These are recommended concentrations. <br><br>Endusers should determine optimal concentrations for their applications.

This antibody recognizes two variants of prekallikrein in human plasma, 88kDa and 85kDa, and its activation products kallikrein, the complexes formed by kallikrein with its endogenous inhibitors C1 inhibitor, alpha-2-macroglobulin and antithrombin III, and 45kDa prekallikrein/kallikrein fragments. It also recognizes prekallikrein and its activation products in chimpanzee, rhesus, and baboon plasmas. The epitope for this antibody is located on the prekallikrein/kallikrein hevy chain and is involved in the interaction between prekallikrein and factor XIIa. This antibody inhibits prekallikrein activation in human and rhesus plasmas by ~60- 80% and 55%, respectively. This antibody does not cross-react with tissue kallikrein.

Human prekallikrein, a serine protease zymogen, is present in plasma as two variants, 88kDa and 85kDa, probably due to different carbohydrate content. Approximately 75% of the total prekallikrein in plasma is noncovalently associated with high molecular weight kininogen (HMWK). HMWK mediates binding of prekallikrein to a negatively-charged surface which is required for its optimal activation to kallikrein by activated factor XII. Although kallikrein light and heavy chains can behave as functionally independent domains, the interaction between these two chains is essential for full biologic activity.