Thrombin R (G17) polyclonal antibody

Thrombin receptor (also designated protease-activated receptor-1 or PAR-1), PAR-2 and PAR-3 compose a distinct class of G protein-coupled receptors activated by proteolysis. Cleavage of these receptors by proteases occurs within the amino-terminal extracellular domain. Thrombin, a serine protease involved in platelet aggregation and blood coagulation, activates the thrombin receptor, resulting in elevated intracellular calcium levels in platelets. Thrombin also cleaves PAR-3 in vitro, suggesting that PAR-3 may be involved in thrombosis or mitogenesis. Thrombin receptor and PAR-4 appear to account for most thrombin signaling in platelets. Activation of PAR-2 in vitro is induced by trypsin, suggesting that PAR-2 is not an alternative thrombin receptor. Cytokines including TNF-α and IL-1β increase PAR-2 expression, indicating PAR-2 involvement in the acute inflammatory response.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of Thrombin R (G17) pAb at 1:500 dilution Lane1:PC3 whole cell lysate (40ug) Lane2:U-87MG whole cell lysate (40ug) Lane3:The Brian tissue lysate of Rat (10ug) Lane4:The Brain tissue lysate of Mouse (20ug)