PAR-2 Anticuerpo(SAM11): sc-13504

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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 (1). Cleavage of these receptors by proteases occurs within the amino-terminal extracellular domain (2). Thrombin, a serine protease involved in platelet aggregation and blood coagulation, activates the thrombin receptor, resulting in elevated intracellular calcium levels in platelets (3,4). Thrombin also cleaves PAR-3 in vitro, suggesting that PAR-3 may be involved in thrombosis or mitogenesis (5). Thrombin receptor and PAR-4 appear to account for most thrombin signaling in platelets (8). Activation of PAR-2 in vitro is induced by trypsin, suggesting that PAR-2 is not an alternative thrombin receptor (2,6). Cytokines including TNF-å and IL-1ß increase PAR-2 expression, indicating PAR-2 involvement in the acute inflammatory response (7).