PAR-3 Background Information 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 TNFå and IL-1ß increase PAR-2 expression, indicating PAR-2 involvement in the acute inflammatory response.
PAR-3 (H-103) Product Citations
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PAR-3 (H-103)
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PAR-3 (H-103): sc-5598. Western blot analysis of human recombinant PAR-3 fusion protein.
PAR-3 (H-103): sc-5598. Western blot analysis of PAR-3 expression in rat eye tissue extract.
PAR-3 (H-103): sc-5598. Western blot analysis of PAR-3 expression in HL-60 (A) and CCD-1064Sk (B) whole cell lysates.
PAR-3 (H-103): sc-5598. Western blot analysis of PAR-3 expression in MEG-01 (A) and K-562 (B) whole cell lysates.
