Background: Thrombin receptor (also designated protease-activated receptor-1 or PAR-1), PAR-2, PAR-3 and PAR-4 compose a distinct class of G protein-coupled rec-eptors 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.
Description: Rabbit polyclonal to PAR3
Immunogen: KLH conjugated synthetic peptide derived from PAR3
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 42 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;
·Immunocytochemistry/Immunofluorescence: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.
