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.

Proteinase-activated receptor 1; PAR-1; Coagulation factor II receptor; Thrombin receptor; F2R; CF2R; PAR1; TR

p25116

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 55 kDa

Rabbit

This antibody detects endogenous levels of Thrombin R protein.

Synthetic peptide, corresponding to amino acids 12-60 of Human Thrombin R.

Polyclonal

Rabbit IgG

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

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.