Background:

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.

Specificity:

Thrombin R (G17) polyclonal antibody detects endogenous levels of Thrombin R protein

Alternative names:

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

Species reactivity:

Human,Mouse,Rat

Host:

Rabbit

Ig type:

Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Immunogen:

Synthetic peptide, corresponding to the N-terminal of Human Thrombin R.

Purification & Purity:

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

Molecular weight:

~ 47 kDa

Applications:

WB

Usage:

WB: 1:500~1:1000

Storage:

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Precautions:

For research use only, not for use in diagnostic procedure.

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