epitope corresponding to amino acids 230-328 of PAR-2 of human origin
Modification Notes
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).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of PAR-2 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine and porcine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 230-328 of PAR-2 of human origin
Tissue Specificity
epitope corresponding to amino acids 230-328 of PAR-2 of human origin
Western blot analysis of PAR-2 expression in non-transfected: (A) and mouse PAR-2 transfected: (B) 293T whole cell lysates.
Application Notes
recommended for detection of PAR-2 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine and porcine:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.