|Reactivity||Human, Mouse, Rat|
|Calculated MW||44441 Da|
|Homology||Mouse -13/15 amino acid residues identical; human 11/15 amino acid residues residues identical.|
|Other Names||Proteinase-activated receptor 2, PAR-2, Coagulation factor II receptor-like 1, Thrombin receptor-like 1, F2rl1, Par2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)KRMQISLTSNKFSRK, corresponding to amino acid residues 368-382 of rat PAR-2 (Accession Q63645). Intracelluar, C- terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.6 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Protease-activated receptor 2 (PAR-2) belongs to a family of four G protein-coupled receptors (PAR-1 - 4) that are activated as a result of proteolytic cleavage by certain serine proteases, hence their name. In this novel modality of activation, a specific protease cleaves the PAR receptor within a defined sequence in its extracellular N-terminal domain. This results in the creation of a new N-terminal tethered ligand, which subsequently binds to a site in the second extracellular loop of the same receptor. This binding results in the coupling of the receptor to G proteins and in the activation of several signal transduction pathways.1-3 Different PARs are activated by different proteases. Hence, PAR-1 is activated by thrombin, as are PAR-3 and PAR-4.1-3 PAR-2 is the only PAR family receptor that is activated by trypsin and not by thrombin. PAR-2 can be also cleaved and activated by other proteases such as tryptase, membrane-type serine protease 1, protease 3, and others.1-3 The intramolecular nature of PAR activation and the continuous presence of the tethered ligand that cannot diffuse away imply the existence of several mechanisms for the rapid termination of PAR signaling. Indeed, following receptor activation, there is rapid phosphorylation of the C-terminal end of the receptor, followed by receptor internalization and degradation. In addition, several proteases can cleave away the tethered ligand, thereby “disarming” the PAR.1-3 PAR-2-mediated intracellular signaling has not been clearly elucidated, but activators of PAR-2 induce generation of IP3 and mobilization of intracellular Ca2+. Activation of the ERK1/2 and NF-kB intracellular pathways following PAR-2 activation has been also described.1-3 Tissue distribution of PAR-2 is wide with the highest expression levels found in pancreas, small intestine, liver and kidney. In addition, PAR-2 expression was observed in dorsal root ganglion neurons, smooth muscle cells and endothelial cells. The physiological role of PAR-2 is not clearly understood, however studies using PAR-2 knockout mice have suggested roles in the cardiovascular, pulmonary and gastrointestinal systems. Several studies suggest that PAR-2 plays a central role in inflammatory diseases and nociceptive pain transduction; hence PAR-2 blockers have been proposed to be useful in the therapeutic control of inflammation and pain.1-3 Abgent is pleased to offer a highly specific antibody directed against an epitope at the intracellular C-terminus of the rat protease-activated receptor-2. Anti-Protease-activated Receptor-2 antibody (#AG1058) can be used in western blot analysis and immunocytochemical applications, and has been tested in rat, mouse and human samples.
References 1. MacFarlane, S.R. et al. (2001) Pharmacol. Rev. 53, 245. 2. Hollenberg, M.D. and Compton, S.J. (2002) Pharmacol. Rev. 54, 203. 3. Ossovskaya, V.S. and Bunnett, N.W. (2004) Physiol. Rev. 84, 579.
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