Overview
- Peptide (C)KRMQISLTSNKFSRK, corresponding to amino acid residues 368-382 of rat PAR-2 (Accession Q63645). Intracelluar, C- terminus.
Western blot analysis of human breast adenocarcinoma MDA-MB-231 (lanes 1 and 4) and MDA-MB-468 (lanes 2 and 5), and human lung small cell carcinoma NCI-H526 (lanes 3 and 6) cell lines:1-3. Anti-PAR2 (F2RL1) Antibody (#APR-032), (1:600).
4-6. Anti-PAR2 (F2RL1) Antibody, preincubated with PAR2/F2RL1 Blocking Peptide (#BLP-PR032).
Western blot analysis of rat lung (lanes 1 and 3) and liver (lanes 2 and 4) lysates:1,2. Anti-PAR2 (F2RL1) Antibody (#APR-032), (1:400).
3,4. Anti-PAR2 (F2RL1) Antibody, preincubated with PAR2/F2RL1 Blocking Peptide (#BLP-PR032).
Western blot analysis of mouse kidney lysates:1. Anti-PAR2 (F2RL1) Antibody (#APR-032), (1:400).
2. Anti-PAR2 (F2RL1) Antibody, preincubated with PAR2/F2RL1 Blocking Peptide (#BLP-PR032).
Western blot analysis of rat dorsal root ganglion lysates:1. Anti-PAR2 (F2RL1) Antibody (#APR-032), (1:200).
2. Anti-PAR2 (F2RL1) Antibody, preincubated with PAR2/F2RL1 Blocking Peptide (#BLP-PR032).
- Human tendon sections (1:100) (Christensen, J. et al. (2015) Mol. Pain 11, 13.).
Expression of PAR-2 in human prostate carcinoma cell lineImmunocytochemical staining of paraformaldehyde-fixed and permeabilized human PC-3 cells. A. Cells were stained with Anti-PAR2 (F2RL1) Antibody (#APR-032), (1:500), followed by goat-anti-rabbit-AlexaFluor-555 secondary antibody (orange). B. Nuclei were visualized with the cell-permeable dye Hoechst 33342 (blue). C. Merge of A and B.
- MacFarlane, S.R. et al. (2001) Pharmacol. Rev. 53, 245.
- Hollenberg, M.D. et al. (2002) Pharmacol. Rev. 54, 203.
- Ossovskaya, V.S. et al. (2004) Physiol. Rev. 84, 579.
Protease-activated receptor 2 (PAR-2) belongs to a family of four G protein-coupled receptors (PAR1-4) 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
Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of rat protease-activated receptor-2. Anti-PAR2 (F2RL1) Antibody (#APR-032) can be used in western blot, immunohistochemistry and and immunocytochemistry applications. It has been designed to recognize PAR-2 from rat, mouse and human samples.
Applications
Citations
Powered by Bioz- Mouse hippocampal sections.
Shavit-Stein, E. et al. (2017) Front. Mol. Neurosci. 10, 42. - Human tendon sections (1:100).
Christensen, J. et al. (2015) Mol. Pain 11, 13. - Mouse and rat kidney sections. Also tested in PAR2-/- mice.
Morla, L. et al. (2013) J. Biol. Chem. 288, 10124.
- Human cultured tenocytes (1:100).
Christensen, J. et al. (2015) Mol. Pain 11, 13.
- Vesey, D.A. et al. (2013) Am. J. Physiol. 304, F737.
