Anti-Proteinase-activated Receptor-2
- 貨號 Cat. No.
- APR-032
- 規格 Size
- 50 μl 0.2ml
Description
Anti-Proteinase-activated Receptor-2
| Product#: | APR-032 |
| Sizes: |
| 50 µl |
| 0.2 ml |
| Host: |
| Rabbit. |
| Epitope: |
Peptide(C)KRMQISLTSNKFSRK corresponding to amino acid residues 368-382 of rat PAR-2 (Accession Q63645). |
 |
| Putative epitope location: |
Intracelluar, C- terminus. |
| Homology: |
| Mouse 13/15 and human 11/15 residues identical. |
| Reactivity Confirmed: |
Rat, mouse, human. |
Applications:
| Western Blotting: |
 | Western blotting of rat dorsal root ganglion lysates: 1. Anti-PAR-2 antibody (#APR-032), (1:200). 2. Anti-PAR-2, preincubated with the control peptide antigen. |
 | Western blotting 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-PAR-2 antibody (#APR-032), (1:600). 4-6. Anti-PAR-2, preincubated with the control peptide antigen. |
 | Western blotting of mouse kidney lysates: 1. Anti-PAR-2 antibody (#APR-032), (1:400). 2. Anti-PAR-2, preincubated with the control peptide antigen. |
| Immunocytochemistry: |
 |
Immunocytochemical staining of PAR-2 in a human prostate carcinoma cell line.
|
Proteinase-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 proteinase 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 proteinases. 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 proteinases such as tryptase, membrane-type serine protease 1, proteinase 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 proteinases can cleave away the tethered ligand, thereby isarming?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 at the intracellular C-terminus of the rat proteinase-activated receptor-2. Anti-Human Proteinase-activated Receptor-2 antibody (#APR-032) can be used in Western blot and immunocytochemical applications and has been tested in rat, mouse and human samples.