Paxillin (Ser-83), phospho-specific polyclonal, anti-mouse, rat

Background:
Paxillin, a focal adhesion protein, is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and SH3-/SH2-binding domains that participate in a variety of protein-protein interactions with kinases, GTPase-activating proteins, and cytoskeletal proteins. Phosphorylation of paxillin occurs at both tyrosine and serine sites. Serine phosphorylation of paxillin occurs in response to growth-factor activation and fibronectins. Both ERK and p38MAPK kinases phosphorylate serine 83 in vitro. HGF stimulation of murine epithelial cells leads to ERK-mediated phosphorylation of Ser-83, which is required for HGF-induced cell spreading and migration. In addition, Ser-83 is phosphorylated in response to NGF in PC12 cells, and this phosphorylation may be involved in neurite extension. In human paxillin, Ser-85 rather than Ser-83 may be the site phosphorylated by p38 MAPK and mutation of this site inhibits NGF-induced neurite extension. Thus, serine residues in the N-terminal region of paxillin may be important for growth-factor mediated changes in activity.

Immunogen: Phospho-Paxillin (Ser-83) synthetic peptide (coupled to KLH) corresponding to amino acid residues around serine 83 of mouse paxillin. This sequence is highly conserved in rat and human paxillin and is also found in all isoforms (a, b, g) of paxillin.

Specificity: This antibody was affinity purified using phospho-Paxillin (Ser-83) peptide (without carrier). The antibody detects a 68kDa* protein corresponding to the molecular mass of phosphorylated paxillin on SDS-PAGE immunoblots of NGF treated rat PC12 cells, as well as calyculin A treated human A431 cells and mouse macrophages.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.