Paxillin (Tyr-31), Phosphospecific Antibody

Paxillin is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and an SH3- and SH2-binding domain 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. Tyrosine phosphorylation of paxillin occurs in response to growth factors, neuropeptides, and integrins. The major sites of tyrosine phosphorylation include Tyr-31 and Tyr-118. Both of these sites may be involved in Crk binding to paxillin during integrin-mediated cell adhesion. These sites may provide docking motifs for recruitment of other signaling molecules to focal adhesions.

Clone M102 was generated from phospho-Paxillin (Tyr-31) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 31 of human paxillin.

This antibody detects a 72kDa* protein corresponding to the molecular mass of phosphorylated paxillin on SDS-PAGE immunoblots of pervanadate treated A431 cells, but not in A431 control cells. This human sequence is highly conserved in rat and mouse paxillin.