Anti-Paxillin (Ser-83), Phosphospecific Antibody

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 tyrosine, threonine, and serine sites. Serine and threonine phosphorylation of paxillin occur in response to growth-factor activation, PKC activators, and fibronectins. Phosphorylation of Ser-85, Ser-178, and Thr-538 may be important sites for regulating paxillin activity. Paxillin phosphorylation of Thr-538 occurs in response to TPA-activated PKCs in vitro, and this phosphorylation may contribute to dissolution of the actin cytoskeleton and redistribution of LFA-1 integrins in vivo.

Our Paxillin (Ser-83) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects rat, mouse Paxillin (Ser-83) and is antigen affinity purified. It is great for use in WB, ICC.

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.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

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.