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.
Ishibe, S. et al. (2004) Mol. Cell 16 :257-267.
*For more information, see UniProt Accession Q8VI36
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Fan, Y. et al. (2018) Front Cell Neurosci. 12:309. (WB: mouse BV2 microglia)
Fuste, NP et al. (2016) Nat Commun. 7:11581. (WB/ICC/IHC: rat tumor cells)
Wu, D. W. et al. (2014) Oncogene 33(35): 4385. (WB: CCM3 cells)
Lee, S. et al. (2013) Biochim Biophys Acta. 1830(8):4017. (WB: rat C6 and human U373 gliomas)
Sen, A. et al. (2012) J Clin Invest. 122(7):2469. (WB, ICC: C4C2, PC3, LNCaP, )
Kwak, T.K. et al. (2010) J Biol Chem. 285(46):36021. (WB: pancreatic INS-1 cells)
Sen, A. et al. (2010) J Biol Chem. 285(37):28787. (WB: human LNCAP cells)
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