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Paxillin, a focal adhesion protein, is a substrate for several tyrosine kinases such as src, FAK, and p120BRC/ABL. The tyrosine phosphorylation of paxillin is affected by conditions that change cell-cell adhesion. This is consisent with the possibility that paxillin is involved in the regulation of cell morphology. Additionally, because of its SH3 binding domain, paxillin associates tightly with FAK and Crk in an extracellular matrix-independent manner. Paxillin was initially detected in fibroblasts, and its phosphorylation may be important during neurite extension during differentiation. This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
