Anti-Paxillin

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge. Salgia et al.(1995) mapped the gene to 12q24 using fluorescence in situ hybridization.The C-terminal region of Paxillin contains four LIM domains that target paxillin to focal adhesions, it is presumed through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal region is rich in protein-protein interaction sites. The proteins that bind to Paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT. Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk. The protein contains 4 LIM domains, a proline-rich domain containing a consensus SH3-binding site, and 3 potential SH2-binding sites. Protein function: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). [The UniProt Consortium]