Paxillin antibody [PXC-10]

Cellular adhesion to the extracellular matrix is critically involved in many processes including normal and transformed cell growth, migration, metastasis, lymphocyte extravasation and also in force transmission during muscle contraction. Paxillin (68 kDa), is a cytoskeletal component found in the focal adhesions at the ends of actin stress fibers, but not in adherens junctions of the cells. Paxillin interacts with several proteins including members of the src family of tyrosine kinases, the transforming protein v-crk, the cytoskeletal protein vinculin, and the tyrosine kinase, focal adhesion kinase (FAK). This interaction has suggested a function for paxillin as a molecular adaptor, responsible for the recruitment of structural and signaling molecules to focal adhesions. The paxillin molecule has a single binding site for vinculin, and at least two binding sites for FAK, that are separated by an intervening sequence of 100 amino acids. Upon transformation by RSV, 20-30% of the paxillin molecules are phosphorylated on tyrosine. In addition, the cellular distribution of paxillin becomes more diffuse, suggesting that phosphorylation of paxillin may have a role in the disassembly of focal adhesions and stress fibers during transformation. The availability of monoclonal antibody reacting specifically with paxillin enables the subcellular detection and localization of paxillin.