A number of cytoskeletal proteins are tyrosine phosphorylated in Rous sarcoma virus-transformed chick embryo fibroblasts. One of these is the 68 kDa paxillin protein. Paxillin is a cytoskeletal component that localizes to the focal adhesions at the ends of actin stress fibers. It is also present in the focal adhesions of Madin-Darby canine kidney epithelial cells, but is absent from the cell adherens junctions of these cells. Paxillin purified from chicken gizzard migrates as a diffuse band on SDS-PAGE with molecular weight of 65-70 kDa. It binds to the rod domain of vinculin, another focal adhesion protein. It is thought that phosphorylation of paxillin may have a role in that disassembly of focal adhesions and stress fibers during transformation.
This antibody is routinely tested by immunofluoresence microscopy. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.