Anti-Paxillin/PXN Antibody Picoband®

PXN (Paxillin) is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge. Salgia et al. (1995) mapped the paxillin 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 association with the cytoplasmic tail of beta-integrin. The N-terminal region of paxillin 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 paxillin protein contains 4 LIM domains, a proline-rich domain containing a consensus SH3-binding site, and 3 potential SH2-binding sites. On Northern blots, paxillin was expressed as a 3.7-kb mRNA in all tissues tested.

1. Fernandez-Valle, C., Tang, Y., Ricard, J., Rodenas-Ruano, A., Taylor, A., Hackler, E., Biggerstaff, J., Iacovelli, J.Paxillin binds schwannomin and regulates its absorbance-dependent localization and effect on cell morphology.Nature Genet. 31: 354-362, 2002. 2. Salgia, R., Li, J.-L., Lo, S. H., Brunkhorst, B., Kansas, G. S., Sobhany, E. S., Sun, Y., Pisick, E., Hallek, M., Ernst, T., Tantravahi, R., Chen, L. B., Griffin, J. D.Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210 (BCR/ABL) .J. Biol. Chem. 270: 5039-5047, 1995. 3. Turner, C. E., Glenney, J. R., Jr., Burridge, K.Paxillin: a new vinculin-binding protein present in focal adhesions.J. Cell Biol. 111: 1059-1068, 1990.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.