Technical Data
Paxillin, phosphorylated, Tyr118 (PXN)
Paxillin is a multi-domain protein that localizes primarily to focal adhesion sites to the extracellular matrix (1). Paxillin is one of the key components of integrin signaling and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at tyrosine 118 (3,4). Phospho-Tyr118 may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).

Suitable for use in ELISA, Western Blot and Immunofluorescence. Other applications have not been tested.

Recommended Dilution:
Western Blot: 1:1000.
Immunofluorescence (IC): 1:50
Optimal dilutions to be determined by researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
100ul4C (-20C Glycerol)Blue IceHumanRabbit
Not determined
Synthetic phosphopeptide corresponding to residues surrounding Tyr118 of human paxillin (KLH).
Purified by Protein A affinity chromatography.
Supplied as liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol. No preservative added.
Recognizes endogenous human paxillin only when phosphorylated at Tyr118 at ~68kD. Does not crossreact with other tyrosine phosphorylated proteins. Species Crossreactivity: mouse, rat and monkey.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Turner, C.E. (2000) J. Cell Sci. 113, 41394140. 2. Burridge, K. et al. (1992) J. Cell Biol. 119, 893903. 3. Bellis, S.L. et al. (1995) J. Biol. Chem. 270, 1743717441. 4. Bellis, S.L. et al. (1997) Biochem. J. 325, 375381. 5. Schaller, M.D. and Parsons, J.T. (1995) Mol. Cell. Biol. 15, 26352645.