Technical Data
FAK (Focal Adhesion Associated Protein Tyrosine Kinase, BC3)
Focal adhesion kinase (FAK) is a widely expressed cytoplasmic protein tyrosine kinase involved in integrin-mediated signal transduction. It plays an important role in the control of several biological processes, including cell spreading, migration and survival (1). Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397, which is a binding site for Src family kinases (2,3), PI3K and PLCg (4,5). The recruitment of Src family kinases results in the phosphorylation of tyrosine residues 407, 576 and 577 in the catalytic domain, and tyrosine residues 871 and 925 in the carboxy-terminal region of FAK (6,7).

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, 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
100ul-20CBlue IceHumanRabbit
Not determined
Synthetic peptide (KLH-coupled) corresponding to residues surrounding amino acid residue 710 of human FAK.
Purified by Protein A and immunoaffinity chramotography.
Supplied as a liquid in 10mM sodium HEPES, pH 7.5,, 150 mM NaCl, 100ug/ml BSA and 50% glycerol.
Detects endogenous levels of FAK protein. Does not crossreact with other proteins.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
(1) Parsons, J. T. et al. (2000) Oncogene 19: 56065613. (2) Schaller, M. D. et al. (1994) Mol. Cell. Biol. 14: 16801688. (3) Cobb, B. S. et al. (1994) Mol. Cell. Biol. 14: 147155. (4) Chen, H. C. et al. (1996) J. Biol. Chem. 271: 2632926334. (5) Zhang, X. et al. (1999) Proc. Natl. Acad. Sci. USA 96: 90219026.
(6) Calalb, M. B. et al. (1995) Mol. Cell. Biol. 15: 954963. (7) Schlaepfer, D. D. et al. (1994) Nature 372: 786791.