Each antibody in the FAK Antibody Sampler Kit detects endogenous levels of its target protein and does not typically cross react with other proteins. Activation state antibodies recognize target proteins only when phosphorylated at the indicated residue. Phospho-FAK (Tyr397) Antibody may cross-react with overexpressed tyrosine phosphorylated EGF receptors.
Source / Purification
Activation state polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Tyr397, Tyr576/577 and Tyr 925 of human FAK protein. FAK Antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding amino acid 710 of human FAK protein. Antibodies are purified by protein A and peptide affinity chromatography.
Description
The FAK Antibody Sampler Kit provides an economical means of evaluating total FAK protein levels as well as FAK phosphorylated at specific sites. The kit contains enough primary and secondary antibody to perform four western blots with each antibody.
Background
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 the Src family kinases PI3K and PLCγ (2-5). Recruitment of Src family kinases results in the phosphorylation of Tyr407, Tyr576, and Tyr577 in the catalytic domain, and Tyr871 and Tyr925 in the carboxy-terminal region of FAK (6,7).