The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation.
Polyclonal antibodies are produced by immunizing animals with a constructed phosphopeptide agnate to residues surrounding Tyr397 of animal FAK. Antibodies are antiseptic by protein A and peptide affection chromatography.
Focal adherence kinase (FAK) is a broadly bidding cytoplasmic protein tyrosine kinase complex in integrin-mediated arresting transduction. It plays an important role in the ascendancy of several biological processes, including corpuscle spreading, migration, and adaptation. Activation of FAK by integrin absorption leads to autophosphorylation at Tyr397, which is a bounden website for the Src ancestors kinases PI3K and PLCγ. Recruitment of Src ancestors kinases after-effects in the phosphorylation of Tyr407, Tyr576, and Tyr577 in the catalytic domain, and Tyr871 and Tyr925 in the carboxy-terminal arena of FAK.
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