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Focal adhesion kinase (FAK) is a widely expressed non-receptor cytoplasmic tyrosine kinase that is implicated in integrin-mediated signal transduction. FAK plays an important role in the control of several biological processes, including cell spreading, migration and survival. Physical interactions of FAK with the integrin cytoplasmic domain and cytoskeletal proteins talin, paxillin and/or tensin play a key role in FAK activation by facilitating its oligomerization and transphosphorylation. FAK shows a rapid increase in tyrosine phosphorylation when stimulated by diverse signaling molecules, including those that regulate embryonic development, cell proliferation, migration and apoptosis, and efficient study methods are in high demand.
Figure 1: Measurement of phosphorylated and total FAK.
NIH/3T3 cells were cultured in 96-well plates and serum-starved for 16 hours. Cells were then treated with 50 ng/ml of PDGF for 5 minutes and fixed. Total and phospho FAK were each assayed in triplicate using the phospho and total FAK antibodies included in the FACE FAK Kit. Data was plotted after correction for cell number (performed through use of Crystal Violet).
Antibody Specificities
The phospho-FAK antibody is specific for phosphorylated FAK and was raised against a synthetic phospho-peptide corresponding to residues surrounding tyrosine 397 of human FAK. This antibody recognizes FAK only when phosphorylated at tyrosine 397. It does not cross-react with related kinases. The total-FAK antibody recognizes FAK proteins regardless of the phosphorylation state.
