Focal Adhesion Kinase (FAK) is a non-receptor protein tyrosine kinase that is expressed ubiquitously. FAK is the critical in forming cell-substratum adhesions or focal adhesion complexes. FAK reportedly has multiple phosphorylation sites. Autophosphorylation of FAK at Tyr397 creates a binding site on FAK for Src-family kinases and is critical for maximum adhesion and migration responses. The phosphorylation of Tyr407 and Tyr861 is induced during epithelial-mesenchymal transition and further augmented during cell migration. FAK activation couples signal transduction via PI3K, CAS and Src. FAK signaling is involved in multiple functions such as proliferation, migration, survival and angiogenesis. Disruption of FAK signalling results in failure of adhesion to the substratum and anoikis (apoptosis) of epithelial cells which are anchorage dependent. FAK has been observed to be upregulated in human tumors such as neuroblastoma and is related to tumor cell survival and prognosis Anti-phospho-FAK (pTyr407) recognizes FAK (Focal Adhesion Kinase) phosphorylated at tyrosine 407 (125 kDa).
Immunogen
synthetic phosphopeptide derived from the region of FAK that contains tyrosine 407.
Application
A starting dilution of 1:1000 is suitable for detection of FAK phosphorylated at tyrosine 407 by immunoblotting.
Physical form
Solution in Dulbecco′s phosphate buffered saline (without magnesium and calcium), pH 7.3 (+/- 0.1), 50% glycerol with 1.0 mg/mL bovine serum albumin (IgG, protease free) as a carrier and 0.05% sodium azide as a preservative.
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