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Focal adhesion kinase 1 (FAK1) is a non-receptor tyrosine kinase and adaptor protein.1,2 It is composed of an N-terminal FERM domain, a proline-rich region, a catalytic domain, two additional proline-rich regions, and a C-terminal focal adhesion-targeting (FAT) domain, which can also be autonomously expressed as FAK-related nonkinase (FRNK) and act as an inhibitor of FAK activity.3,4 FAK is ubiquitously expressed and localizes to focal adhesion sites at the plasma membrane, as well as the cytoplasm and nucleus.2,3,5 It is activated by autophosphorylation of Tyr397, which recruits c-Src to initiate signaling through PI3K/Akt or MAPK/ERK pathways, and is involved in integrin signaling, cell adhesion, migration, and survival.1,2 Overexpression of FAK is associated with various cancers and metastasis.6,1 Cayman’s FAK1 Rabbit Monoclonal Antibody (Clone RM472) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Signal transduction mechanisms of focal adhesions: Src and FAK-
2. Focal adhesion kinase: In command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6(1), 56-68 (2005).
3. Focal adhesion signaling in heart failure. Pflugers Arch. 466(6), 1101-1111 (2014).
4. FRNK inhibition of focal adhesion kinase-
5. Direct interaction of the N-
6. Focal adhesion kinase: Targeting adhesion signaling pathways for therapeutic intervention. Clin. Cancer Res. 14(3), 627-632 (2008).