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     Western blot analysis of Phospho-FAK (Tyr576) in A549, U251, C2C12 lysates using Phospho-FAK (Tyr576) antibody.    

  
  

Phospho-FAK (Tyr576) antibody detects the activated form of Focal Adhesion Kinase (FAK), a cytoplasmic tyrosine kinase critical for regulating cell adhesion, migration, and survival. FAK integrates signals from integrins and growth factor receptors, promoting downstream pathways like RAS-MAPK and PI3K-AKT. Its activation involves autophosphorylation at Tyr397. which recruits SRC-family kinases to phosphorylate additional residues, including Tyr576/577 in the kinase domain’s activation loop. Phosphorylation at Tyr576 enhances FAK’s catalytic activity and stabilizes its interaction with substrates, driving cellular processes like cytoskeletal remodeling and focal adhesion turnover.

This antibody specifically recognizes FAK when phosphorylated at Tyr576. serving as a key tool to study FAK activation dynamics in physiological contexts (e.g., embryonic development, wound healing) and pathological conditions (e.g., cancer metastasis, fibrosis). It is widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess FAK signaling activity in cell lines, tissues, or disease models. Researchers also employ it to evaluate therapeutic responses to FAK inhibitors or to explore FAK’s role as a biomarker in tumors. Validation often includes testing in FAK-deficient cells or using phosphorylation-blocking mutants to ensure specificity. Understanding FAK activation via Tyr576 phosphorylation provides insights into mechanisms underlying cell motility and potential targets for anti-cancer therapies.