Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

FAK Antibody #3285

Applications Reactivity MW (kDa) Source
W IHC-P H M R Pg B (C) 125 Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Pg=Pig  C=Chicken  B=Bovine
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

FAK Antibody detects endogenous levels of FAK protein. This antibody does not cross-react with other proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding amino acid 710 of human FAK. Antibodies are purified by protein A and peptide affinity chramotography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using FAK Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using FAK Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using FAK Antibody in thre presence of control peptide (left) or antigen-specific peptide (right).


Background

Focal adhesion kinase (FAK) is a widely expressed cytoplasmic protein tyrosine kinase involved in integrin-mediated signal transduction. It plays an important role in the control of several biological processes, including cell spreading, migration and survival (1). Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397, which is a binding site for the Src family kinases PI3K and PLCγ (2-5). Recruitment of Src family kinases results in the phosphorylation of tyrosine residues at 407, 576 and 577 in the catalytic domain, and tyrosine residues at 871 and 925 in the carboxy-terminal region of FAK (6,7).

  1. Parsons, J.T. et al. (2000) Oncogene 19, 5606-5613.
  2. Schaller, M.D. et al. (1994) Mol. Cell. Biol. 14, 1680-1688.
  3. Cobb, B.S. et al. (1994) Mol. Cell. Biol. 14, 147-155.
  4. Chen, H.C. et al. (1996) J. Biol. Chem. 271, 26329-26334.
  5. Zhang, X. et al. (1999) Proc. Natl. Acad. Sci. USA 96, 9021-9026.
  6. Calalb, M.B. et al. (1995) Mol. Cell. Biol. 15, 954-963.
  7. Schlaepfer, D.D. et al. (1994) Nature 372, 786-791.

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