Anti-phospho-FAK (Tyr397) Antibody

Control
untransfected and Src-transfected RAT2 cell lysates

Evaluated by Western Blot in untransfected and Src-transfected RAT2 cell lysates.

Western Blot Analysis: A 1:1,000 dilution of this antibody detected phospho-FAK (Tyr397) in 10 µg of untransfected and Src-transfected RAT2 cell lysates.

Detect phospho-FAK (Tyr397) using this Anti-phospho-FAK (Tyr397) Antibody validated for use in WB, Cell Function Assay.

Peptide Inhibition Assay Analysis: A 1:1,000 dilution from a representative lot peptide blocked on RAT2 cells transfected with Src.

Research Category
Cell Structure

Research Sub Category
Adhesion (CAMs)

This antibody recognizes FAK phosphorylated at Tyr397.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Focal adhesion kinase (FAK) is a non receptor protein tyrosine kinase discovered as a substrate for Src and a key element in integrin signaling. FAK plays a central role in cell spreading, differentiation, migration, cell death and acceleration of the G1 to S phase transition of the cell cycle. FAK regulation includes phosphorylation at multiple tyrosine and serine residues. Phosphorylation of tyrosine is generally associated with positive regulation and growth promotion; however, dephosphorylation at these sites occurs as cells enter mitosis (M-Phase). In contrast, serine phosphorylation either remains high or is increased as cells enter mitosis and may play a role in focal adhesion disassembly. FAK and its phosphorylation states have been implicated in cancer metastasis, tumor cell survival, and adhesion-independent growth. Recent evidence indicates that elevation of FAK activity in human carcinoma cells is associated with increased invasive potential. A central role in tumor formation and progression suggests that FAK is an attractive target for therapeutic intervention. Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397.

~125 kDa observed.
An uncharacterized band appears at ~190 kDa in some lysates.

Epitope: Phosphorylated Tyr397

KLH-conjugated linear peptide corresponding to human FAK phosphorylated at Tyr397.

Replaces: 04-974

Affinity purified

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.