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FAK, phosphorylated (Tyr397) (Focal Adhesion Associated Protein Tyrosine Kinase, BC3)

Cat no: F0019-57H


Supplier: United States Biological
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Focal adhesion kinase (FAK) is a non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis (1). FAK is composed of a central catalytic domain flanked by large N- and C-terminal regions. FAK is activated by phosphorylation at tyrosine 397 in response to integrin clustering which can be induced by cell adhesion or antibody cross-linking or via G-protein-coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid (2-3). Phosphorylation of FAK Tyr-397 creates a binding site for Src-family kinases, and phosphorylation of FAK Tyr-576/Tyr-577 in the kinase domain activation loop enhances catalytic activity (4). Increased FAK expression has been correlated with the enhanced motility and invasiveness of human tumor cells, as well as with promoting increased cell proliferation. Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilutions: Western Blot: 1:1000-2000 Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. Manufactured incorporating RabMAb(R) technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
Catalogue number: F0019-57H
Reactivities: Human, Rat
Hosts: Rabbit
Applications: Western Blot
Size: 100ul
Form: Supplied as a liquid in 50mM Tris-glycine, pH 7.4, 0.15M sodium chloride, 40% glycerol, 0.01% sodium azide, 0.05% BSA.
P type: Mab
Isotype: IgG
Purity: Supernatant
References: 1. Schaller, M.D. (2001) Biochim. Biophys. Acta 1540, 1
Additional info: Recognizes FAK phosphorylated at Tyr397.

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