The antibody detects endogenous level of FAK only when phosphorylated at tyrosine 576/577.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
Peptide sequence around phosphorylation site of pTyr 576, pTyr577 (S-T-Y (p) -Y (p) -K-A) derived from Human FAK. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
Western blotting: 1:500-1:1000 Immunofluorescence: 1:100-1:200
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C/-20 °C
Storage Comment
Store at -20 °C for long term preservation (recommended). Store at 4 °C for short term use.
Ruan, Liu, Zhang, Yan, Fan, Shen, Wang, Zheng, Wang, Lu: "Luteolin reduces the invasive potential of malignant melanoma cells by targeting ?3 integrin and the epithelial-mesenchymal transition." in: Acta pharmacologica Sinica, Vol. 33, Issue 10, pp. 1325-31, (2012) (PubMed).
Zheng, Wei, Wang, Gong, Zhang: "Surface characterization and cytocompatibility of three chitosan/polycation composite membranes for guided bone regeneration." in: Journal of biomaterials applications, Vol. 24, Issue 3, pp. 209-29, (2009) (PubMed).
Target
FAK (PTK2)
(PTK2 Protein tyrosine Kinase 2 (PTK2))
Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity.