Focal adhesion kinase was initially identified as a major substrate for the intrinsic protein tyrosine kinase activity of Src encoded pp60. The deduced amino acid sequence of FAK p125 has shown it to be a cytoplasmic protein tyrosine kinase whose sequence and structural organization are unique as compared to other proteins described to date. Localization of p125 by immunofluorescence suggests that it is primarily found in cellular focal adhesions leading to its designation as focal adhesion kinase (FAK). FAK is concentrated at the basal edge of only those basal keratinocytes that are actively migrating and rapidly proliferating in repairing burn wounds and is activated and localized to the focal adhesions of spreading keratinocytes in culture. Thus, it has been postulated that FAK may have an important in vivo role in the reepithelialization of human wounds. FAK protein tyrosine kinase activity has also been shown to increase in cells stimulated to grow by use of mitogenic neuropeptides or neurotransmitters acting through G protein-coupled receptors.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
PTK2 (phospho-S722) polyclonal antibody detects endogenous levels of PTK2 protein only when phosphorylated at Ser722 .
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