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c-Src (proto-oncogene tyrosine-protein kinase Src) is a 60 kDa tyrosine protein kinase that contains both SH2 and SH3 domains. c-Src is a lipid-modified signaling molecule (myristoylated) involved in cell-cell interactions, cell migration and proliferation through the phosphorylation of many substrates. c-Src is expressed at high levels in differentiated cells including neurons, platelets and macrophages, and can be activated by phospholipase D, insulin-like growth factor receptor, EGF-receptor, fibroblast growth factor receptor and prolactin receptor binding. c-Src can be phosphorylated on multiple sites to interact with polyoma virus middle T antigen, PYK2, HSP72 and caveolin, and efficient study methods are in high demand.
Figure 1: Measurement of phosphorylated and total c-Src.
A-431 cells were cultured in 96-well plates and serum-starved for 16 hours. Cells were then treated with 100 ng/ml EGF for 20 minutes and fixed. Total and phospho c-Src were each assayed in triplicate using the phospho and total c-Src antibodies included in the FACE c-Src Kit. Data was plotted after correction for cell number (performed through use of Crystal Violet).
Antibody Specificities
The phospho-c-Src antibody is specific for phosphorylated c-Src and was raised against a synthetic phospho-peptide corresponding to residues surrounding Tyr418 of human c-Src. This antibody recognizes c-Src when phosphorylated at this site and also recognizes Fyn and c-Yes. The total-c-Src antibody recognizes c-Src proteins regardless of the phosphorylation state.
