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.

The Src gene family is represented by at least eight different protein tyrosine kinases that belong to the non-receptor tyrosine kinase family. These protein tyrosine kinases are important regulators of many cellular processes, including cytoskeletal organization, cell-cell contact, DNA synthesis and cellular proliferation. Members of this group of proteins include c-Src, c-Yes, Fyn, Lck, Lyn, Hck, Blk and c-Fgr. The proto-oncogene c-Src is the prototype member of this gene family and is expressed in a broad range of tissues and cells. Elevated c-Src tyrosine kinase activity has been found in many types of human cancers, most notably in breast carcinomas.

The activity of Src family tyrosine kinase (SFK) is determined by an equilibrium between an inactive (phosphorylated) and a primed (dephosphorylated) state regulated by a balance of Csk (C-terminal Src kinase) and its counteracting tyrosine phosphatase(s). Upon cell stimulation, SFKs at a primed state become functionally activated to relay signals into the cells. Thus, perturbation of the equilibrium status of SFK may greatly affect the sensitivity of the cells to extracellular cues.

There are two tyrosine phosphorylation sites with opposing effects in Src. Tyrosine 418 is located in the catalytic SH2 domain and is one of the autophosphorylation sites. Phosphorylation of Tyr418 upregulates the enzyme while phosphorylation of Tyr529 in the C-terminal tail by Csk renders the enzyme less active. SFKs are required for EGF-, PDGF- and CSF-1-stimulated entry to the S-phase of the mitotic cycle in fibroblasts. Similarly, they are activated at mitosis and play a role in cellular division at the G2-M transition phase. Activated c-Src can increase tyrosine phosphorylation of paxillin and is involved in the activation of the Ras/ERK pathway.

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