Recombinant Src protein, active

The proto-oncogene tyrosine-protein kinase Src is a non-receptor protein tyrosine protein kinase that is involved in different signal transduction pathways that regulate such vital cellular processes as cell-cell interactions, cell migration, transcription and proliferation through the phosphorylation of many substrates. It is one of eight members of the Src family of non-receptor tyrosine kinases (Src, Fyn, Yes, Lck, Lyn, Hck, Fgr and Blk) that interact with the intracellular domains of growth factor/cytokine receptors, GPCRs and integrins. Members of the Src kinase family have a very similar domain structure with a high degree of homology in the SH1 (catalytic), linker, SH2 (p-Tyr binding), SH3 (protein-protein interaction) and SH4 (membrane association) domains. c-Src, Fyn and Yes are ubiquitously expressed, although high levels of c-Src are found in platelets, neural tissue and osteoclasts. The activity of the Src kinase family can also be regulated by phosphatases (e.g. SHP1), binding to adaptor proteins (e.g. CBP) and proteasomal degradation. Src kinases are key upstream mediators of both the PI 3-K and MAPK signaling pathways, and have been shown to have important roles in cell proliferation, migration and survival.