Src (human, recombinant)

Src is a non-receptor protein tyrosine kinase, and SRC, which encodes Src, is considered a protooncogene.¹ Src is composed of unique, SH3, SH2, linker, and SH1 protein tyrosine kinase domains, and a C-terminal regulatory tail. It is ubiquitously expressed with higher levels in the brain, osteoclasts, and platelets. Src is myristoylated at the N-terminus during biosynthesis, a modification which facilitates its attachment to membranes. It primarily localizes to the plasma membrane where it interacts with receptor tyrosine kinases involved in cell division, growth, migration, and survival, as well as to the perinuclear membranes, endosomes, and secretory vesicles. It exists in an autoinhibited state and is activated by receptor tyrosine kinases, such as PDGFR, autophosphorylation at tyrosine 419, dephosphorylation of negative regulatory residues, or certain mutations.^1,2 Src protein levels and activity are elevated in a variety of cancers and are positively correlated with the degree of malignancy.² An activating truncation mutation in SRC is associated with highly metastatic forms of colon carcinoma.² Cayman’s Src (human, recombinant) protein can be used for enzyme assay applications. This protein consists of 536 amino acids and has a calculated molecular weight of 86 kDa.

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1. Roskoski, R., Jr. Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors. Pharmacol. Res. 94, 9-25 (2015).

2. Bjorge, J.D., Jakymiw, A., and Fujita, D.J. Selected glimpses into the activation and function of Src kinase. Oncogene 19(49), 5620-5635 (2000).