C-Src (Tyr-215) [conserved site], Phosphospecific Antibody

C-Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family is composed of nine members in vertebrates, including c-Src, Yes, Fgr, Yrk, Fyn, Lyn, Hck, Lck, and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility, and adhesion. Src-family kinases contain an N-terminal cell membrane anchor followed by SH3 and SH2 domains. The activity of c-Src is regulated by tyrosine phosphorylation at multiple sites. Tyrosine 418 is autophosphorylated following c-Src activation. Tyrosine 215 in the SH2 domain of c-Src is phosphorylated following growth factor receptor activation. Both Tyr-215 and Tyr-418 phosphorylation increases tyrosine kinase activity, while phosphorylation of Tyr-530 downregulates c-Src kinase activity. Thus, tyrosine phosphorylation of c-Src is critical for regulating its kinase activity.

This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose then Affinity purification using phospho-c-Src (Tyr-215) peptide (without carrier) . The antibody detects a 60 kDa* protein on SDS-PAGE immunoblots of mouse SYF cells transformed with c-Src and human A431 cells that have been treated with pervanadate. This sequence has homology to the conserved site in other Src family members, such as hck, fyn, csk, and yes.