c-Src (Tyr-215)[conserved site], phospho-specific polyclonal, anti-human, mouse, rat

Background:
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.

Immunogen: c-Src (Tyr-215) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 215 of human c-Src. This sequence has homology to the conserved site in other Src family members, such as hck, fyn, csk, and yes.

Specificity: This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose then affinity purified 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.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.