Anti-Src Antibody, clone N6L, rabbit monoclonal

pp60c-Src is the prototype non-receptor tyrosine kinase. Homology to Src in three regions is shared by a number of proteins: SH1 being the catalytic domain, SH2 being a phospho-tyrosine binding domain, and SH3 being a proline-binding domain. The Src SH2 domain binds to phospho-Tyr527 (phosphorylated by Csk) within the Src molecule, causing Src to adopt an inactive conformation. Mutation of Tyr527 to phenylalanine removes the SH2-binding target and results in a constitutively active kinase. A second mutation at the conserved lysine residue at the ATP-binding site abolishes kinase activity, but without Tyr527, the conformation of the protein is open, allowing interaction with endogenous activators. Consequently, this double-mutant exhibits a dominant-negative phenotype