The role of tyrosine phosphorylation in transduction of the mitogenic signal from transmembrane receptors and in transformation by oncogene tyrosine kinases has been the subject of intense investigation for several years. While the phosphorylation of specific tyrosine residues has been shown to be a primary mechanism of signal transduction during normal mitogenesis, cell cycle progression and oncogenic transformation, its role in other areas such as differentiation and gap junction communication, is a matter of active and ongoing research. Antibodies that specifically recognize phosphorylated tyrosine residues have proved to be invaluable to the study of tyrosine-phosphorylated proteins biochemical pathways in which they function.

This antibody is known to be inhibited by divalent cations (>1mM) and high salt concentrations (>0.2M).

The purified antibody is coupled through free primary amino groups to biotin. The binding site of the antibody was protected by the addition of phenyl phosphate prior to coupling.

Source: Hybridoma produced from Balb/C mice immunized with phosphotyrosine coupled to carrier protein.