Protein tyrosine residues are phosphorylated as a result of intracellular protein kinase activation (e.g. via growth factors) during normal growth and development, and in oncogenesis. The most abundant population of target proteins for tyrosine phosphorylation are cell surface glycoproteins. Antibody to phosphotyrosine enables the detection, isolation and characterization of proteins containing phosphotyrosine. PY20 also prevents internalization of activated receptors, e.g. EGFr, when microinjected into cells. The affinity of PY20 for phosphotyrosine is approximately 10-6 to 10-7 M. PY20 binding to phosphorylated tyrosines can be inhibited by free phosphotyrosine and phenylphosphate, but not by phosphoserine, phosphothreonine or free phosphate.1-3
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