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Many cellular proteins are regulated by post-translational phosphorylation and dephosphorylation. Covalent modification by phosphorylation often serves as a molecular switch for cell regulatory and signal transduction events. In eukaryotic cells, reversible modification of proteins by phosphorylation occurs at specific tyrosine, serine and/or threonine amino acid residues. Monoclonal antibodies specific for phosphotyrosine, phosphoserine and phosphothreonine are important tools for studying protein phosphorylation. These antibodies, alone or conjugated to biotin or agarose, are useful for the detection, identification and purification of proteins containing specific phosphorylated amino acids.
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