Phospho Tyrosine Antibody (YA5306)

Phospho Tyrosine is a Phosphotyrosine is a reversibly modified amino acid in proteins that acts as a strong hapten; antiphosphotyrosine antibodies (α-pTyr) are a straightforward method to detect protein phosphorylation, which can monitor phosphorylation at any tyrosine of a specific protein, but during detection, the identity of the detected proteins needs to be inferred from their size relative to markers, and more exact verification can be done by stripping the blot and reprobing with antibodies specific to potential target proteins. Phosphotyrosine phosphatases (PTPs) remove phosphate from phosphotyrosine and are regulated by mechanisms including inactivation via oxidation or S-nitrosylation of cysteine in their catalytic sites, localization through localization domains, regulation of enzyme turnover by PEST (proline, glutamic acid, serine, threonine-rich) domains, phosphorylation (serine-threonine phosphorylation is usually inhibitory, while the effect of tyrosine phosphorylation depends on the site, and phosphotyrosine can allosterically activate PTPs with SH2 domains), and inhibition of membrane-bound PTPs by dimerization. It regulates numerous intracellular signaling pathways by mediating protein-protein interactions, with SH2 domains and phosphotyrosine binding (PTB) domains being two classes of phosphotyrosine-binding domains. Since there is no genetic codon for phosphotyrosine, it is difficult to study phosphotyrosine-mediated binding interactions using DNA-encoded libraries, but in vitro phosphorylated phage-displayed peptide libraries can be used to isolate phosphotyrosine-containing peptide ligands for investigating the binding specificities of related domains.