Phospho-L-Tyrosine Disodium Salt
In molecular and cell biology research, Phospho-L-Tyrosine Disodium Salt is used to probe protein-protein interactions, particularly between phosphotyrosine-containing peptides/proteins and SH2 (Src homology 2) domain-containing proteins (e.g., Grb2, PI3K), helping elucidate molecular recognition mechanisms in signal transduction. In structural biology, it serves as a ligand in X-ray crystallography or NMR studies to determine the 3D structure of phosphotyrosine-binding proteins (e.g., phosphatases, SH2 domain proteins), providing atomic-level insights into substrate recognition. It is also applied in functional validation of phosphorylation sites: through site-directed mutagenesis, it mimics constitutive phosphorylation at specific tyrosine residues in target proteins, allowing researchers to compare the activity of wild-type vs. phosphomimetic mutants and confirm the functional significance of individual phosphorylation sites (e.g., in enzyme activation or protein localization).
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