Species: All-Multi
Applications: WB, ICC/IF
Host: Rat Monoclonal
Species: All-NA
Applications: WB, Flow, ICC/IF, IHC, IP
Host: Mouse Monoclonal
Species: All-NA
Applications: WB, Flow, ICC/IF, IHC, IP
Host: Mouse Monoclonal
Description
Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a
protein's activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various
specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine; others act on
tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple
sites on any given protein, it can therefore change the function or localization of that protein at any time (1). Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes,
heart disease, inflammation and neurological disorders (2-4). In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity (5). Phosphotyrosine can be detected
through specific antibodies, and are helpful in facilitating the
identification of tyrosine kinase substrates (6).
Bioinformatics
| Alternate Names |
- 2 amino 3(4 hydroxyphenyl) propanoic acid
- 4 hydroxyphenylalanine
- PhosphoTyrosine
- pTyrosine
- pY20
- Tyrosine
|