Protein phosphorylation and dephosphorylation are basic mechanisms for the modification of protein function in eukaryotic cells. Phosphorylation is a rare post-translational event in normal tissue, however, the abundance of phosphorylated cellular proteins increases several fold following various activation processes which are mediated through phosphotyrosine, phosphoserine or phosphothreonine (p-tyr/p-ser/p-thr). Many signal transduction pathways, such as the EGF, PDGF and insulin receptor systems, contain tyr/ser/thr kinase which phosphorylate specific tyr/ser/thr residues upon binding of ligands to their receptors. T cell antigen receptor complex or the receptors for some hemopoietic growth factors may stimulate these phosphorylation associated kinases, and cells transformed by viral oncogenes contain elevated levels of phosphorylated tyr/ser/thr.
Synonyms: p-Thr, pthr, phospho-threonine
Application: Immunocytochemistry Analysis: A representative lot of this antibody at 1:500 dilution detected phosphothreonine modification on Calyculin A/Okadaic Acid treated A431 cellsImmunohistochemistry Analysis: A representative lot of this antibody at 1:500 dilution detected phosphothreonine modification on human colon cancer tissueImmunoprecipitation Analysis: A representative lot of this antibody at 1:500 dilution immunoprecipitated phosphothreonine modified proteins from Calyculin A/Okadaic Acid treated A431 cell lysate
Other Notes: Concentration: Please refer to lot specific datasheet.