Description_x000D_ General description_x000D_ As determined by ELISA and dot blot, the antibody reacts specifically with phosphorylated threonine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated threonine, phosphoserine, phosphotyrosine, AMP or ATP. This antibody has been used in immunoblotting for the localization of some phosphothreonine-containing proteins. Certain proteins known to contain phosphorylated threonine may not be recognized by this antibody due to steric hindrance of the recognition site._x000D_ Monoclonal Anti-Phosphothreonine (mouse IgG2b isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse._x000D_ Immunogen_x000D_ phosphothreonine conjugated to keyhole limpet hemocyanin (KLH)._x000D_ Application_x000D_ Monoclonal Anti-Phosphothreonine antibody produced in mouse has been used in:immunoblotting, enzyme linked immuno sorbent assay (ELISA) ,dot blot._x000D_ Mouse monoclonal clone PTR-8 anti-Phosphothreonine antibody reacts with phosphorylated threonine both as a free amino acid or when conjugated to carriers such as BSA or KLH, using ELISA and dot blot. It does not react with nonphosphorylated threonine, phosphorylated tyrosine or serine, AMP or ATP._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ 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 tenfold following various activation processes, which are mediated through phosphotyrosine, phosphoserine or phosphothreonine (p-Tyr/p-Ser/p-Thr). Many different mitogenic systems, such as the EGF, PDGF and insulin receptor systems, contain Tyr/Ser/Thr kinase domains that autophosphorylate specific Tyr/Ser/Thr residues upon binding of their ligands. T cell antigen receptor complex or receptors for some hemopoietic growth factors may stimulate associated kinases, and cells transformed by viral oncogenes contain elevated levels of phosphorylated Tyr/Ser/Thr. An understanding of transformation by oncogenes and mitogenic processes of growth factors depends on the identification of their substrate and a subsequent determination of how phosphorylation affects the properties of these proteins.