Monoclonal Anti-Phosphothreonine antibody produced in mouse

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.

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.

phosphothreonine conjugated to keyhole limpet hemocyanin (KLH).

Monoclonal Anti-Phosphothreonine antibody produced in mouse has been used in:immunoblotting, enzyme linked immuno sorbent assay (ELISA) ,dot blot.

Monoclonal and polyclonal antibodies directed against phosphorylated residues may be useful as analytical and preparative tools, by enabling the identification, quantification and immunoaffinity isolation of phosphorylated cellular proteins. Antibodies can be employed to monitor alterations in phosphorylation of specific proteins as they occur in intact organs or even whole animals.
Mouse monoclonal clone PTR-8 anti-phosphothreonine antibody may be used for the localization of phosphorylated threonine using various immunochemical assays such as ELISA, dot blot, and immunoblotting. Due to steric hindrance of the recognition site, this antibody may not recognize certain proteins known to contain phosphorylated threonine.

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.

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.

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