Monoclonal Anti-Phosphotyrosine–Peroxidase antibody produced in mouse

As determined by ELISA and competitive ELISA, the antibody reacts specifically with phosphorylated tyrosine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated tyrosine, phosphothreonine, phosphoserine, AMP or ATP.

Monoclonal Anti-Phosphotyrosine (mouse IgG1 isotype) is derived from the PT-66 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a phosphotyrosine-BSA conjugate.

phosphotyrosine conjugated to BSA

Monoclonal Anti-Phosphotyrosine-Peroxidase antibody has been used in

• enzyme linked immunosorbent assay (ELISA)
• dot blot
• Chemiluminescence dot blot
• kinase assay

Mouse anti-phosphotyrosine-peroxidase antibody reacts specifically with phosphorylated tyrosine coupled to BSA. The product has shown no reactivity for other phosphorylated amino acids like phosphothreonine and phosphoserine.

Reversible phosphorylation of proteins is an important post-translational modification that plays a regulatory role in the expression of most proteins in the cells. Reversible phosphorylation at multiple serine, tyrosine and threonine residues mediates numerous signalling pathways in both prokaryotic and eukaryotic cells . Cellular proteins with phosphorylated tyrosine increase many fold by the activation of tyrosine kinases. Most mitogenic receptor systems such as EGF, PDGF, insulin receptors contain serine/threonine/tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. Monoclonal anti-phosphotyrosine–peroxidase antibody can be used in kinase assay to visualize the fraction of phosphorylated substrate.

Lyophilized from a solution containing 1% bovine serum albumin and 0.05% MIT in 0.01 M sodium phosphate buffered saline.

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