Monoclonal Anti-Protein Tyrosine Phosphatase μ antibody produced in mouse

Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. The protein phosphatases can be divided into two main groups: protein tyrosine phosphatases (PTPs) and protein serine/threonine phosphatases (PPs) which remove phosphate from proteins/peptides containing phosphotyrosine (pTyr) or phosphoserine/phosphothreonine (pSer/pThr), respectively. Several of the PTPs are known to control the function of growth factor receptors, many of which are tyrosine kinases encoded by oncogenes. PTPmu participates in homophilic binding of extracellular surface of adjacent cells. PTPmu is reported to be downregulated in glioblastoma in which it regulates cell migration and growth factor-independent survival
Monoclonal Anti-Protein Tyrosine Phosphatase mu recognizes PTPmu isoforms in all mammalian species.

peptide corresponding to amino acid residues 42-60 of PTPμ.

Anti-protein tyrosine phosphatase mu may be used for detection by immunoblotting at a working concentration of 1 to 10 μg/mL. The antibody is suitable for immunoprecipitation.

Solution in phosphate buffered saline with 0.08% sodium azide.

Purified from tissue culture supernatant using Protein G.