Monoclonal Anti-Protein Tyrosine Phosphatase PEST antibody produced in mouse

full-length, recombinant PTP PEST.

Solution in phosphate buffered saline containing 0.08% sodium azide.

Purified from tissue culture supernatant using Protein G.

Anti-Protein Tyrosine Phosphatase PEST antibody is suitable for immunoblotting and immunoprecipitation.

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.

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. PTP PEST is a cytosolic protein tyrosine phosphatase which is ubiquitously expressed in mammalian tissues. PTP PEST is subject to regulation via phosphorylation of Ser39 by both protein kinase C and protein kinase A
Monoclonal Anti-Protein Tyrosine Phosphatase PEST recognizes PTP PEST isoforms in all mammalian species (88 kDa).