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P9109

Sigma-Aldrich

Monoclonal Anti-Protein Tyrosine Phosphatase PEST antibody produced in mouse

clone AG25, purified immunoglobulin

Synonym(s):

Anti-PTP PEST

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

AG25, monoclonal

mol wt

antigen 88 kDa

species reactivity

mouse, human, bovine, rat

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... PTPN12(5782)
mouse ... Ptpn12(19248)
rat ... Ptpn12(117255)

General description

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).

Immunogen

full-length, recombinant PTP PEST.

Application

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

Physical form

Solution in phosphate buffered saline containing 0.08% sodium azide.

Preparation Note

Purified from tissue culture supernatant using Protein G.

Disclaimer

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.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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David Taieb et al.
Cancer research, 68(12), 4588-4596 (2008-06-19)
The poor prognosis of pancreatic cancer is due to rapid locoregional invasion, the early development of metastases, and the limited efficacy of current therapies. To date, none of the identified oncogenes and suppressors involved in this disease have led to
Rosario Espejo et al.
Journal of cell science, 127(Pt 3), 497-508 (2013-11-29)
Tyrosine phosphorylation is implicated in regulating the adherens junction protein, p120 catenin (p120), however, the mechanisms are not well defined. Here, we show, using substrate trapping, that p120 is a direct target of the protein tyrosine phosphatase, PTP-PEST, in epithelial

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