P9109
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
conjugate:
unconjugated
application:
IP
WB
WB
clone:
AG25, monoclonal
species reactivity:
mouse, human, bovine, rat
citations:
2
technique(s):
immunoprecipitation (IP): suitable
western blot: suitable
western blot: suitable
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).
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
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
A Gjörloff-Wingren et al.
European journal of immunology, 30(8), 2412-2421 (2000-08-15)
A high protein tyrosine phosphatase (PTPase) activity is required to maintain circulating T lymphocytes in a resting phenotype, and to limit the initiation of T cell activation. We report that 15 of the currently known 24 intracellular PTPases are expressed
M F Gebbink et al.
The Journal of biological chemistry, 268(22), 16101-16104 (1993-08-05)
Receptor-like protein tyrosine phosphatases (receptor-PTPs) represent a novel family of transmembrane proteins that are thought to play important roles in cellular regulation. They consist of a cytoplasmic catalytic region, a single transmembrane segment and an extracellular, putative ligand-binding domain, but
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
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