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Merck
모든 사진(1)

주요 문서

P9109

Sigma-Aldrich

Monoclonal Anti-Protein Tyrosine Phosphatase PEST antibody produced in mouse

clone AG25, purified immunoglobulin

동의어(들):

Anti-PTP PEST

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About This Item

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

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

AG25, monoclonal

분자량

antigen 88 kDa

종 반응성

mouse, human, bovine, rat

기술

immunoprecipitation (IP): suitable
western blot: suitable

동형

IgG1

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

유전자 정보

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

일반 설명

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).

면역원

full-length, recombinant PTP PEST.

애플리케이션

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

물리적 형태

Solution in phosphate buffered saline containing 0.08% sodium azide.

제조 메모

Purified from tissue culture supernatant using Protein G.

면책조항

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


시험 성적서(COA)

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문서 라이브러리 방문

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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