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SRP5073

Sigma-Aldrich

PTPN12 (1-355), active, GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

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Synonym(s):
PTPG1, tcag7.1075
NACRES:
NA.32

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

2520-3410 nmol/min·mg

mol wt

~66 kDa

NCBI accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PTPN12(5782)

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This Item
SAB1406346SRP5074SRP5072
specific activity

2520-3410 nmol/min·mg

specific activity

-

specific activity

2040-2760 nmol/min·mg

specific activity

507-687 nmol/min·mg

assay

≥70% (SDS-PAGE)

assay

-

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

form

buffered aqueous solution

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

recombinant

expressed in E. coli

storage temp.

−70°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−70°C

General description

Protein tyrosine phosphatase-PEST (PTPN12), a ubiquitously expressed cytoplasmic tyrosine phosphatase, is thought to play an important role in cell adhesion and motility, cell migration, and signal transduction for antigen receptors in B and T lymphocytes. Signal transduction via tyrosine phosphorylation, normally fine-tuned by the concerted action of both protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is a key mechanism in tumorigenesis. Studies suggest potential role for PTP-PEST in regulation of p130(cas) in mitogen- and cell adhesion-induced signaling events.

Physical form

Supplied in 20mM MOPS, pH 7.5, 50mM NaCl, 10mM glutathione, 0.25mM DTT, 0.1mM PMSF, 30% glycerol.

Preparation Note

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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A J Garton et al.
Molecular and cellular biology, 16(11), 6408-6418 (1996-11-01)
PTP-PEST is a ubiquitously expressed, cytosolic, mammalian protein tyrosine phosphatase (PTP) which exhibits high specific activity in vitro. We have investigated the substrate specificity of PTP-PEST by a novel substrate-trapping approach in combination with in vitro dephosphorylation experiments. We initially
A Angers-Loustau et al.
The Journal of cell biology, 144(5), 1019-1031 (1999-03-23)
In this article, we show that, in transfected COS-1 cells, protein tyrosine phosphatase (PTP)-PEST translocates to the membrane periphery following stimulation by the extracellular matrix protein fibronectin. When plated on fibronectin, PTP-PEST (-/-) fibroblasts display a strong defect in motility.

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