SRP5073
PTPN12 (1-355), active, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Sinônimo(s):
PTPG1, tcag7.1075
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About This Item
Código UNSPSC:
12352200
NACRES:
NA.32
recombinante
expressed in E. coli
Ensaio
≥70% (SDS-PAGE)
forma
buffered aqueous glycerol solution
atividade específica
2520-3410 nmol/min·mg
peso molecular
~66 kDa
nº de adesão NCBI
Condições de expedição
dry ice
temperatura de armazenamento
−70°C
Informações sobre genes
human ... PTPN12(5782)
Descrição geral
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.
forma física
Supplied in 20mM MOPS, pH 7.5, 50mM NaCl, 10mM glutathione, 0.25mM DTT, 0.1mM PMSF, 30% glycerol.
Nota de preparo
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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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.
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
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