跳转至内容
Merck
CN

SRP5073

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

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

别名:

PTPG1, tcag7.1075

登录 查看组织和合同定价。

选择尺寸


关于此项目

NACRES:
NA.32
UNSPSC Code:
12352200
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助

产品名称

PTPN12 (1-355), active, GST tagged human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

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)

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

存储类别

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

新产品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

没有发现合适的版本?

如果您需要特殊版本,可通过批号或批次号查找具体证书。

已有该产品?

在文件库中查找您最近购买产品的文档。

访问文档库

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.

相关内容

我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.

联系客户支持