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Merck

SRP5068

Sigma-Aldrich

PKN2/PRK2, active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

别名:

MGC150606, MGC71074, PAK2, PKN2, PRK2, PRKCL2, PRO2042, Pak-2

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About This Item

UNSPSC代码:
12352200
NACRES:
NA.32

重组

expressed in baculovirus infected Sf9 cells

产品线

PRECISIO® Kinase

方案

≥70% (SDS-PAGE)

表单

buffered aqueous glycerol solution

比活

63-85 nmol/min·mg

分子量

~145 kDa

NCBI登记号

运输

dry ice

储存温度

−70°C

基因信息

human ... PKN2(5586)

一般描述

PKN2 (also known as PRK2) is a Rho effector and a member of the protein kinase C superfamily of serine/threonine kinases. PKN2 is an essential regulator of both entry into mitosis and exit from cytokinesis in HeLa S3 cells. PKN2 is required for abscission of the midbody at the end of the cell division cycle and for phosphorylation and activation of Cdc25B, the phosphatase required for activation of mitotic cyclin/Cdk1 complexes at the G2/M transition. C-terminus of PKN2 could be a potential drug target for effector-specific pharmacological intervention of Rho-medicated biological processes.

外形

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

制备说明

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

法律信息

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

储存分类代码

10 - Combustible liquids

WGK

WGK 1


历史批次信息供参考:

分析证书(COA)

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Anja Schmidt et al.
The EMBO journal, 26(6), 1624-1636 (2007-03-03)
Rho GTPases regulate multiple signal transduction pathways that influence many aspects of cell behaviour, including migration, morphology, polarity and cell cycle. Through their ability to control the assembly and organization of the actin and microtubule cytoskeletons, Rho and Cdc42 make
Wee Guan Lim et al.
Archives of biochemistry and biophysics, 479(2), 170-178 (2008-10-07)
PRK2/PKNgamma is a Rho effector and a member of the protein kinase C superfamily of serine/threonine kinases. Here, we explore the structure-function relationship between various motifs in the C-terminal half of PRK2 and its kinase activity and regulation. We report

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