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Merck
CN

SRP5109

Sigma-Aldrich

p27KIP1, GST tagged human

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

别名:

CDKN1B, CDKN4, MEN1B

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About This Item

UNSPSC代码:
12352202
NACRES:
NA.32

生物来源

human

重组

expressed in E. coli

方案

≥70% (SDS-PAGE)

表单

buffered aqueous glycerol solution

分子量

~52 kDa

NCBI登记号

应用

cell analysis

运输

dry ice

储存温度

−70°C

基因信息

human ... CDKN1B(1027)

一般描述

KIP1 (cyclin-dependent kinase inhibitor 1B) is a kinesin-related motor protein required for mitotic spindle assembly and chromosome segregation. Many tumorigenic processes modulate cell-cycle progression by regulating the levels of the cyclin-dependent kinase inhibitor KIP1. KIP1 binds to and inhibits cyclinE-Cdk2 complex, cyclinA-CDK2 and cyclinD1-CDK4. The phosphorylation- and ubiquitination-dependent proteolysis of KIP1 is implicated in control of the G1-S transition in the cell cycle. KIP1 is critical for retinoblastoma protein (Rb)-induced cellular proliferative senescence.

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

储存分类代码

10 - Combustible liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

Lot/Batch Number

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M A Hoyt et al.
The Journal of cell biology, 118(1), 109-120 (1992-07-01)
Two Saccharomyces cerevisiae genes, CIN8 and KIP1 (a.k.a. CIN9), were identified by their requirement for normal chromosome segregation. Both genes encode polypeptides related to the heavy chain of the microtubule-based force-generating enzyme kinesin. Cin8p was found to be required for
A C Carrano et al.
Nature cell biology, 1(4), 193-199 (1999-11-13)
Degradation of the mammalian cyclin-dependent kinase (CDK) inhibitor p27 is required for the cellular transition from quiescence to the proliferative state. The ubiquitination and subsequent degradation of p27 depend on its phosphorylation by cyclin-CDK complexes. However, the ubiquitin-protein ligase necessary

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