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Merck
CN

SRP5191

Sigma-Aldrich

HSP90 α,His 标记 人

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

别名:

FLJ31884, HSP86, HSP90AA1, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP2

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About This Item

UNSPSC代码:
12352200
NACRES:
NA.32

生物来源

human

重组

expressed in baculovirus infected Sf9 cells

检测方案

≥70% (SDS-PAGE)

形式

buffered aqueous glycerol solution

分子量

~94 kDa

技术

cell culture | mammalian: suitable

溶解性

water: soluble

适用性

suitable for molecular biology

NCBI登记号

运输

dry ice

储存温度

−70°C

基因信息

human ... HSP90AA1(3320)

一般描述

Research area: Cell cycle. The gene encoding this protein is localized on human chromosome 14q32.31.

应用

HSP90 α, His tagged human has been used to measure antibodypolyspecificity by flow cytometry. It has also been used as a molecularmarker to study the effect of Temozolomide on glioblastoma cells releasedextracellular vesicles.

生化/生理作用

Heat shock protein 90α (HSP90α) is a molecular chaperone involved in the folding, assembly-disassembly, and activation of multiple types of target proteins such as kinases, steroid hormone receptors and transcription factors. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (matrix metalloproteinase-2).HSP90α are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins.

外形

Supplied in 50mM MOPS, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 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

象形图

Health hazardExclamation mark

警示用语:

Danger

危险声明

危险分类

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

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Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness.
Eustace BK
Nature Cell Biology (2004)
P Csermely et al.
Pharmacology & therapeutics, 79(2), 129-168 (1998-09-28)
The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of
De novo unbalanced translocation resulting in monosomy for distal 5p (5p14.1 ? pter) and 14q (14q32.31 ? qter) associated with fetal nuchal edema, microcephaly, intrauterine growth restriction, and single umbilical artery: Prenatal diagnosis and molecular cytogenetic characterization
Chih-Ping
Taiwanese Journal of Obstetrics & Gynecology (2013)
Role of plant heat- hock proteins and molecular chaperones in the abiotic stress response
Wang-Xia Wang
Trends in Plant Science (2004)
Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J
BMC Cancer (2010)

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