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Merck

SRP5256

Sigma-Aldrich

HSP90β,His 标记 人

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

别名:

D6S182, HSP90AB1, HSP90B, HSPC2, HSPCB

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About This Item

分類程式碼代碼:
12352200
NACRES:
NA.32

生物源

human

重組細胞

expressed in baculovirus infected Sf9 cells

化驗

≥70% (SDS-PAGE)

形狀

buffered aqueous glycerol solution

分子量

~91 kDa

NCBI登錄號

應用

cell analysis

運輸包裝

dry ice

儲存溫度

−70°C

基因資訊

human ... HSP90AB1(3326)

一般說明

HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins. HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis.

生化/生理作用

Heat shock protein 90kDa α family class B member 1 (HSP90AB1) is expressed in cancers and has a role in the infection of Japanese encephalitis virus. It also takes part in signal transduction pathways.

外觀

Supplied in 50 mM sodium phosphate, pH 7.0, 300 mM NaCl, 150 mM imidazole, 0.1 mM PMSF, 0.2 mM DTT, 25% glycerol.

準備報告

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

象形圖

Health hazardExclamation mark

訊號詞

Danger

危險聲明

危險分類

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

儲存類別代碼

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
Bin Chen
BMC Genomics, 7, 156-156 (2006)
Heat-shock protein 90 inhibitors in cancer therapy: 17AAG and beyond.
Georgakis GV and Younes A
Future Oncology, 1(2), 273-281 (2005)
Morgan C Hunter et al.
PloS one, 9(1), e86842-e86842 (2014-01-28)
Heat shock protein 90 (Hsp90) has been identified in the extracellular space and has been shown to chaperone a finite number of extracellular proteins involved in cell migration and invasion. We used chemical cross-linking and immunoprecipitation followed by tandem mass
Yan Zhao et al.
PloS one, 8(3), e58646-e58646 (2013-03-22)
Variations in genetic background are the leading cause of differential susceptibility to traumatic infection. Heat shock protein 90 (HSP90), a broadly distributed and conserved molecule, regulates inflammation under stressful and traumatic conditions. However, the relationships between HSP90 genetic polymorphisms, post-traumatic
Yueh-Liang Tsou et al.
PloS one, 8(10), e77133-e77133 (2013-10-08)
Although several factors participating in enterovirus 71 (EV71) entry and replication had been reported, the precise mechanisms associated with these events are far from clear. In the present study, we showed that heat shock protein 90 (HSP90) is a key

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