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SRP5256

Sigma-Aldrich

HSP90β, His tagged human

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

Synonyme(s) :

D6S182, HSP90AB1, HSP90B, HSPC2, HSPCB

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in baculovirus infected Sf9 cells

Pureté

≥70% (SDS-PAGE)

Forme

buffered aqueous glycerol solution

Poids mol.

~91 kDa

Numéro d'accès NCBI

NM_ 007355

Application(s)

cell analysis

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... HSP90AB1(3326)

Description générale

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.

Actions biochimiques/physiologiques

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.

Forme physique

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.

Notes préparatoires

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

Pictogrammes

Health hazardExclamation mark
GHS08,GHS07

Mention d'avertissement

Danger

Mentions de danger

H315,H319,H360D

Classification des risques

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

Code de la classe de stockage

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

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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