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SRP5191

Sigma-Aldrich

HSP90 α, His tagged human

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

Synonyme(s) :

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

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About This Item

Numéro CAS:
481150-77-0
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.

~94 kDa

Technique(s)

cell culture | mammalian: suitable

Solubilité

water: soluble

Adéquation

suitable for molecular biology

Numéro d'accès NCBI

NM_005348

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... HSP90AA1(3320)

Description générale

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

Application

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness.
Eustace BK
Nature Cell Biology (2004)
Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J
BMC Cancer (2010)
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)
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