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Safety Information

SRP5191

Sigma-Aldrich

HSP90 α, His tagged human

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

Synonym(s):

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

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About This Item

CAS Number:
481150-77-0
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

Assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

~94 kDa

technique(s)

cell culture | mammalian: suitable

solubility

water: soluble

suitability

suitable for molecular biology

NCBI accession no.

NM_005348

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HSP90AA1(3320)

General description

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.

Biochem/physiol Actions

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.

Physical form

Supplied in 50mM MOPS, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.

Preparation Note

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

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H360D

Hazard Classifications

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

Storage Class Code

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

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

ISHL Indicated Name

Substances Subject to be Indicated Names

ISHL Notified Names

Substances Subject to be Notified Names

Cartagena Act

Cartagena Act Listed

JAN Code

SRP5191-50UG:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J
BMC Cancer (2010)
Role of plant heat- hock proteins and molecular chaperones in the abiotic stress response
Wang-Xia Wang
Trends in Plant Science (2004)
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)
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
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