SRP5191
HSP90 α, His tagged human
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
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Synonym(s):
FLJ31884, HSP86, HSP90AA1, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP2
Recommended Products
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
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HSP90AA1(3320)
General description
Heat shock protein 90α (HSP90α) is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins. The gene encoding this protein is localized on human chromosome 14q32.31.
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).
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation.
McCready J
BMC Cancer (2010)
Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness.
Eustace BK
Nature Cell Biology (2004)
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)
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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