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H6774

Sigma-Aldrich

Heat Shock Protein 90 from bovine brain

≥95% (SDS-PAGE), lyophilized powder

Synonym(s):

HSP 90

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

bovine brain

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

technique(s)

affinity binding assay: suitable

storage temp.

−20°C

Application

Heat shock protein 90 from bovine brain has been used to perform the in vitro ubiquitination assay.

Biochem/physiol Actions

HSPs (heat shock proteins) are generated in response to environmental stresses, including, changes in temperature and physiological inhibitors. HSP90 is a cytosolic chaperon. Mammalian HSP 90 has an affinity for steroid receptors, actin, nucleotides, etc., suggesting an important, multifunctional role in vivo. It is present in most eukaryotes as well as prokaryotes.

Physical form

Contains Tris buffer salts

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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N Yonezawa et al.
European journal of biochemistry, 177(1), 1-7 (1988-10-15)
The 90-kDa heat-shock protein (HSP90) has been purified from mammalian tissues, mouse liver and porcine brain, with a good yield by a new method involving hydrophobic chromatography. Mouse liver HSP90 and porcine brain HSP90 were compared with mouse lymphoma HSP90
Yu Shang et al.
Biochemical and biophysical research communications, 386(1), 242-246 (2009-06-16)
Runx1 is a key factor in the generation and maintenance of hematopoietic stem cells. Improper expression and mutations in Runx1 are frequently implicated in human leukemia. Here, we report that CHIP, the carboxyl terminus of Hsc70-interacting protein, also named Stub1
P Csermely et al.
The Journal of biological chemistry, 266(8), 4943-4950 (1991-03-15)
The 90-kDa heat shock protein (hsp-90) is an abundant cytosolic protein believed to play a role in maintenance of protein trafficking and closely associated with several steroid hormone receptors. Incubation of highly purified hsp-90 with [gamma-32P]ATP results in its autophosphorylation
Jason C Young et al.
Cell, 112(1), 41-50 (2003-01-16)
The role of cytosolic factors in protein targeting to mitochondria is poorly understood. Here, we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a specialized TPR domain in the import receptor Tom70 at the outer mitochondrial

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