H6774
Heat Shock Protein 90 from bovine brain
≥95% (SDS-PAGE), lyophilized powder
Synonyme(s) :
HSP 90
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About This Item
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
bovine brain
Pureté
≥95% (SDS-PAGE)
Forme
lyophilized powder
Technique(s)
affinity binding assay: suitable
Température de stockage
−20°C
Application
Heat shock protein 90 from bovine brain has been used to perform the in vitro ubiquitination assay.
Actions biochimiques/physiologiques
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.
Forme physique
Contains Tris buffer salts
Code de la classe de stockage
13 - Non Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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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
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.
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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