H6774
Heat Shock Protein 90 from bovine brain
≥95% (SDS-PAGE), lyophilized powder
Synonym(s):
HSP 90
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About This Item
NACRES:
NA.32
UNSPSC Code:
12352202
Form:
lyophilized powder
Assay:
≥95% (SDS-PAGE)
Biological source:
bovine brain
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
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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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