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Merck

H6774

Sigma-Aldrich

Heat Shock Protein 90 from bovine brain

≥95% (SDS-PAGE), lyophilized powder

别名:

HSP 90

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About This Item

分類程式碼代碼:
12352202
NACRES:
NA.32

生物源

bovine brain

化驗

≥95% (SDS-PAGE)

形狀

lyophilized powder

技術

affinity binding assay: suitable

儲存溫度

−20°C

應用

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

生化/生理作用

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.

外觀

含 Tris 缓冲盐

儲存類別代碼

13 - Non Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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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
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
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
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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