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- 文献和实验
- 技术资料
- 保存条件:
Powder: -20°C, 3 years; 4°C, 2 years.In solvent: -80°C, 6 months; -20°C, 1 month.
- 库存:
货期:1-2天
- 供应商:
MedChemExpress LLC
- CAS号:
1268273-90-0
- 规格:
10 mM * 1 mL/1 mg/5 mg/10 mg
| 规格: | 10 mM * 1 mL | 产品价格: | ¥2657.0 |
|---|---|---|---|
| 规格: | 1 mg | 产品价格: | ¥1086.0 |
| 规格: | 5 mg | 产品价格: | ¥2600.0 |
| 规格: | 10 mg | 产品价格: | ¥3950.0 |
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HSP70-IN-1
CAS No. : 1268273-90-0
MCE 国际站:HSP70-IN-1
产品活性:HSP70-IN-1是一种热休克蛋白 (HSP) 抑制剂; 抑制Kasumi-1细胞的生长的IC50值为2.3 μM。
研究领域:Cell Cycle/DNA Damage | Metabolic Enzyme/Protease
作用靶点:HSP
In Vitro: The heat shock protein 70 (Hsp70) is a molecular chaperone which plays an important function in protein homeostasis as well as in cell signaling and survival. Hsp70 is frequently overexpressed in cancer, where the elevated expression is furthermore believed to be a cause of or to lead to resistance to chemotherapy and other treatments. HSP70-IN-1 interferes with the formation of functional Hsp70-HOP-Hsp90 machinery by its ability to dose-dependently alter the megacomplex components and to destabilize an Hsp70-Hsp90 machinery client, Raf-1. In cells, the refolding of heat-denatured luciferase by endogenous as well as transfected Hsp70 is inhibited by HSP70-IN-1. HSP70-IN-1 also results in induction of apoptosis in cancer cells. Addition of HSP70-IN-1to cancer cells dose-dependently alters the formation of the Hsp70-HOP complex, a phenomenon associated with their destabilization and reduction in half-life.
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热门产品线:重组蛋白 | 化合物库 | 天然产物 | 荧光染料 | PROTAC | 同位素标记物
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文献和实验94是热休克蛋白HSP90家族的成员之一,与HSP90具有50%的同源性,是高度保守的蛋白。 它们间在ca2+信号中应用文献如下,希望对你有用. kaige88 它们间在ca2+信号中应用文献如下,希望对你有用. shaoliming 向kaige88版主学习! mini综述1篇,Extracellular heat shock proteins in cell signaling. FEBS
内, Hsp70 家族成员的主要功能是以 ATP 依赖的方式结合未折叠多肽链的疏水区以稳定蛋白质的未折叠状态,再通过有控制的释放帮助其折叠; 应激蛋白 90 家族 (Stress-90 family) 即热休克蛋白 90 家族,分子量在 90Ku 左右,包括大肠杆菌胞浆中的 HtpG
Isolation of CFTR: Chaperone Complexes by Co-Immunoprecipitation
is retained in the ER and degraded via the ubiquitin-proteasome pathway (2 ,3 ). Molecular chaperones localized to the ER lumen (calnexin) and the cytosol (Hsp70, Hsc70, Hdj-2, Hdj-1, and Hsp90) have been shown to transiently associate with both CFTR
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