Phospho-HSP90α (Thr5/7) Antibody
货号：
3488S 基本售价：
3980.0 元 规格：
-
产品信息
概述| 货号 | 3488S |
| 反应种属 | Human/Mouse/Rat/Monkey |
| 来源宿主 | Rabbit |
| 应用 | W |
| 目标/特异性 | Phospho-HSP90α (Thr5/7) Antibody detects endogenous levels of HSP90α only when phosphorylated at Thr5/7. |
| 使用方法 | WB(1:1000) |
性能| 供应商 | CST |
| 背景 | HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP and co-chaperone dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2). |
| 存放说明 | -20C |
| 计算分子量 | 90 |
参考图片Western blot analysis of extracts from HeLa and COS cells, treated with either λ phosphatase or UV, using Phospho-HSP90α (Thr5/7) Antibody and β-Actin Antibody #4967 as a loading control. 对HeLa和COS细胞，进行λ磷酸酶或紫外线处理，使用Phospho-HSP90α (Thr5/7) Antibody和β-Actin Antibody #4967作为上样对照进行Western blot分析。 |
