| 货号 | 5087S |
| 反应种属 | Human/Mouse/Rat/Monkey/Bovine |
| 来源宿主 | Rabbit |
| 应用 | W/IP |
| 目标/特异性 | HSP90β Antibody detects endogenous levels of total HSP90β protein. It does not cross-react with HSP90α. |
| 使用方法 | WB(1:1000) IP (1:50) |
| 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 |
Western blot analysis of extracts from various cell lines using HSP90β Antibody. 对多个细胞系使用HSP90β Antibody进行Western blot分析。 |
