- 询价
- Cell Signaling Technology
- 5087
- USA
- 2026年01月05日
- W, IP
- Rabbit
- H,M,R,Mk,B
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- 详细信息
- 文献和实验
- 技术资料
- 抗体英文名：
HSP90β Antibody
- 抗原：
synthetic peptide corresponding to the region surrounding Val473 of human HSP90β protein
- 应用范围：
W, IP
- 宿主：
Rabbit
- 供应商：
CST
- 级别：
详见MSDS文件
- 适应物种：
H,M,R,Mk,B
- 库存：
大量
- 保质期：
详见说明书
- 是否单克隆：
2
- 保存条件：
-20°c
- 规格：
100 ul (10 western blots)/carrier free & custom formulation / quantity
| 规格： | 产品价格： | ￥请询价 | |
|---|---|---|---|
| 规格： | 100 ul (10 western blots) | 产品价格： | ￥请询价 |
| 规格： | carrier free & custom formulation / quantity | 产品价格： | ￥请询价 |
pathway more info application references datasheet PDF MSDS PDF protocols
Applications Key: W=Western Blotting IP=Immunoprecipitation
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H M R Mk B | Endogenous | 90 | Rabbit |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | HSP90β Antibody detects endogenous levels of total HSP90β protein. It does not cross-react with HSP90α. |
| Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the region surrounding Val473 of human HSP90β protein. Antibodies are purified by protein A and peptide affinity chromatography. Western Blotting
Western blot analysis of extracts from various cell lines using HSP90β Antibody. |
| Background | 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). |
| Application References | Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know ! |
| Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |
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