- 询价
- Cell Signaling Technology
- 4874
- USA
- 2025年08月18日
- W, IHC-P
- Rabbit
- H,M,R,Mk,Dm,Z,C,B
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- 详细信息
- 文献和实验
- 技术资料
- 抗体英文名：
HSP90 Antibody
- 抗原：
synthetic peptides corresponding to human HSP90
- 应用范围：
W, IHC-P
- 宿主：
Rabbit
- 保质期：
详见说明书
- 适应物种：
H,M,R,Mk,Dm,Z,C,B
- 库存：
大量
- 供应商：
CST
- 级别：
详见MSDS文件
- 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 IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey C=Chicken Dm=D. melanogaster Z=Zebrafish 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 IHC-P | H M R Mk Dm Z (C) (B) | Endogenous | 90 | Rabbit |
| Protocols |
|
|---|---|
| Specificity / Sensitivity | HSP90 Antibody detects endogenous levels of total HSP90 protein, alpha and beta isoforms. This antibody does not cross-react with other HSPs. |
| Source / Purification | Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to human HSP90. Antibodies are purified by protein A and peptide affinity chromatography. Western Blotting
Western blot analysis of extracts from HeLa, NIH/3T3, C6 and COS cells using HSP90 Antibody. IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human colon carcinoma, using HSP90 Antibody. IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, showing cytoplasmic and nuclear localization, using HSP90 Antibody. IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human Non-Hodgkin's lymphoma, using HSP90 Antibody. IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human prostate carcinoma, using HSP90 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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文献和实验Detecting HSP90 Phosphorylation
Heat-shock protein 90 (HSP90 ) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90 ’s ATPase activity is associated with its chaperone
Assays for HSP90 and Inhibitors
The molecular chaperone HSP90 is currently under investigation as a promising target for anticancer drug discovery. It constitutes 1–2% of total cellular protein and is present in the cell as a dimer in association with a number
Hsp90 and Client Protein Maturation
Heat-shock protein 90 (Hsp90) is a molecular chaperone that assists in the maturation of a limited set of substrate proteins that are collectively referred to as clients. The majority of identified Hsp90 clients are involved in signal
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