癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
Anti-Hsp90 beta/HSP90AB1 Antibody Picoband™ (monoclonal, 7B7F5)
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IF, ICC, FC |
|---|---|
| Primary Accession | P08238 |
| Host | Mouse |
| Isotype | IgG2b |
| Reactivity | Rat, Human, Mouse |
| Clonality | Monoclonal |
| Format | Lyophilized |
| Description | Anti-Hsp90 beta/HSP90AB1 Antibody Picoband™ (monoclonal, 7B7F5) . Tested in Flow Cytometry, IF, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. |
| Reconstitution | Adding 0.2 ml of distilled water will yield a concentration of 500 µg/ml. |
| Gene ID | 3326 |
|---|---|
| Other Names | Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, Heat shock protein family C member 3, HSP90AB1 (HGNC:5258) |
| Calculated MW | 83264 Da |
| Application Details | Western blot, 0.25-0.5 µg/ml, Human, Mouse, Rat Immunocytochemistry/Immunofluorescence, 5 µg/ml, Human Flow Cytometry, 1-3 µg/1x10^6 cells, Human |
| Source | Eukaryota |
| Contents | Each vial contains 4 mg Trehalose, 0.9 mg NaCl and 0.2 mg Na2HPO4. |
| Clone Names | Clone: 7B7F5 |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of human Hsp90 beta, identical to the related mouse and rat sequences. |
| Purification | Immunogen affinity purified. |
| Storage | At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | HSP90AB1 (HGNC:5258) |
|---|---|
| Function | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1- mediated inhibition of TGF-beta signaling via inhibition of STUB1- mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). |
| Cellular Location | Cytoplasm. Melanosome Nucleus. Secreted. Cell membrane. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065) Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673). Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762). |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Heat shock protein HSP 90-beta, also called HSP90beta, is a protein that in humans is encoded by the HSP90AB1 gene. It is mapped to chromosome 6p21.1. This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. And this gene is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes.
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