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Rabbit Monoclonal p23 Antibody

  • 中文名: p23抗体
  • 别    名: cPGES; Cytosolic prostaglandin E synthase; Hsp90 co chaperone; P23; Sid 3177; TEBP;;Prostaglandin E synthase 3
货号: IPDX17659
Price: ¥1280
数量:
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验证与应用

应用及物种
WB 咨询技术 Human,Mouse,Rat
IF 1/20-1/50 Human,Mouse,Rat
IHC 咨询技术 Human,Mouse,Rat
ICC 1/50-1/200 Human,Mouse,Rat
FCM 咨询技术 Human,Mouse,Rat
Elisa 咨询技术 Human,Mouse,Rat

产品详情

AliasescPGES; Cytosolic prostaglandin E synthase; Hsp90 co chaperone; P23; Sid 3177; TEBP;;Prostaglandin E synthase 3
WB Predicted band sizeCalculated MW: 19 kDa ; Observed MW: 23 kDa
Host/IsotypeRabbit IgG
Antibody TypePrimary antibody
StorageStore at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species ReactivityHuman,Mouse,Rat
ImmunogenA synthesized peptide derived from human Prostaglandin E synthase 3
FormulationPurified antibody in PBS with 0.05% sodium azide,0.05% BSA and 50% glycerol.

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参考文献

以下是关于p23抗体的3篇示例参考文献(注:文献为示例性内容,实际文献需通过学术数据库查询):

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1. **标题**:*"The co-chaperone p23 modulates Hsp90 function in client protein folding and stabilization"*

**作者**:Johnson, J.L., et al.

**摘要**:该研究探讨了p23作为HSP90辅助伴侣蛋白的作用,通过抑制ATP水解调节HSP90的构象变化,促进客户蛋白(如类固醇激素受体)的稳定性和成熟。实验表明p23抗体可用于检测其在复合体中的动态结合。

2. **标题**:*"p23 overexpression correlates with poor prognosis in breast cancer and promotes tumor cell invasion"*

**作者**:Smith, R.K., & Chen, Y.

**摘要**:通过免疫组化分析乳腺癌组织,发现p23蛋白高表达与患者生存率降低显著相关。体外实验显示,p23抗体阻断其功能可抑制癌细胞迁移,提示其作为潜在治疗靶点。

3. **标题**:*"Structural insights into p23-HSP90 interaction using cryo-EM and antibody-based probing"*

**作者**:Lee, S., et al.

**摘要**:利用冷冻电镜和特异性p23抗体,研究揭示了p23与HSP90复合体的结合位点及构象变化机制,为开发靶向HSP90/p23相互作用的抗癌药物提供结构基础。

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**提示**:实际研究中建议通过PubMed、Web of Science等平台,以“p23 antibody”、“HSP90 co-chaperone”等关键词检索最新文献,重点关注其在疾病机制或实验工具中的应用。

背景信息

The p23 antibody targets the p23 protein, a co-chaperone of the heat shock protein 90 (HSP90) complex. First identified in the 1990s, p23 plays a critical role in stabilizing HSP90-client protein interactions, facilitating the conformational maturation of diverse client proteins, including steroid hormone receptors, kinases, and transcription factors. Its ATPase activity and ability to bind HSP90 during the late stages of the chaperone cycle make it essential for maintaining proteostasis and regulating cellular stress responses.

p23 is overexpressed in various cancers, where it supports tumorigenesis by stabilizing oncogenic clients like HER2. AKT, and mutant p53. This association has driven interest in p23 as a potential therapeutic target and biomarker. Researchers use p23 antibodies in techniques such as Western blotting, immunohistochemistry, and co-immunoprecipitation to study its expression, localization, and interactions in normal and diseased tissues.

Recent studies also explore p23’s role in non-cancer pathologies, including neurodegenerative diseases and viral infections, where HSP90-client pathways are dysregulated. Despite its importance, p23’s regulatory mechanisms and tissue-specific functions remain incompletely understood, prompting ongoing research to clarify its broader biological and clinical implications.

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