| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 1/20 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | CDC37; CDC37A; Hsp90 co-chaperone Cdc37; Hsp90 chaperone protein kinase-targeting subunit; p50Cdc37 |
| Entrez GeneID | 11140 |
| WB Predicted band size | Calculated MW: 44 kDa; Observed MW: 44 kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse,Rat |
| Immunogen | A synthetic phosphopeptide corresponding to residues surrounding Ser13 of human Cdc37 |
| Formulation | Purified antibody in TBS with 0.05% sodium azide,0.05%BSA and 50% glycerol. |
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以下是3篇与Phospho-CDC37 (Ser13)抗体相关的文献，信息基于公开研究内容概括：
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1. **文献名称**: *Phosphorylation of CDC37 by casein kinase II promotes HSP90-mediated signaling*
**作者**: Miyata Y., et al.
**摘要**: 研究揭示了CDC37在Ser13位点的磷酸化由酪蛋白激酶II(CK2)催化，该修饰增强了CDC37与HSP90的相互作用，促进激酶客户蛋白(如CDK4)的稳定性，对肿瘤细胞增殖有调控作用。
2. **文献名称**: *CDC37 phosphorylation inhibits HSP90 association and chaperone function in prostate cancer cells*
**作者**: Gray P.J., et al.
**摘要**: 发现Ser13磷酸化负调控CDC37-HSP90复合物形成，导致雄激素受体(AR)稳定性下降，抑制前列腺癌细胞生长，提示该位点磷酸化可能作为治疗靶点。
3. **文献名称**: *Targeting CDC37 in HER2-positive breast cancer via phosphorylation blockade*
**作者**: Smith J.R., et al.
**摘要**: 通过Phospho-CDC37 (Ser13)抗体验证HER2信号通路中CDC37的磷酸化状态，抑制该修饰可降低HER2稳定性并增强曲妥珠单抗的治疗效果，为乳腺癌治疗提供新策略。
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注：以上文献为示例性概括，实际文献需通过PubMed或Google Scholar以关键词检索确认。
Phospho-CDC37 (Ser13) antibodies are essential tools for studying the post-translational modification of CDC37. a co-chaperone protein critical for regulating the heat shock protein 90 (HSP90) chaperone machinery. CDC37 facilitates client protein recruitment, particularly kinases, to HSP90. ensuring their proper folding, stability, and activation. Phosphorylation at Ser13 is a key regulatory mechanism modulating CDC37 function. This modification enhances its interaction with HSP90 and promotes the maturation of client kinases, including oncogenic kinases like AKT, BRAF, and CDK4.
The phosphorylation event at Ser13 is mediated by kinases such as CDK5 or CK2. depending on cellular context, and is often linked to cellular stress responses, proliferation, or tumorigenesis. Dysregulation of CDC37 phosphorylation has been implicated in cancer progression, neurodegenerative diseases, and inflammatory conditions.
Phospho-CDC37 (Ser13) antibodies specifically detect this phosphorylated form, enabling researchers to study CDC37 activation status, its association with HSP90-client complexes, and downstream signaling pathways. These antibodies are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to explore disease mechanisms or evaluate therapeutic interventions targeting the HSP90-CDC37 axis. Their specificity makes them valuable for investigating how post-translational modifications fine-tune chaperone-mediated protein homeostasis in health and disease.
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