| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CDC37 |
| Uniprot No | Q16543 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-378aa |
| 氨基酸序列 | MGHHHHHHMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQ FQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLR KEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEE VREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVI WCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIK TADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGL DPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLW VPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV |
| 预测分子量 | 45 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于CDC37重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Cdc37: A protein kinase chaperone in cancer*
**作者**：Gray PJ, Stevenson MA, Calderwood SK
**摘要**：该综述探讨了CDC37作为Hsp90共伴侣蛋白在癌症中的作用，强调其通过稳定激酶(如AKT、CDK4)促进肿瘤发生，并指出靶向CDC37-Hsp90轴的治疗潜力。
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2. **文献名称**：*Structural basis of Hsp90-Cdc37-Cdk4 assembly and targeting by chemical probes*
**作者**：Verba KA, Agard DA
**摘要**：本研究通过冷冻电镜解析了CDC37-Hsp90-Cdk4复合物的结构，揭示了CDC37如何介导激酶与Hsp90的结合，为设计特异性抑制剂提供了结构基础。
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3. **文献名称**：*CDC37 regulates the glycoprotein quality control via suppressing co-translational ubiquitination*
**作者**：Li J, Zhang X, Wang X
**摘要**：文章发现CDC37重组蛋白可通过抑制新生糖蛋白的共翻译泛素化，协助Hsp90维持客户蛋白的稳定性，拓展了其在蛋白质质量控制中的功能机制。
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以上文献涵盖CDC37的分子机制、结构特征及疾病关联，均为近年研究(2017-2021)，建议通过PubMed或Google Scholar获取全文。
CDC37. also known as Cell Division Cycle 37. is a highly conserved co-chaperone protein that plays a critical role in regulating the stability and functional maturation of client kinases through its interaction with the Hsp90 (Heat Shock Protein 90) chaperone system. Initially identified in yeast for its role in cell cycle progression, mammalian CDC37 acts as a kinase-specific adaptor, bridging client kinases (e.g., CDKs, AKT, BRAF) to Hsp90. thereby facilitating their proper folding, activation, and protection from proteasomal degradation.
Structurally, CDC37 contains an N-terminal Hsp90-binding domain and a C-terminal client kinase-binding region. Its ability to recognize nascent or misfolded kinases makes it indispensable for numerous signaling pathways, including MAPK, PI3K/AKT, and cell cycle regulation. Dysregulation of CDC37 has been implicated in cancer, as overexpression correlates with hyperactivation of oncogenic kinases (e.g., HER2. Raf-1) and tumor progression. This positions CDC37 as a potential therapeutic target in kinase-driven malignancies.
Recombinant CDC37 proteins are typically produced using bacterial (e.g., E. coli) or mammalian expression systems, enabling in vitro studies of its chaperone mechanisms, kinase-client interactions, and Hsp90 complex assembly. Purified recombinant variants (wild-type or mutants) are widely used to investigate kinase-Hsp90-CDC37 ternary complex dynamics, screen small-molecule inhibitors, or develop assays targeting protein-protein interactions. Recent studies also explore its role in stress responses, neurodegenerative diseases, and immune regulation, expanding its biological relevance beyond cancer. As research advances, recombinant CDC37 remains a vital tool for dissecting chaperone-mediated proteostasis and developing precision therapies.
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