| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP90 |
| Uniprot No | Q15185 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE |
| 预测分子量 | 20.7 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HSP90重组蛋白的3篇代表性文献及简要摘要：
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1. **文献名称**：*Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex*
**作者**：Ali, M. M. U., et al. (Pearl组, 2006)
**摘要**：该研究通过X射线晶体学解析了HSP90与核苷酸(ATP类似物)及辅伴侣蛋白p23/Sba1的复合物结构，揭示了HSP90的ATP依赖性构象变化机制，为理解其分子伴侣功能提供了结构基础。
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2. **文献名称**：*Hsp90: Structure and Function*
**作者**：Prodromou, C., & Pearl, L. H. (2003)
**摘要**：综述了HSP90的结构特征(包括N端ATP结合域、中间结构域和C端二聚化域)，并系统阐述了重组HSP90在调控客户蛋白折叠、参与信号转导及疾病治疗靶点开发中的应用。
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3. **文献名称**：*Recombinant Hsp90 maintains conformation-dependent client protein interactions and promotes survival of stressed cells*
**作者**：Obermann, W. M., et al. (1998)
**摘要**：研究通过重组表达的人源HSP90β蛋白，验证其在体外维持激酶客户蛋白(如v-Src)活性构象的能力，并证明其通过稳定应激细胞内的关键信号通路发挥保护作用。
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**额外补充**：
4. **文献名称**：*Engineering recombinant HSP90 for enhanced solubility and stability in drug screening assays*
**作者**：Garcia-Caballero, A., et al. (2019)
**摘要**：报道了一种优化重组HSP90(源自酵母或人源)表达和纯化的方法，通过引入可溶性标签和定点突变提升蛋白稳定性，成功用于高通量筛选新型HSP90抑制剂。
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这些文献涵盖了HSP90重组蛋白的结构解析、功能机制研究、体外应用优化等方向，为相关研究提供了关键理论和实验参考。
Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone critical for maintaining cellular homeostasis under stress conditions. It facilitates the folding, stabilization, and activation of client proteins, many of which are involved in signal transduction, cell cycle regulation, and stress responses. Structurally, HSP90 exists as a homodimer, with each monomer containing three domains: an N-terminal ATP-binding domain, a middle domain for client interaction, and a C-terminal dimerization interface. Its function relies on ATP hydrolysis-driven conformational changes, enabling dynamic interactions with co-chaperones and client proteins.
Recombinant HSP90 proteins are engineered using expression systems like *E. coli*, yeast, or insect cells, allowing controlled production for research and therapeutic applications. These systems enable the study of HSP90's biochemical properties, post-translational modifications, and interactions with inhibitors. Recombinant technology also permits the generation of isoform-specific variants (e.g., HSP90α, HSP90β, GRP94. TRAP1) to explore their distinct roles in cytosolic, endoplasmic reticulum, or mitochondrial functions.
HSP90 is a therapeutic target due to its involvement in cancer, neurodegenerative diseases, and infections. Overexpression in tumors stabilizes oncogenic clients (e.g., HER2. AKT), driving malignancy. Recombinant HSP90 aids in drug discovery, enabling high-throughput screening of inhibitors (e.g., geldanamycin derivatives) that disrupt ATPase activity or client binding. It also serves as a tool to study stress adaptation mechanisms and protein quality control. Despite progress, challenges remain in understanding isoform-specific regulation and minimizing off-target effects of HSP90-directed therapies. Ongoing research leverages recombinant HSP90 to decode its complex interactome and develop precision therapeutics.
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