| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP90aA1 |
| Uniprot No | P07900 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 233-291aa |
| 氨基酸序列 | DEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELN |
| 预测分子量 | 11.2 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HSP90AA1重组蛋白的3篇代表性文献概览：
1. **《Expression and purification of recombinant human HSP90α in E. coli for structural studies》**
- **作者**：Smith J. et al.
- **摘要**：本研究开发了一种高效的大肠杆菌表达系统，用于生产高纯度重组人源HSP90α蛋白。通过优化诱导条件和亲和层析技术，成功获得可用于X射线晶体学分析的蛋白样品，为后续结构功能研究奠定基础。
2. **《Functional characterization of HSP90AA1 in cancer cell migration using a recombinant GST-tagged protein》**
- **作者**：Li Y. et al.
- **摘要**：作者构建了GST标签融合的HSP90AA1重组蛋白，证明其通过调控细胞外基质的金属蛋白酶活性促进肿瘤细胞迁移。实验验证了重组蛋白与客户蛋白(client proteins)的相互作用机制。
3. **《A novel HSP90α-derived peptide vaccine targeting cancer immunotherapy》**
- **作者**：Wang X. et al.
- **摘要**：利用重组HSP90AA1蛋白设计多肽疫苗，在小鼠模型中显著增强抗肿瘤免疫应答。研究揭示了重组蛋白在抗原呈递中的作用，为癌症免疫治疗提供新策略。
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**备注**：以上文献信息为示例性概括，实际引用需根据具体研究需求检索PubMed或Web of Science数据库，优先选择近五年内高影响因子期刊论文(如《Nature Communications》《Cell Stress and Chaperones》等)。重组HSP90AA1研究多集中于癌症靶向治疗、蛋白相互作用网络及药物筛选平台开发领域。
HSP90AA1. a member of the heat shock protein 90 (HSP90) family, is a highly conserved molecular chaperone critical for maintaining cellular homeostasis under stress conditions. It specifically refers to the inducible cytosolic isoform HSP90α, encoded by the HSP90AA1 gene. This protein facilitates the folding, stabilization, and activation of diverse "client proteins," including kinases, transcription factors, and steroid hormone receptors, through ATP-dependent conformational cycles. Its function is tightly regulated by co-chaperones and post-translational modifications.
Recombinant HSP90α is produced using expression systems like *E. coli* or mammalian cells, often tagged for purification (e.g., His-tag). Purification typically involves affinity chromatography and refolding steps to ensure proper conformation. The recombinant form retains ATPase activity and client-binding capacity, making it invaluable for biochemical studies, drug discovery, and structural analyses (e.g., crystallography).
HSP90AA1 overexpression is linked to cancer progression, neurodegenerative diseases, and inflammation, positioning it as a therapeutic target. Over 20 HSP90 inhibitors (e.g., geldanamycin analogs) have entered clinical trials, though challenges like toxicity and resistance persist. Recombinant HSP90α also serves as a biomarker in cancer diagnostics, with elevated serum levels correlating with tumor aggressiveness. Recent research explores its role in extracellular signaling, viral infection, and immune regulation, expanding its biomedical relevance. Despite its promise, understanding isoform-specific functions and developing selective modulators remain key challenges in translating HSP90AA1 research into clinical applications.
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