| 纯度 | >85%SDS-PAGE. |
| 种属 | Saccharomyces cerevisiae |
| 靶点 | HSP10 |
| Uniprot No | P38910 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-106aa |
| 氨基酸序列 | STLLKSAKS IVPLMDRVLV QRIKAQAKTA SGLYLPEKNV EKLNQAEVVA VGPGFTDANG NKVVPQVKVG DQVLIPQFGG STIKLGNDDE VILFRDAEIL AKIAKD |
| 预测分子量 | 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HSP10重组蛋白的3篇代表性文献示例及简要摘要：
1. **文献名称**：*Recombinant HSP10 maintains structural stability and chaperone activity under oxidative stress*
**作者**：Li, X., et al.
**摘要**：研究通过大肠杆菌表达系统成功制备重组HSP10蛋白，并证明其在氧化应激条件下仍能维持结构稳定性，有效协助HSP60介导的线粒体蛋白折叠，提示其在细胞应激保护中的潜在应用。
2. **文献名称**：*HSP10 interacts with HSP60 via a novel domain essential for mitochondrial protein homeostasis*
**作者**：Smith, J.R., et al.
**摘要**：通过X射线晶体学解析重组HSP10与HSP60的复合物结构，发现HSP10的C端结构域对两者协同调控底物蛋白折叠至关重要，为设计靶向分子伴侣系统的药物提供结构基础。
3. **文献名称**：*Overexpression of recombinant HSP10 suppresses apoptosis in cancer cells through modulating Bcl-2 pathways*
**作者**：Wang, Y., et al.
**摘要**：在乳腺癌细胞模型中，重组HSP10的高表达显著抑制线粒体途径凋亡，其机制与调控Bcl-2家族蛋白平衡相关，提示HSP10可能成为肿瘤治疗的分子靶点。
(注：上述文献为示例性内容，实际文献需通过PubMed或Web of Science等数据库检索。)
Heat shock protein 10 (HSP10), also known as chaperonin 10. is a conserved molecular chaperone that plays a critical role in maintaining cellular proteostasis. It primarily functions as a co-chaperone for HSP60. forming a HSP60/HSP10 complex that assists in the folding of nascent polypeptides and the refolding of misfolded proteins, particularly in mitochondria. This ATP-dependent interaction is essential for protein quality control under both physiological and stress conditions, such as heat shock, oxidative stress, or inflammation.
Recombinant HSP10 proteins are engineered through genetic modification, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems. Advanced purification techniques like affinity chromatography ensure high-purity products for research and therapeutic applications. The recombinant form preserves the native structure and functional epitopes, enabling studies on its biological mechanisms and interactions.
Beyond its classical chaperone role, HSP10 shows intriguing extramitochondrial localization in certain pathological states, suggesting involvement in immune modulation, apoptosis regulation, and cellular signaling. Its dual nature as both a pro-survival molecule and potential disease biomarker has drawn attention to cancer, neurodegenerative disorders (e.g., Alzheimer's), and autoimmune diseases. In cancer, HSP10 overexpression correlates with tumor progression, while in chronic inflammation, it may exhibit immunosuppressive properties.
Therapeutic exploration includes HSP10-based vaccines and anti-inflammatory strategies, though challenges persist in understanding its context-dependent functions. Current research leverages recombinant HSP10 to dissect its structure-function relationships, post-translational modifications, and extracellular signaling pathways. These efforts aim to harness its chaperone capabilities for protein-stress-related diseases while navigating its paradoxical roles in different pathological microenvironments.
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