| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPE1 |
| Uniprot No | P61604 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-102aa |
| 氨基酸序列 | AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD |
| 预测分子量 | 14.8 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HSPE1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**：*Recombinant human HSP10 produced in Escherichia coli protects against oxidative stress*
**作者**：Cappello F, et al.
**摘要**：研究利用大肠杆菌表达重组人HSPE1(HSP10)，验证其抗氧化功能，发现其通过调节线粒体活性氧(ROS)减少细胞氧化损伤，提示在神经退行性疾病中的潜在治疗价值。
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2. **文献名称**：*Structural and functional analysis of HSPE1/HSP60 interaction in cancer progression*
**作者**：Ghosh JC, et al.
**摘要**：通过重组HSPE1和HSP60蛋白的体外互作实验，揭示二者在肿瘤细胞线粒体中的协同作用机制，并证明靶向该复合物可抑制癌细胞增殖，为癌症治疗提供新靶点。
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3. **文献名称**：*High-yield purification of HSPE1 using a novel affinity chromatography approach*
**作者**：Li Y, et al.
**摘要**：开发了一种基于镍柱亲和层析的新型纯化方法，高效获取高纯度重组HSPE1蛋白，验证其与伴侣蛋白HSP60的功能活性，为后续研究提供可靠技术方案。
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**备注**：以上文献为示例，实际引用时需核实具体来源及准确性。若需进一步扩展，建议检索PubMed或Web of Science数据库，结合关键词“HSPE1 recombinant”或“HSP10 expression”获取最新研究。
**Background of HSPE1 Recombinant Protein**
HSPE1 (Heat Shock Protein Family E1), also known as HSP10 or chaperonin 10. is a member of the heat shock protein (HSP) family, which plays critical roles in cellular stress responses and protein homeostasis. As a mitochondrial chaperonin, HSPE1 forms a functional complex with HSP60 (chaperonin 60) to facilitate the folding of newly synthesized or misfolded proteins in the mitochondrial matrix. This HSP60/HSPE1 complex operates in an ATP-dependent manner, ensuring proper protein conformation and preventing aggregation, which is vital for mitochondrial integrity and cellular survival.
HSPE1 has garnered attention due to its dual role in health and disease. Beyond its canonical chaperone function, it exhibits extracellular signaling properties under stress conditions, modulating immune responses and inflammation. Dysregulation of HSPE1 expression has been linked to various pathologies, including cancer, neurodegenerative disorders (e.g., Alzheimer’s and Parkinson’s diseases), and autoimmune conditions. For instance, elevated HSPE1 levels in certain cancers correlate with tumor progression and chemoresistance, while its downregulation in neurodegenerative contexts may exacerbate protein misfolding pathologies.
Recombinant HSPE1 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic applications. Its purified form retains chaperone activity and structural stability, making it valuable for *in vitro* studies on protein folding mechanisms, mitochondrial dysfunction, and disease pathways. Additionally, recombinant HSPE1 serves as a potential diagnostic biomarker or therapeutic target, with ongoing investigations into its utility in cancer immunotherapy and neuroprotection strategies.
In summary, HSPE1 recombinant protein represents a key tool for dissecting mitochondrial protein quality control mechanisms and developing interventions for diseases linked to proteostatic imbalance.
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