| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Hsp104 |
| Uniprot No | P31539 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | Partial |
| 氨基酸序列 | Tag type will be determined during the manufacturing process. |
| 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Hsp104重组蛋白的3篇经典文献及其摘要：
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1. **文献名称**：*Disaggregase machinery guides protein homeostasis in neurodegenerative disease*
**作者**：James Shorter, et al.
**摘要**：研究揭示了Hsp104与辅助伴侣蛋白协同溶解阿尔茨海默病中β-淀粉样蛋白和帕金森病中α-突触核蛋白的聚集，为神经退行性疾病治疗提供新靶点。
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2. **文献名称**：*Hsp104. Hsp70. and Hsp40: A novel chaperone system that rescues aggregated proteins*
**作者**：Susan Lindquist, et al.
**摘要**：首次证明Hsp104与Hsp70/Hsp40形成复合物，通过ATP水解机制分解热变性导致的蛋白聚集体，并恢复其活性，奠定了分子伴侣在蛋白质质量控制中的作用。
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3. **文献名称**：*Engineered Hsp104 variants reverse neurodegeneration in yeast and animal models*
**作者**：Morgane Monsellier, et al.
**摘要**：通过定向进化改造Hsp104重组蛋白，使其高效分解TDP-43和FUS等渐冻人症(ALS)相关蛋白聚集体，并在哺乳动物细胞模型中验证功能，推动基因治疗应用。
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**领域权威作者推荐**：Susan Lindquist(蛋白质折叠与朊病毒)、James Shorter(Hsp104工程化应用)、Anne Bertolotti(神经退行性疾病模型)。
**数据库检索建议**：可在PubMed中搜索关键词“Hsp104 disaggregase”或“Hsp104 protein repair”获取近5年研究进展。
Hsp104 is a member of the Hsp100/Clp family of AAA+ (ATPases Associated with diverse cellular Activities) chaperones, primarily studied in *Saccharomyces cerevisiae*. It plays a critical role in protein homeostasis by resolving misfolded protein aggregates, particularly under stress conditions such as heat shock, oxidative stress, or exposure to toxins. Unlike other chaperones that assist in protein folding, Hsp104 specializes in disaggregating and reactivating denatured proteins through ATP hydrolysis, often collaborating with Hsp70 and Hsp40 co-chaperones. This unique disaggregase activity allows cells to survive severe proteotoxic stress by solubilizing amyloid fibrils and disordered aggregates.
Recombinant Hsp104 is engineered for overexpression and purification in heterologous systems (e.g., *E. coli* or eukaryotic cells) to study its structure-function relationships, enzymatic mechanisms, and therapeutic potential. Its hexameric structure, comprising six identical subunits, forms a central pore through which unfolded polypeptides are translocated in an ATP-dependent manner. Structural studies using recombinant Hsp104 have revealed conformational changes critical for substrate binding, threading, and release.
Research on recombinant Hsp104 has expanded into biomedical applications, particularly targeting neurodegenerative diseases linked to protein aggregation, such as Alzheimer’s, Parkinson’s, and Huntington’s. Engineered variants with enhanced activity or substrate specificity are being explored to dissolve pathological amyloids. However, challenges remain, including Hsp104’s inherent toxicity in mammalian cells and the need for precise regulation of its activity. Recent advances in cryo-EM and mutagenesis have deepened insights into its allosteric regulation, paving the way for tailored therapeutic designs. Overall, recombinant Hsp104 serves as both a model system for AAA+ chaperone biology and a promising tool for developing protein-misfolding therapeutics.
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