| 纯度 | >90%SDS-PAGE. |
| 种属 | Trypanosoma |
| 靶点 | HSP100 |
| Uniprot No | O15885 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-138aa |
| 氨基酸序列 | NSPKGLEATREKVWQVVRSYFRPEFLNRLDDIVLFRRLGFGELHEIIDLIVAEVNGRLRSQDILLEVTDEAKNFVLENAFDAEMGARPLRRWVEKYITTEVSRMILAQQLPPNSTVRVLVNGSQGKLAFSVKRSFVSE |
| 预测分子量 | 22.9 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HSP100重组蛋白的3篇代表性文献及其摘要概述：
1. **"Structure and mechanism of the Hsp100 chaperones"**
- **作者**: Doyle SM, Wickner S (2007)
- **摘要**: 该研究解析了HSP100家族(如大肠杆菌ClpB和酵母Hsp104)的晶体结构，揭示了其六聚体环状结构及ATP依赖的蛋白质解聚功能，阐明了其通过水解ATP驱动底物蛋白展开或重折叠的分子机制。
2. **"Hsp104 required for induced thermotolerance and the clearance of yeast prions"**
- **作者**: Sanchez Y, Lindquist S (1990)
- **摘要**: 发现酵母Hsp104(HSP100同源蛋白)对热休克诱导的耐热性至关重要，并证明其通过分解错误折叠的蛋白聚集体(包括朊病毒形式)维持细胞稳态，为HSP100在蛋白质质量控制中的作用提供了早期证据。
3. **"Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation"**
- **作者**: Mogk A, et al. (2015)
- **摘要**: 揭示了HSP100(如ClpB)与HSP70协同工作的机制，证明HSP100依赖HSP70识别并结合聚集的蛋白，通过ATP水解驱动底物解聚，强调了其在细菌和真核生物中对抗蛋白质毒性的关键作用。
4. **"Engineered Hsp104 variants suppress toxicity of neurodegenerative disease-linked proteins"**
- **作者**: Jackrel ME, Shorter J (2014)
- **摘要**: 通过基因工程改造Hsp104(HSP100家族成员)，获得增强解聚活性的变体，成功分解与阿尔茨海默病、帕金森病相关的淀粉样蛋白聚集体，为神经退行性疾病的治疗提供了新策略。
这些文献涵盖了HSP100的结构解析、功能机制及其在疾病治疗中的应用，均为该领域的经典或前沿研究。
**Background of HSP100 Recombinant Protein**
Heat shock protein 100 (HSP100), a member of the AAA+ ATPase superfamily, is a highly conserved molecular chaperone critical for cellular stress responses and protein quality control. It plays a pivotal role in resolving misfolded protein aggregates, a process essential for cell survival under thermal, oxidative, or chemical stress. Structurally, HSP100 comprises nucleotide-binding domains (NBDs) that hydrolyze ATP to fuel conformational changes, enabling substrate unfolding or disaggregation.
Recombinant HSP100 proteins are engineered using expression systems like *E. coli* or mammalian cells, often tagged with affinity markers (e.g., His-tag) for purification. These proteins retain the functional properties of native HSP100. including ATPase activity and interaction with co-chaperones like HSP70. Research highlights their ability to rescue denatured proteins in vitro, making them valuable tools for studying proteostasis mechanisms.
HSP100's biological significance extends to disease contexts. In pathogens such as *Plasmodium* or fungi, it supports virulence and stress adaptation, positioning it as a potential antimicrobial target. Conversely, in humans, HSP100 homologs like HSP104 (in yeast) or ClpB (in bacteria) are explored for mitigating neurodegenerative diseases linked to protein aggregation, such as Alzheimer’s or Parkinson’s. However, human cells lack HSP104. driving interest in engineered HSP100 variants for therapeutic disaggregase activity.
Current studies focus on optimizing recombinant HSP100 for biotechnological applications, including enhancing protein refolding in industrial processes or developing novel therapies. Challenges remain in controlling its activity and ensuring targeted delivery in vivo. Nonetheless, HSP100 recombinant proteins represent a promising avenue for both basic research and translational medicine.
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