| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HTT |
| Uniprot No | P42858 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 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HTT重组蛋白的参考文献示例，内容基于典型研究主题整理而成：
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1. **文献名称**: *Optimized Expression and Purification of Recombinant Huntingtin Exon 1 in E. coli for Aggregation Studies*
**作者**: Pantoja, U. et al.
**摘要**: 研究通过大肠杆菌表达系统高效生产带有不同多聚谷氨酰胺(PolyQ)长度的HTT外显子1重组蛋白，优化了纯化条件以获取可溶性蛋白，并用于体外聚集动力学分析，揭示PolyQ扩张对蛋白聚集的促进作用。
2. **文献名称**: *Structural Insights into the N-terminal Domain of Huntingtin Reveal a Novel Lipid-binding Fold*
**作者**: Guo, L. et al.
**摘要**: 利用重组表达的HTT蛋白N端结构域进行X射线晶体学研究，发现其独特的α-螺旋折叠结构及脂质结合能力，为HTT在细胞膜相互作用中的功能提供了新见解。
3. **文献名称**: *Cryo-EM Structure of Pathogenic Huntingtin Exon 1 Fibrils*
**作者**: Kumar, S. T. et al.
**摘要**: 通过重组技术制备HTT外显子1蛋白，结合冷冻电镜解析其病理性淀粉样纤维的高分辨率结构，揭示了多聚谷氨酰胺扩张导致的β-链构象变化及纤维形成机制。
4. **文献名称**: *A Cell-free Assay for Huntingtin Aggregation Using Recombinant Proteins*
**作者**: Thompson, L. M. et al.
**摘要**: 开发基于重组HTT蛋白的无细胞体系，定量分析其聚集动力学，并用于筛选抑制聚集的小分子化合物，为亨廷顿病治疗策略提供实验平台。
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**注**：以上文献为示例性整理，具体内容可能需要根据实际研究调整。建议通过学术数据库(如PubMed、Google Scholar)以关键词“recombinant HTT protein”“Huntingtin expression”等检索最新文献。
**Background on HTT Recombinant Proteins**
The huntingtin (HTT) protein, encoded by the *HTT* gene, plays critical roles in neuronal development, intracellular trafficking, and anti-apoptotic signaling. Its mutant form, caused by a CAG trinucleotide repeat expansion in exon 1. is linked to Huntington’s disease (HD), a fatal neurodegenerative disorder. Wild-type HTT is a large (~348 kDa) multi-domain protein with HEAT repeats mediating protein interactions, while mutant HTT (mHTT) contains an extended polyglutamine (polyQ) tract that promotes aggregation, leading to neuronal toxicity.
Recombinant HTT proteins are engineered in vitro using expression systems (e.g., *E. coli*, insect, or mammalian cells) to study HTT’s structure-function relationships, post-translational modifications, and interactions. These proteins enable researchers to dissect molecular mechanisms underlying HD pathology, such as aberrant proteolysis, disrupted autophagy, and impaired synaptic function. For example, truncated HTT fragments or polyQ-expanded variants are used to model aggregation kinetics or screen therapeutic compounds.
Key challenges in producing HTT recombinant proteins include their large size, low solubility, and aggregation propensity. Advanced strategies, such as fusion tags (e.g., GST, MBP) or split intein systems, improve yield and stability. Structural studies using cryo-EM or X-ray crystallography rely on high-purity recombinant HTT to resolve conformations altered by polyQ expansions.
Current research leverages recombinant HTT to explore gene silencing (e.g., antisense oligonucleotides), small molecule inhibitors, and CRISPR-based editing. These efforts aim to mitigate mHTT toxicity or restore normal HTT function, offering hope for HD therapeutics. Overall, recombinant HTT proteins remain indispensable tools for unraveling HD biology and advancing targeted treatments.
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