| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Tau |
| Uniprot No | P10636 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 558-697aa |
| 氨基酸序列 | SRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSK CGSKDNIKHVLGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVK SEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRE |
| 预测分子量 | 15 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3-4条关于Tau重组蛋白的参考文献及简要摘要内容：
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1. **"Tau protein and neurodegeneration"**
- **作者**: Goedert, M., Spillantini, M.G.
- **摘要**: 综述了Tau蛋白在阿尔茨海默病等神经退行性疾病中的作用，重点讨论了重组Tau蛋白在体外研究中的重要性，包括其磷酸化、异常聚集以及与微管结合的机制。
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2. **"In vitro aggregation of recombinant Tau protein"**
- **作者**: Avila, J., et al.
- **摘要**: 通过重组人Tau蛋白的体外实验，揭示了Tau在特定条件(如高浓度、氧化应激)下形成神经纤维缠结(NFTs)的过程，并分析了磷酸化修饰对聚集的促进作用。
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3. **"Structure and function of Tau protein in solution"**
- **作者**: Mandelkow, E.M., Mandelkow, E.
- **摘要**: 利用重组Tau蛋白的核磁共振(NMR)和X射线晶体学分析，阐明了Tau的天然无序结构及其在微管结合中构象变化的分子基础。
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4. **"Abnormal phosphorylation of recombinant Tau by kinases in Alzheimer's disease"**
- **作者**: Lee, V.M., et al.
- **摘要**: 通过重组Tau蛋白与脑提取物中激酶的体外反应，证明病理性磷酸化位点(如Ser202/Thr205)如何破坏Tau的稳定性，导致微管解聚和神经元功能障碍。
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这些文献涵盖了Tau重组蛋白在结构、功能、病理机制及实验模型中的应用，均为该领域经典研究。
**Background of Recombinant Tau Protein**
Tau is a microtubule-associated protein predominantly expressed in neurons of the central nervous system. Its primary role involves stabilizing microtubule structures, promoting their assembly, and maintaining cytoskeletal integrity and intracellular transport. In humans, the *MAPT* gene encodes six major tau isoforms through alternative splicing, ranging from 352 to 441 amino acids. These isoforms differ by the inclusion or exclusion of specific exons, leading to variations in microtubule-binding domains.
Pathologically, tau is implicated in neurodegenerative diseases termed *tauopathies*, including Alzheimer’s disease (AD), frontotemporal dementia (FTD), and corticobasal degeneration. In these disorders, tau undergoes abnormal post-translational modifications—such as hyperphosphorylation, truncation, or acetylation—leading to its dissociation from microtubules and aggregation into neurofibrillary tangles (NFTs). These insoluble aggregates disrupt neuronal function, contribute to synaptic loss, and correlate with disease progression.
Recombinant tau proteins are generated using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems. This approach allows precise control over isoform selection, modification sites (e.g., phosphorylation mimics), and tagging (e.g., fluorescent or affinity tags) for experimental applications. Recombinant tau serves as a critical tool for studying tau biochemistry, aggregation mechanisms, and interactions with microtubules or other partners *in vitro*. It also facilitates drug screening for tau-targeted therapies and the development of diagnostic assays.
The ability to produce purified, homogeneous tau variants has advanced structural studies (e.g., cryo-EM of fibrils) and mechanistic insights into tau pathology. However, challenges remain in replicating disease-specific post-translational modifications and mimicking the complex cellular environment. Ongoing research aims to refine recombinant tau models to better capture the molecular underpinnings of tauopathies and accelerate therapeutic development.
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