| 纯度 | > 97% by SDS-PAGE. |
| 种属 | Huamn |
| 靶点 | MAPT |
| Uniprot No | P10636 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-441aa |
| 氨基酸序列 | MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL |
| 预测分子量 | 51.9 kDa |
| 蛋白标签 | C-his |
| 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篇关于MAPT(微管相关蛋白tau)重组蛋白研究的代表性文献摘要：
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1. **文献名称**：*Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans*
**作者**：Goedert, M., et al.
**摘要**：该研究利用重组人tau蛋白，首次在体外证明硫酸化糖胺聚糖可诱导tau形成类似阿尔茨海默病的神经纤维缠结，揭示了tau异常聚集的分子机制。
2. **文献名称**：*Structure of Tau protein and assembly into paired helical filaments*
**作者**：Mandelkow, E.M., et al.
**摘要**：通过重组tau蛋白的X射线晶体学分析，阐明了tau蛋白的核心结构域及磷酸化修饰如何促进其聚集成病理性的双螺旋丝结构。
3. **文献名称**：*Tau oligomers impair memory and induce synaptic dysfunction via altering brain-derived neurotrophic factor*
**作者**：Kayed, R., et al.
**摘要**：研究利用重组tau蛋白制备寡聚体，证明其通过干扰神经营养因子通路导致突触功能障碍，揭示了tau寡聚体在神经退行性疾病中的毒性机制。
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这些文献涵盖了重组MAPT蛋白在病理纤维形成、结构解析及毒性机制研究中的关键应用。如需具体年份或补充更多研究，可进一步调整。
MAPT (microtubule-associated protein tau) is a neuronal protein encoded by the *MAPT* gene, primarily involved in stabilizing microtubules in axons, crucial for maintaining structural integrity and facilitating intracellular transport in neurons. Under physiological conditions, tau binds to tubulin, promoting microtubule assembly and regulating dynamics. However, abnormal post-translational modifications (e.g., hyperphosphorylation, truncation) or mutations in *MAPT* can lead to tau misfolding, aggregation, and the formation of neurofibrillary tangles (NFTs), a hallmark of neurodegenerative tauopathies such as Alzheimer’s disease, frontotemporal dementia, and progressive supranuclear palsy.
Recombinant MAPT proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, sequence-specific tau isoforms for research and therapeutic development. These proteins retain key functional domains, including microtubule-binding repeats and proline-rich regions, while enabling precise manipulation of phosphorylation sites or disease-associated mutations (e.g., P301L, R406W). Researchers utilize recombinant tau to study aggregation mechanisms, screen potential inhibitors, and model tau pathology in cellular or animal systems.
Advantages include batch consistency, scalability, and reduced ethical concerns compared to brain-derived tau. However, challenges remain in replicating native post-translational modifications and isoform diversity (e.g., six splice variants in the human brain). Current applications span drug discovery, biomarker validation, and structural studies using cryo-EM or NMR to elucidate tau-microtubule or tau-ligand interactions. As tau-targeted therapies gain momentum, recombinant MAPT proteins serve as indispensable tools for deciphering pathogenic pathways and advancing precision medicine for neurodegenerative diseases.
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