| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TARDBP |
| Uniprot No | Q13148 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-181aa |
| 氨基酸序列 | TVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSK |
| 预测分子量 | 21.8 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篇关于TARDBP(TDP-43)重组蛋白的关键文献概览：
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1. **文献名称**：*Structural characterization of the TDP-43 N-terminal domain*
**作者**：Mompeán et al. (2017)
**摘要**：通过核磁共振解析TDP-43 N端结构域(NTD)的构象，揭示其介导同源二聚化的分子机制，为重组TDP-43蛋白的功能研究提供结构基础。
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2. **文献名称**：*TDP-43 aggregation in neurodegeneration: Insights from in vitro recombinant protein models*
**作者**：Chhangani et al. (2019)
**摘要**：利用重组表达的人源TDP-43蛋白建立体外聚集模型，探究其病理性纤维化机制及与肌萎缩侧索硬化症(ALS)的相关性。
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3. **文献名称**：*High-yield purification of full-length TDP-43 from E. coli for biochemical and biophysical studies*
**作者**：Afroz et al. (2015)
**摘要**：开发一种高效大肠杆菌表达系统，获得高纯度全长TDP-43重组蛋白，优化纯化流程并验证其RNA结合活性，适用于体外功能实验。
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这些文献涵盖重组TDP-43的结构解析、病理机制研究和制备方法，可支撑相关研究的实验设计。
TARDBP (TAR DNA-binding protein 43), encoded by the TARDBP gene, is a ubiquitously expressed RNA/DNA-binding protein involved in transcriptional regulation, RNA splicing, transport, and stability. Its recombinant form, TARDBP recombinant protein, is artificially produced in laboratory systems (e.g., bacterial, mammalian) for functional and pathological studies. TDP-43 gained prominence due to its pathological role in neurodegenerative diseases: over 95% of amyotrophic lateral sclerosis (ALS) and ~50% of frontotemporal lobar degeneration (FTLD) cases exhibit cytoplasmic TDP-43 aggregates. These aggregates are hyperphosphorylated, ubiquitinated, and often fragmented, leading to loss of nuclear function and RNA processing defects.
Recombinant TDP-43 enables researchers to study its prion-like aggregation mechanisms, liquid-liquid phase separation properties, and interactions with proteins like hnRNPs or stress granule components. It is instrumental in modeling disease-associated mutations (e.g., G298S, A382T) linked to familial ALS, which accelerate aggregation or impair RNA-binding capacity. Structural studies using recombinant protein revealed its two RNA-recognition motifs (RRM1. RRM2) and C-terminal low-complexity domain critical for aggregation.
Pharmaceutical applications include screening small molecules to inhibit pathological aggregation or restore nuclear localization. Challenges remain in replicating post-translational modifications (e.g., phosphorylation) inherent to disease states, necessitating advanced expression systems. Overall, TARDBP recombinant protein serves as a vital tool to dissect ALS/FTLD pathogenesis and explore therapeutic strategies targeting TDP-43 proteotoxicity.
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