| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | tuf1 |
| Uniprot No | A3M1F6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-396aa |
| 氨基酸序列 | MAKAKFERNKPHVNVGTIGHVDHGKTTLTAAIATICAKTYGGEAKDYSQIDSAPEEKARGITINTSHVEYDSPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMPQTREHILLSRQVGVPYIIVFLNKCDLVDDEELLELVEMEVRELLSTYDFPGDDTPVIRGSALAALNGEAGPYGEESVLALVAALDSYIPEPERAIDKAFLMPIEDVFSISGRGTVVTGRVEAGIIKVGEEVEIVGIKDTVKTTVTGVEMFRKLLDEGRAGENCGILLRGTKREEVQRGQVLAKPGTIKPHTKFDAEVYVLSKEEGGRHTPFLNGYRPQFYFRTTDVTGAIQLKEGVEMVMPGDNVEMSVELIHPIAMDPGLRFAIREGGRTVGAGVVAKVTA |
| 预测分子量 | 44.9 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TUF1重组蛋白的3篇参考文献的模拟示例(注：部分内容基于假设，实际文献需通过学术数据库验证)：
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1. **文献名称**：*"Heterologous Expression and Functional Characterization of Recombinant TUF1 in Saccharomyces cerevisiae"*
**作者**：Zhang, L. et al.
**摘要**：本研究利用酿酒酵母系统成功表达并纯化了重组TUF1蛋白。实验表明，重组TUF1能够恢复线粒体缺陷型酵母菌株的蛋白质翻译功能，证实其在维持线粒体翻译延伸过程中的关键作用。
2. **文献名称**：*"Recombinant TUF1 Protein Attenuates Oxidative Stress in Neuronal Cells via Mitochondrial Pathway Modulation"*
**作者**：Chen, H. & Wang, Y.
**摘要**：作者通过大肠杆菌表达系统获得高纯度重组TUF1.并发现其在神经元细胞模型中能够减少活性氧(ROS)积累，改善线粒体膜电位，提示其在神经退行性疾病治疗中的潜在应用。
3. **文献名称**：*"Structural and Functional Analysis of TUF1 Recombinant Protein Using Cryo-EM"*
**作者**：Smith, J. et al.
**摘要**：本研究通过冷冻电镜技术解析了重组TUF1的三维结构，揭示了其与线粒体核糖体相互作用的分子机制，为靶向TUF1的抗生素设计提供了结构基础。
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**注意事项**：
- 上述文献为假设性示例，实际研究中请通过**PubMed**、**Google Scholar**等平台检索真实文献(关键词：TUF1 recombinant protein, mitochondrial EF-Tu expression)。
- 若研究领域较新或小众，建议扩展检索词(如结合物种名或功能关键词，如“mitochondrial translation”)。
TUF1 (Tu Translation Elongation Factor, Mitochondrial) is a nuclear-encoded protein critical for mitochondrial protein synthesis. It functions as a translation elongation factor in mitochondrial ribosomes, facilitating the elongation phase of polypeptide chains during mitochondrial translation. Structurally, it belongs to the GTPase superfamily and shares homology with bacterial EF-Tu, reflecting its evolutionary conservation in supporting organellar gene expression. Mitochondria, as semi-autonomous organelles, rely on TUF1 for synthesizing key components of the electron transport chain (ETC), particularly subunits of Complexes I, III, IV, and V, which are essential for oxidative phosphorylation (OXPHOS) and cellular energy production.
Dysregulation of TUF1 has been implicated in mitochondrial disorders, neurodegenerative diseases, and cancer. Mutations or reduced expression of TUF1 can impair mitochondrial translation, leading to ETC dysfunction, bioenergetic deficits, and increased reactive oxygen species (ROS). In cancer, altered TUF1 levels are linked to metabolic reprogramming, a hallmark of tumor cells adapting to hypoxic or nutrient-poor microenvironments.
Recombinant TUF1 protein is produced using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) for functional studies. Its purification typically involves affinity chromatography tags (e.g., His-tag) followed by biochemical characterization. Researchers utilize recombinant TUF1 to investigate mitochondrial translation mechanisms, model diseases in vitro, screen therapeutic compounds targeting mitochondrial dysfunction, or develop diagnostic tools. Additionally, it serves as an antigen for antibody production in biomarker studies. Ongoing research aims to elucidate its post-translational modifications, interaction partners, and tissue-specific roles, offering insights into mitochondrial biology and therapeutic strategies for mitochondrial-related pathologies.
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