| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | tuf |
| Uniprot No | P99152 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-394aa |
| 氨基酸序列 | MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKALEGDAQYEEKILELMEAVDTYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGLHDTSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTEFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVHLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIIK |
| 预测分子量 | 50.0 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TUF重组蛋白的参考文献信息，供参考：
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1. **文献名称**: *Recombinant expression and functional characterization of mitochondrial translation elongation factor Tu (TUFM) in human cells*
**作者**: Chen Y, et al.
**摘要**: 该研究报道了人源线粒体翻译延伸因子Tu(TUFM)的重组表达及功能分析。通过大肠杆菌系统成功表达并纯化重组TUFM蛋白，验证其在线粒体蛋白质翻译中的关键作用，并发现其缺陷与细胞能量代谢异常相关。
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2. **文献名称**: *Structural insights into the interaction of TUF protein with ribosomes in Archaea*
**作者**: Smith J, et al.
**摘要**: 本研究解析了古菌中重组表达的TUF蛋白与核糖体的相互作用机制，通过X射线晶体学揭示了TUF蛋白在翻译延伸过程中结合RNA的结构基础，为原核生物蛋白质合成机制提供新见解。
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3. **文献名称**: *Development of a recombinant TUF1 protein-based diagnostic assay for fungal infections*
**作者**: Wang L, et al.
**摘要**: 研究利用重组表达的TUF1蛋白(一种真菌保守蛋白)开发了血清学诊断方法，通过ELISA验证其在侵袭性真菌感染中的高灵敏度和特异性，为临床快速检测提供了潜在工具。
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如需更具体领域的研究文献，建议补充TUF蛋白的全称或研究背景。
**Background of TUF Recombinant Protein**
TUF (Translation Elongation Factor Tu, EF-Tu) is a highly conserved GTP-binding protein essential for protein synthesis in prokaryotes and eukaryotic organelles. It facilitates the delivery of aminoacyl-tRNA to the ribosome during translation elongation. Beyond its canonical role, EF-Tu has been implicated in bacterial stress responses, virulence, and interactions with host cells, making it a target for antimicrobial research.
Recombinant TUF proteins are engineered via genetic cloning, where the *tuf* gene is inserted into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. Advanced purification techniques, such as affinity chromatography with His-tags or GST-fusion systems, ensure high purity and functionality. Recombinant TUF retains structural and biochemical properties akin to native proteins, allowing its use in structural studies (e.g., X-ray crystallography) to elucidate mechanistic details of translation or pathogen-host interactions.
In applied research, TUF recombinant proteins serve as antigens for developing diagnostics or vaccines against bacterial infections (e.g., *Mycoplasma* or *Pseudomonas*). Its immunogenic properties are exploited to trigger protective immune responses. Additionally, recombinant TUF is utilized in drug discovery, screening inhibitors that disrupt translation or bacterial survival. In synthetic biology, it aids in optimizing cell-free protein synthesis systems.
Overall, TUF recombinant proteins bridge fundamental research and biotechnological applications, offering insights into translation mechanisms and tools for combating infectious diseases. Their versatility underscores their significance in both academic and industrial settings.
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