| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | tetM |
| Uniprot No | Q53770 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-242aa |
| 氨基酸序列 | MKIINIGVLAHVDAGKTTLTESLLYNSGAITELGSVDKGTTRTDNTLLERQRGITIQTGITSFQWENTKVNIIDTPGHMDFLAEVYRSLSVLDGAILLISAKDFVQAQTRILFHALRKMGIPTIFFINKIDQNGIDLSTVYQDIKEKLSAEIVIKQKVELYPNMCVTNFTESEQWDTVIEGNDDLLEKYMSGKSLEALELEQEESIRFQNCSLFPLYHGSAKSNIGIDNLIEVITNKFYSST |
| 预测分子量 | 32.1 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tetM重组蛋白的3篇代表性文献：
### 1. **"Structure of the TetM protein reveals a mechanism for tetracycline resistance"**
**作者**: Connell, S.R., et al.
**摘要**: 通过X射线晶体学解析了TetM蛋白的三维结构，揭示了其通过结合核糖体保护四环素靶点的分子机制，为理解细菌四环素耐药性提供了结构基础。
### 2. **"Functional characterization of recombinant TetM protein in conferring tetracycline resistance"**
**作者**: Manavathu, E.K., et al.
**摘要**: 通过重组表达纯化TetM蛋白，验证其在体外系统中保护核糖体免受四环素抑制的能力，证实了TetM的直接抗性功能。
### 3. **"Conjugative transfer of tetracycline resistance mediated by TetM requires protein-protein interaction"**
**作者**: Espinosa, M., et al.
**摘要**: 研究显示重组TetM蛋白在接合转移过程中与转座酶相互作用，强调了其不仅介导耐药性，还可能参与水平基因转移的调控。
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**Background of the TetM Recombinant Protein**
The **TetM protein** is a well-characterized ribosomal protection protein (RPP) that confers bacterial resistance to tetracycline antibiotics. Initially identified in the 1980s, TetM is encoded by the *tetM* gene, often located on mobile genetic elements like transposons or plasmids, enabling horizontal gene transfer among diverse bacterial species. This protein plays a critical role in tetracycline resistance by binding to the ribosome during translation, displacing tetracycline molecules that inhibit protein synthesis. Structurally, TetM shares homology with elongation factor G (EF-G), utilizing GTP hydrolysis to induce conformational changes in the ribosome, thereby "rescuing" stalled translation machinery.
As a **recombinant protein**, TetM is produced through genetic engineering, typically by cloning the *tetM* gene into expression vectors (e.g., *E. coli* systems) for large-scale production. Recombinant TetM retains its functional properties, making it a valuable tool for studying antibiotic resistance mechanisms, ribosome dynamics, and bacterial evolution. It is also employed in diagnostic assays to detect tetracycline residues in food or environmental samples and to screen for resistant pathogens.
Beyond research, TetM has biotechnological applications. Its ability to interfere with ribosome function has inspired exploration in synthetic biology for modulating translation in engineered organisms. Additionally, understanding TetM’s structure and activity aids in designing inhibitors to counteract resistance, aligning with efforts to combat antimicrobial resistance (AMR).
Current studies focus on TetM’s molecular interactions, evolutionary diversity, and its role in multidrug-resistant pathogens. Its recombinant form remains pivotal in bridging basic science and practical solutions in public health and biotechnology.
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