| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmC |
| Uniprot No | P0A7M6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-63aa |
| 氨基酸序列 | MKAKELREKSVEELNTELLNLLREQFNLRMQAASGQLQQSHLLKQVRRDVARVKTLLNEKAGA |
| 预测分子量 | 34.3 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rpmC重组蛋白的虚构参考文献示例(注：内容为模拟创作，非真实文献)：
1. **《Functional characterization of recombinant rpmC in ribosome stabilization》**
- 作者：T. Müller et al.
- 摘要：通过在大肠杆菌中重组表达rpmC蛋白，验证其作为核糖体L28亚基对50S核糖体稳定性的关键作用，并发现其缺失导致氨基糖苷类抗生素敏感性升高。
2. **《Structural insights into rpmC-antibiotic interactions using recombinant protein》**
- 作者：A. Gupta & S. Lee
- 摘要：利用重组rpmC蛋白进行体外结合实验，首次证明其直接结合红霉素类药物，揭示了该蛋白在抗生素作用靶点中的新功能。
3. **《High-yield production of rpmC recombinant protein for structural studies》**
- 作者：J. Park et al.
- 摘要：优化毕赤酵母表达系统实现rpmC蛋白毫克级纯化，通过X射线晶体学解析2.1Å分辨率结构，发现其C端螺旋在核糖体装配中的关键构象变化。
(注：实际研究中建议通过PubMed或Web of Science以"rpmC recombinant protein"为关键词检索真实文献。)
**Background of rpmC Recombinant Protein**
The rpmC gene encodes the ribosomal protein L29. a component of the 50S subunit in bacterial ribosomes. In *Escherichia coli*, rpmC plays a structural role in ribosome assembly and contributes to translation fidelity by stabilizing rRNA interactions. As a conserved bacterial protein, rpmC has drawn attention in studies exploring ribosome biology, antibiotic development, and protein synthesis mechanisms.
Recombinant rpmC protein is typically produced using heterologous expression systems, such as *E. coli*, due to its simplicity and cost-effectiveness. The gene is cloned into expression vectors under inducible promoters (e.g., T7 or lac), allowing controlled overexpression. Affinity tags (e.g., His-tag) are often fused to the protein to facilitate purification via immobilized metal affinity chromatography (IMAC). Post-purification steps may include tag removal and refolding, depending on downstream applications.
Research applications of rpmC recombinant protein include structural studies (e.g., X-ray crystallography, cryo-EM) to resolve ribosome architecture, as well as functional assays to investigate its role in translation or interactions with antibiotics. Its conserved nature also makes it a potential target for designing novel antimicrobial agents that disrupt ribosome function.
Challenges in rpmC recombinant production include ensuring proper folding and solubility, as ribosomal proteins often require specific chaperones or conditions for stability. Advances in expression optimization, solubility tags, and high-throughput screening have mitigated these issues, enabling broader use in both academic and industrial settings.
Overall, rpmC recombinant protein serves as a valuable tool for dissecting ribosome mechanics and developing strategies to combat bacterial infections, highlighting its significance in molecular microbiology and drug discovery.
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