| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmE |
| Uniprot No | P0A7M9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-70aa |
| 氨基酸序列 | MKKDIHPKYEEITASCSCGNVMKIRSTVGHDLNLDVCSKCHPFFTGKQRDVATGGRVDRFNKRFNIPGSK |
| 预测分子量 | 34.9 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rpmE重组蛋白的示例参考文献(注：以下内容为模拟生成，实际文献需通过学术数据库查询)：
1. **《重组表达大肠杆菌核糖体蛋白L31(rpmE)及其纯化研究》**
- 作者：Smith J, et al.
- 摘要：研究通过克隆rpmE基因至表达载体，在大肠杆菌中实现高效可溶性表达，并利用亲和层析技术纯化获得高纯度重组蛋白，为核糖体组装机制研究提供材料。
2. **《rpmE蛋白的结构与功能分析》**
- 作者：Zhang L, et al.
- 摘要：采用X射线晶体学解析了重组rpmE蛋白的三维结构，揭示其与核糖体RNA结合的特定区域，并探讨其在翻译过程中的潜在调控作用。
3. **《rpmE缺失对细菌抗生素敏感性的影响》**
- 作者：Wang Y, et al.
- 摘要：通过构建rpmE缺陷型菌株，发现该蛋白缺失可增强细菌对特定氨基糖苷类抗生素的敏感性，提示rpmE在耐药性中的潜在角色。
4. **《重组rpmE与伴侣蛋白DnaK的相互作用研究》**
- 作者：Kim S, et al.
- 摘要：通过体外实验证实重组rpmE蛋白与分子伴侣DnaK存在直接结合，推测该互作可能参与维持核糖体蛋白的稳定性及正确折叠。
建议通过PubMed、Web of Science等平台以关键词“rpmE recombinant”“ribosomal protein L31”检索最新实证研究。
**Background of rpmE Recombinant Protein**
The *rpmE* gene encodes the ribosomal protein L31. a conserved component of the 50S subunit in prokaryotic ribosomes. As part of the translation machinery, L31 contributes to ribosome assembly, stability, and function. In bacteria, ribosomal proteins like L31 are often constitutively expressed under normal growth conditions, reflecting their essential role in protein synthesis. However, *rpmE* has garnered attention due to its unique structural features and potential regulatory roles. For instance, some bacterial L31 proteins contain a zinc-binding motif, suggesting involvement in metal ion homeostasis or stress responses.
Recombinant rpmE protein is typically produced via heterologous expression in *E. coli* or other host systems. The gene is cloned into expression vectors, often fused with affinity tags (e.g., His-tag) for purification. This enables large-scale production of the protein for functional and structural studies. Researchers have utilized rpmE recombinant protein to investigate its interactions with RNA or other ribosomal components, shedding light on ribosome biogenesis and translational fidelity.
Beyond basic science, rpmE has implications in antimicrobial drug development. Since ribosomes are targets for antibiotics, understanding L31’s role could inform strategies to combat bacterial resistance. Additionally, studies have explored rpmE’s potential as a diagnostic marker or vaccine candidate in pathogenic species.
Recent advances in structural biology, such as cryo-EM, have further elucidated L31’s conformational dynamics within the ribosome. These insights highlight its adaptability during translation elongation and its interactions with elongation factors like EF-Tu or EF-G.
In summary, rpmE recombinant protein serves as a critical tool for dissecting ribosomal function, bacterial physiology, and evolutionary conservation, with applications spanning biotechnology, medicine, and molecular biology. Ongoing research continues to uncover its multifaceted roles in microbial systems.
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