| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmD |
| Uniprot No | P0AG51 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-59aa |
| 氨基酸序列 | MAKTIKITQTRSAIGRLPKHKATLLGLGLRRIGHTVEREDTPAIRGMINAVSFMVKVEE |
| 预测分子量 | 33.5kDa |
| 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 rpmD 重组蛋白的示例参考文献(仅供参考，具体文献需通过学术数据库验证)：
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1. **标题**：*Expression and Structural Analysis of Recombinant rpmD in Bacillus subtilis*
**作者**：Miyazaki, T. et al.
**摘要**：研究通过大肠杆菌系统克隆并表达了枯草芽孢杆菌的 rpmD 基因，利用X射线晶体学解析了重组RpmD蛋白的三维结构，揭示了其在核糖体组装中的潜在作用。
2. **标题**：*Functional Characterization of rpmD in Mycobacterium tuberculosis*
**作者**：Smith, J. & Patel, R.
**摘要**：探讨了结核分枝杆菌中重组RpmD蛋白的功能，发现其缺失导致核糖体稳定性下降，并验证了其作为抗菌药物靶点的可能性。
3. **标题**：*Optimization of Recombinant rpmD Production in E. coli*
**作者**：Lee, S. et al.
**摘要**：系统优化了 rpmD 在大肠杆菌中的可溶性表达条件，比较了不同表达载体和诱导策略对蛋白产量的影响，为后续研究提供高效纯化方案。
4. **标题**：*Interactions between rpmD and Ribosomal RNA in Bacterial Stress Response*
**作者**：Johnson, A. & Müller, P.
**摘要**：通过体外重组实验，证明RpmD蛋白与16S rRNA的特定区域结合，可能在细菌应激条件下调节核糖体功能。
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**注意**：以上为模拟示例，实际文献需通过 **PubMed**、**Google Scholar** 或 **Web of Science** 等平台，以关键词“rpmD recombinant protein”“ribosomal protein L30”等检索。
The rpmD gene encodes the ribosomal protein L30. a component of the 50S subunit in bacterial ribosomes. As part of the ribosome, L30 plays a role in translation by facilitating subunit assembly, stabilizing rRNA structure, and participating in peptidyl transferase activity. In recombinant protein studies, rpmD-derived L30 is often expressed heterologously for structural or functional analyses. Recombinant L30 production typically involves cloning the rpmD gene into expression vectors (e.g., pET or pGEX systems) followed by expression in bacterial hosts like E. coli. Purification methods may include affinity chromatography tags (His-tag, GST-tag) or ion-exchange chromatography.
Research on recombinant L30 has provided insights into ribosome biogenesis and antibiotic mechanisms. Some studies focus on its interactions with rRNA or antibiotics targeting the 50S subunit, as ribosomal proteins are potential targets for novel antimicrobials. Structural analyses using recombinant L30 have helped map binding sites for antibiotics like macrolides and elucidate resistance mechanisms. Additionally, L30's role in autoregulation of its own synthesis through feedback inhibition of rpmD mRNA translation has been investigated using recombinant protein systems.
The conservation of rpmD across bacterial species makes it useful for evolutionary studies of ribosomal proteins. However, sequence variations in pathogenic bacteria have drawn attention to its potential as a species-specific therapeutic target. Current applications extend to structural biology (cryo-EM/X-ray crystallography), antibiotic discovery platforms, and synthetic biology approaches for engineered ribosomes. Ongoing research continues to explore L30's extra-ribosomal functions and regulatory roles in bacterial physiology.
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