| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmG |
| Uniprot No | P0A7N9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-54aa |
| 氨基酸序列 | AKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKI |
| 预测分子量 | 33.1 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rpmG重组蛋白的示例参考文献(内容为虚构示例，仅供参考)：
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1. **文献名称**: *Structural and functional analysis of the ribosomal protein L33 (rpmG) in Escherichia coli*
**作者**: Zhang L, et al.
**摘要**: 本研究解析了大肠杆菌rpmG编码的L33核糖体蛋白的晶体结构，揭示了其与rRNA结合的特定结构域，并证明其缺失会导致细菌生长抑制。
2. **文献名称**: *Heterologous expression and purification of recombinant rpmG protein in Bacillus subtilis*
**作者**: Tanaka K, et al.
**摘要**: 报道了在枯草芽孢杆菌系统中高效表达重组rpmG蛋白的优化方法，通过亲和层析纯化获得高纯度蛋白，为后续功能研究提供材料基础。
3. **文献名称**: *Role of rpmG in bacterial stress response: Insights from gene knockout experiments*
**作者**: Müller S, et al.
**摘要**: 通过敲除rpmG基因发现其参与细菌对高温和氧化应激的适应性，重组蛋白回补实验证实了L33在应激响应中的调控作用。
4. **文献名称**: *Targeting rpmG for novel antimicrobial drug discovery*
**作者**: Gupta R, et al.
**摘要**: 筛选了靶向rpmG蛋白的小分子抑制剂，发现部分化合物可通过干扰核糖体组装抑制病原菌增殖，提示其作为抗菌药物靶点的潜力。
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注：以上文献为示例，实际研究需通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of rpmG Recombinant Protein**
The rpmG gene encodes a small ribosomal protein, L33. which is a component of the 50S subunit in bacterial ribosomes. As a highly conserved protein across prokaryotes, L33 plays a structural or functional role in ribosome assembly, stability, or translation regulation, though its precise mechanistic contributions remain less characterized compared to other ribosomal proteins. Studies suggest that L33 may interact with rRNA or other ribosomal proteins to maintain ribosome integrity, and its deletion or mutation can affect bacterial growth under stress conditions.
Recombinant rpmG protein (rpmG) is typically produced via heterologous expression in systems like *E. coli*, enabling large-scale purification for functional or structural studies. Generating recombinant rpmG is valuable for exploring its role in ribosome biology, antibiotic resistance mechanisms, or interactions with antibiotics that target the ribosome. For instance, certain macrolides or peptide antibiotics are known to bind near L33. making rpmG a potential target for studying drug-ribosome interactions.
Additionally, rpmG has garnered interest in synthetic biology and biotechnology. Engineered variants of L33 could be used to develop orthogonal ribosomes for specialized translation systems or to probe ribosome function in vivo. Its small size and solubility also make it a candidate for structural analyses, such as NMR or X-ray crystallography, to resolve ribosome assembly dynamics.
Despite its importance, challenges persist in studying rpmG, including its tendency to aggregate or its low abundance in native ribosomes. Recombinant expression systems help overcome these limitations, providing purified protein for biochemical assays. Recent advances in cryo-EM have further enabled visualization of L33 within ribosomal complexes, shedding light on its conformational flexibility during translation.
Overall, rpmG recombinant protein serves as a critical tool for dissecting bacterial ribosome function, antibiotic development, and understanding fundamental processes in protein synthesis.
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