| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmB |
| Uniprot No | P0A7M2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-78aa |
| 氨基酸序列 | SRVCQVTGKRPVTGNNRSHALNATKRRFLPNLHSHRFWVESEKRFVTLRVSAKGMRVIDKKGIDTVLAELRARGEKY |
| 预测分子量 | 35.9 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3篇模拟的关于rpmB重组蛋白研究的参考文献(信息为学术模拟，供参考)：
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1. **文献名称**: "Expression and purification of recombinant rpmB protein in Escherichia coli"
**作者**: Zhang L, et al.
**摘要**: 研究报道了利用大肠杆菌表达系统高效表达rpmB基因编码的核糖体蛋白L28.通过优化诱导条件和纯化步骤，获得高纯度重组蛋白，并验证其与RNA结合的生物学活性，为后续功能研究奠定基础。
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2. **文献名称**: "Structural characterization of rpmB-encoded ribosomal protein L28 and its interaction with 23S rRNA"
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析了重组rpmB蛋白(L28)的三维结构，并发现其C端结构域在稳定23S rRNA特定区域中起关键作用，揭示了该蛋白在核糖体组装中的分子机制。
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3. **文献名称**: "Functional analysis of rpmB deletion mutants in bacterial stress response"
**作者**: Müller S, et al.
**摘要**: 构建了rpmB基因缺失的大肠杆菌突变株，发现重组表达的rpmB蛋白可恢复突变株在高温和高盐胁迫下的生长缺陷，表明L28蛋白参与细菌环境适应性的调控。
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**备注**：以上文献信息为模拟生成，实际研究需通过PubMed、Web of Science等平台检索关键词如"rpmB recombinant protein"或"ribosomal protein L28"获取准确数据。
**Background of rpmB Recombinant Protein**
The rpmB gene encodes a ribosomal protein belonging to the L28 family, a component of the 50S subunit in bacterial ribosomes. Ribosomal proteins like RpmB play essential roles in translation, ribosome assembly, and structural stability. In *Bacillus subtilis* and other bacteria, rpmB is part of a conserved genomic cluster involved in stress responses and cellular adaptation.
Recombinant RpmB protein is produced using genetic engineering techniques, typically by cloning the rpmB gene into expression vectors (e.g., *E. coli* systems) followed by purification via affinity chromatography. This approach allows large-scale production of the protein for functional and structural studies. Research on RpmB has focused on its role in ribosome biogenesis, interactions with rRNA, and potential contributions to antibiotic resistance. For instance, ribosomal proteins are often targets of antibiotics, and understanding RpmB's structure-function relationships could inform drug development.
Additionally, rpmB has been studied in the context of bacterial persistence and dormancy. Under stress conditions, such as nutrient limitation, ribosomal protein dynamics may influence bacterial survival strategies. Recombinant RpmB enables biochemical assays, crystallography, and mutagenesis studies to dissect these mechanisms.
Despite its conserved role, rpmB is not always essential in all bacterial species, suggesting functional redundancy or context-dependent roles. This variability makes it a subject of interest in comparative genomics and evolutionary biology. Overall, rpmB recombinant protein serves as a tool to explore fundamental ribosomal biology, antimicrobial targets, and bacterial stress adaptation pathways.
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