| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpsO |
| Uniprot No | P0ADZ4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-89aa |
| 氨基酸序列 | SLSTEATAKIVSEFGRDANDTGSTEVQVALLTAQINHLQGHFAEHKKDHHSRRGLLRMVSQRRKLLDYLKRKDVARYTQLIERLGLRR |
| 预测分子量 | 14.1 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. |
以下为模拟生成的参考文献示例，建议通过学术数据库获取真实文献：
1. **标题**: "Cloning and expression of the rpsO gene encoding ribosomal protein S15 in Escherichia coli"
**作者**: Smith J, et al.
**摘要**: 报道了rpsO基因在大肠杆菌中的重组克隆与表达，优化了蛋白可溶性表达条件，并通过亲和层析获得高纯度S15蛋白。
2. **标题**: "Crystal structure analysis of recombinant RpsO protein from Bacillus subtilis"
**作者**: Lee S, et al.
**摘要**: 解析了枯草芽孢杆菌RpsO重组蛋白的晶体结构，揭示了其与16S rRNA结合的潜在作用位点及构象变化机制。
3. **标题**: "Functional characterization of RpsO in stress response through recombinant protein interaction studies"
**作者**: Garcia R, et al.
**摘要**: 利用重组RpsO蛋白进行体外互作实验，证明其通过与RNA解旋酶结合参与细菌氧化应激反应调控。
4. **标题**: "High-yield production of RpsO using a novel E. coli expression system"
**作者**: Wang Y, et al.
**摘要**: 开发新型原核表达系统，显著提升重组RpsO蛋白产量，并验证其用于体外核糖体组装的功能活性。
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实际文献可通过 **PubMed** 或 **Google Scholar** 以关键词 "rpsO recombinant protein" / "ribosomal protein S15 expression" 检索。
**Background of RpsO Recombinant Protein**
The RpsO protein, encoded by the *rpsO* gene, is a ribosomal component found in various bacterial species, notably in *Escherichia coli* and other Gram-negative bacteria. As part of the 30S ribosomal subunit, RpsO (ribosomal protein S15) plays a critical role in translation by stabilizing the binding of mRNA and initiator tRNA during ribosome assembly. Beyond its ribosomal function, RpsO is involved in transcriptional regulation, particularly in the stringent response under stress conditions. For example, in *E. coli*, RpsO interacts with the alarmone (p)ppGpp and regulates the expression of stress-responsive genes, linking translational machinery to cellular adaptation.
The production of recombinant RpsO protein has become essential for structural and functional studies. Using molecular cloning techniques, the *rpsO* gene is expressed in heterologous systems (e.g., *E. coli*), often fused with affinity tags (e.g., His-tag) to facilitate purification. Recombinant RpsO enables detailed analysis of its interaction networks, such as binding to rRNA or regulatory proteins, and its role in stress signaling. Structural studies (e.g., X-ray crystallography, NMR) using recombinant RpsO have provided insights into its conformational dynamics and ligand-binding mechanisms.
Additionally, RpsO is studied as a potential antimicrobial target due to its conserved role in bacterial translation and stress survival. Its recombinant form is also utilized in synthetic biology for engineering ribosome variants or designing novel regulatory circuits. Challenges in RpsO production, such as solubility or aggregation, are addressed through codon optimization, fusion partners, or chaperone co-expression. Overall, recombinant RpsO serves as a versatile tool for exploring bacterial physiology, antibiotic development, and ribosome-related biotechnology applications.
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