| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpsG |
| Uniprot No | P02359 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-179aa |
| 氨基酸序列 | PRRRVIGQRKILPDPKFGSELLAKFVNILMVDGKKSTAESIVYSALETLAQRSGKSELEAFEVALENVRPTVEVKSRRVGGSTYQVPVEVRPVRRNALAMRWIVEAARKRGDKSMALRLANELSDAAENKGTAVKKREDVHRMAEANKAFAHYRWLSLRSFSHQAGASSKQPALGYLN |
| 预测分子量 | 23.9 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. |
以下是模拟生成的关于rpsG重组蛋白的参考文献示例(非真实文献，仅供格式参考)：
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1. **标题**: *Cloning and Expression of the rpsG Gene Encoding Ribosomal Protein S7 in Escherichia coli*
**作者**: Smith J., et al.
**摘要**: 研究报道了通过PCR扩增大肠杆菌rpsG基因，构建重组质粒并在BL21(DE3)中诱导表达，纯化获得高纯度S7蛋白，验证其参与核糖体组装的生物学功能。
2. **标题**: *Structural Analysis of Recombinant S7 Protein and Its Interaction with 16S rRNA*
**作者**: Li X., et al.
**摘要**: 利用X射线晶体学解析重组S7蛋白的三维结构，结合体外结合实验证明其与16S rRNA特定区域的相互作用，为核糖体小亚基组装机制提供分子基础。
3. **标题**: *Functional Characterization of rpsG Mutants via Recombinant Protein Complementation*
**作者**: Garcia R., et al.
**摘要**: 通过构建rpsG点突变体并表达重组S7变体蛋白，验证其在核糖体缺陷型菌株中的功能互补性，揭示关键氨基酸残基对翻译活性的影响。
4. **标题**: *High-Yield Purification of Recombinant rpsG-Encoded Protein Using a Dual-Tag System*
**作者**: Wang Y., et al.
**摘要**: 开发了一种基于His/SUMO双标签的重组S7蛋白纯化策略，显著提高蛋白可溶性和产量，适用于大规模结构生物学研究。
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**注意**：以上内容为模拟示例，建议通过PubMed、Google Scholar等平台检索真实文献(关键词：rpsG, recombinant S7 protein, ribosomal protein expression)。
**Background of rpsG Recombinant Protein**
The *rpsG* gene encodes the ribosomal protein S7. a critical component of the 30S subunit in prokaryotic ribosomes. S7 plays a dual role in protein synthesis and ribosome assembly, contributing to the structural stability of the 30S subunit and participating in the binding of mRNA and tRNA during translation. Due to its essential function in bacterial growth, S7 has been studied as a potential target for antibiotic development.
Recombinant rpsG protein is produced through genetic engineering, typically by cloning the *rpsG* gene into expression vectors (e.g., plasmids) and expressing it in host systems like *Escherichia coli*. This approach enables large-scale production of the protein with high purity, bypassing the challenges of isolating it from native sources. The recombinant protein retains its biological activity, making it valuable for structural studies (e.g., X-ray crystallography or cryo-EM) to elucidate ribosome architecture and S7’s interaction with antibiotics or other molecules.
Research on rpsG recombinant protein has also advanced understanding of antibiotic resistance mechanisms. For instance, mutations in *rpsG* can alter ribosome function, reducing drug efficacy. Additionally, S7’s role in ribosomal RNA (rRNA) binding highlights its importance in ribosome biogenesis, offering insights into bacterial physiology. Beyond basic science, recombinant S7 is used in drug screening platforms to identify compounds that disrupt ribosomal function, aiding the development of novel antimicrobial agents.
The protein’s solubility and stability under experimental conditions further enhance its utility in biochemical assays. Furthermore, engineered variants (e.g., tagged or truncated forms) facilitate studies on protein-protein interactions or post-translational modifications. Overall, rpsG recombinant protein serves as a vital tool in microbiology, structural biology, and antibiotic discovery, bridging fundamental research and therapeutic applications.
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