| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpsS |
| Uniprot No | P0A7U3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-92aa |
| 氨基酸序列 | PRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK |
| 预测分子量 | 14.3 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rpsS重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅供参考格式)：
1. **文献名称**：*Expression and Purification of Recombinant rpsS in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：研究利用大肠杆菌表达系统高效表达并纯化重组rpsS蛋白，优化了诱导条件和亲和层析步骤，获得高纯度蛋白用于后续功能研究。
2. **文献名称**：*Structural Analysis of rpsS Reveals Its Role in Ribosome Assembly*
**作者**：Zhang L, et al.
**摘要**：通过X射线晶体学解析重组rpsS蛋白的三维结构，揭示了其与16S rRNA结合的关键区域，阐明其在核糖体组装中的分子机制。
3. **文献名称**：*Functional Interaction of rpsS with Antibiotic Resistance Proteins*
**作者**：Wang Y, et al.
**摘要**：利用表面等离子体共振(SPR)技术证明重组rpsS蛋白与多种抗生素耐药蛋白的相互作用，提示其在细菌耐药性调控中的潜在作用。
4. **文献名称**：*rpsS Knockout and Complementation Study in Bacterial Stress Response*
**作者**：Johnson R, et al.
**摘要**：构建rpsS基因敲除菌株，并通过重组rpsS蛋白回补实验验证其在氧化应激条件下对细菌生存的关键调控功能。
(注：以上文献为模拟内容，实际研究中建议通过PubMed、Web of Science等平台以关键词“rpsS recombinant protein”检索最新文献。)
The rpsS gene encodes the ribosomal protein S19. a critical component of the 30S subunit in bacterial ribosomes. As part of the small ribosomal subunit, S19 plays a pivotal role in protein synthesis by facilitating mRNA decoding and tRNA interactions during translation. In Escherichia coli, rpsS is highly conserved and essential for cell viability, underscoring its functional importance in ribosome assembly and stability.
Recombinant rpsS protein is produced through genetic engineering, typically by cloning the rpsS gene into expression vectors, followed by overexpression in bacterial hosts like E. coli. Purification methods, such as affinity chromatography with His-tag systems, yield high-purity, soluble protein for structural and functional studies. This recombinant approach allows precise control over protein production, enabling researchers to study S19 in isolation or within reconstituted ribosomal complexes.
Research on recombinant rpsS has provided insights into ribosome biogenesis, antibiotic targeting, and bacterial protein synthesis mechanisms. S19 is implicated in binding antibiotics like spectinomycin, making it a potential target for antimicrobial drug development. Additionally, studies leveraging recombinant S19 have explored its role in ribosomal subunit assembly and interactions with rRNA or other ribosomal proteins.
The protein’s conserved nature across prokaryotes also positions it as a model for understanding evolutionary adaptations in translation machinery. Overall, recombinant rpsS serves as a valuable tool for both basic research and applied biotechnology, bridging gaps between ribosomal biology, structural studies, and therapeutic innovation.
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