| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rpsE |
| Uniprot No | A6QJ75 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-163aa |
| 氨基酸序列 | MARREEETKEFEERVVTINRVAKVVKGGRRFRFTALVVVGDKNGRVGFGTGKAQEVPEAIKKAVEAAKKDLVVVPRVEGTTPHTITGRYGSGSVFMKPAAPGTGVIAGGPVRAVLELAGITDILSKSLGSNTPINMVRATIDGLQNLKNAEDVAKLRGKTVEE |
| 预测分子量 | 24.8 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rpsE重组蛋白的3篇参考文献示例：
1. **"Expression and purification of recombinant ribosomal protein S5 (rpsE) from Escherichia coli"**
- **作者**: Smith A, et al.
- **摘要**: 研究通过大肠杆菌表达系统克隆并纯化rpsE蛋白，优化了诱导条件与亲和层析步骤，为后续结构功能研究提供高纯度蛋白。
2. **"Structural insights into ribosomal protein S5 in antibiotic resistance"**
- **作者**: Johnson R, et al.
- **摘要**: 利用重组rpsE蛋白进行X射线晶体学分析，揭示其突变体与链霉素结合的分子机制，阐明其在细菌耐药性中的作用。
3. **"Functional characterization of rpsE in ribosome assembly using recombinant protein reconstitution"**
- **作者**: Lee H, et al.
- **摘要**: 通过体外重组rpsE与16S rRNA结合实验，证明该蛋白对30S核糖体亚基的组装具有关键调控功能。
(注：以上文献为示例，实际引用需根据具体研究检索PubMed、Google Scholar等数据库。)
**Background of RpsE Recombinant Protein**
RpsE, a ribosomal protein component of the 30S subunit in prokaryotes, is encoded by the *rpsE* gene and plays a critical role in translation fidelity and ribosome assembly. In *Escherichia coli*, RpsE (also known as ribosomal protein S5) stabilizes the structure of the 16S rRNA and interacts with other ribosomal proteins to ensure proper decoding during protein synthesis. Mutations in *rpsE* have been linked to antibiotic resistance, particularly to streptomycin, by altering ribosome conformation and reducing drug-binding affinity.
Recombinant RpsE protein is produced through genetic engineering, typically by cloning the *rpsE* gene into expression vectors (e.g., plasmids) and expressing it in heterologous hosts like *E. coli*. This allows large-scale production of the protein for functional and structural studies. Researchers often employ affinity chromatography tags (e.g., His-tag) to purify the recombinant protein efficiently.
Studies on RpsE have focused on its role in ribosome function, antibiotic resistance mechanisms, and interactions with RNA or other ribosomal proteins. Structural analyses, including X-ray crystallography and cryo-EM, have revealed its binding sites on rRNA and its conformational changes during translation. Additionally, RpsE serves as a model to investigate post-translational modifications and stress responses in bacteria.
Beyond basic research, recombinant RpsE is utilized in drug discovery, particularly in screening compounds targeting bacterial ribosomes. Its conserved nature across pathogens makes it a potential candidate for developing broad-spectrum antimicrobial agents. Understanding RpsE's dynamics also contributes to synthetic biology, enabling the design of engineered ribosomes for industrial protein production. Overall, RpsE recombinant protein is a vital tool for exploring prokaryotic translation and advancing antimicrobial strategies.
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