| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmI |
| Uniprot No | P0A7Q1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 7-64aa |
| 氨基酸序列 | VRGAAKRFKKTGKGGFKHKHANLRHILTKKATKRKRHLRPKAMVSKGDLGLVIACLPY |
| 预测分子量 | 33.5 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rpmI重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
1. **《Cloning and expression of recombinant rpmI in Escherichia coli》**
- 作者：Smith A, et al.
- 摘要：研究报道了rpmI(编码核糖体蛋白L35)基因的克隆及在大肠杆菌中的可溶性表达，优化了重组蛋白的纯化条件，并验证其与核糖体亚基的相互作用。
2. **《Structural analysis of RPMI protein from Mycobacterium tuberculosis》**
- 作者：Zhang L, et al.
- 摘要：通过X射线晶体学解析了结核分枝杆菌RPMI蛋白的三维结构，揭示了其在核糖体组装中的关键作用，为新型抗菌药物靶点开发提供依据。
3. **《Functional characterization of RPMI in bacterial growth and stress response》**
- 作者：Wang Y, et al.
- 摘要：利用基因敲除和回补实验，证明rpmI对细菌正常生长和氧化应激耐受性至关重要，重组RPMI蛋白可恢复突变株的表型缺陷。
4. **《RPMI as a potential vaccine candidate against Staphylococcus aureus》**
- 作者：Kim H, et al.
- 摘要：评估重组RPMI蛋白作为金黄色葡萄球菌疫苗的潜力，动物实验显示其能诱导保护性免疫应答并降低感染小鼠的细菌载量。
**说明**：以上内容为模拟生成，实际文献需通过PubMed、Web of Science等数据库检索。建议用关键词"rpmI recombinant protein"或"ribosomal protein L35"结合研究领域(如结构/功能/应用)筛选文献。
**Background of rpmI Recombinant Protein**
The rpmI gene encodes the ribosomal protein L35. a conserved component of the bacterial 50S ribosomal subunit. As part of the ribosome’s structural and functional core, L35 plays a critical role in protein synthesis by stabilizing ribosomal architecture and facilitating interactions during translation. In bacteria, rpmI is essential for viability, as its deletion disrupts ribosome assembly, impairing cell growth and survival.
Recombinant rpmI protein is produced through genetic engineering, typically by cloning the rpmI gene into expression vectors (e.g., plasmids) and expressing it in host systems like *Escherichia coli*. This approach allows large-scale production of the protein for functional and structural studies. The recombinant protein is often purified using affinity tags (e.g., His-tag) and validated via techniques such as SDS-PAGE or mass spectrometry.
Research on rpmI focuses on its role in ribosome biogenesis, antibiotic resistance, and bacterial physiology. Since ribosomes are key targets for antibiotics, understanding L35’s structure and interactions aids in studying drug mechanisms or designing novel antimicrobials. For example, certain antibiotics bind to the 50S subunit, and mutations in rpmI have been linked to resistance in some pathogens.
Additionally, rpmI recombinant protein serves as a tool in structural biology (e.g., X-ray crystallography or cryo-EM) to resolve ribosome assembly dynamics. It also has applications in synthetic biology for engineering minimal ribosomes or studying evolutionary conservation across species.
Overall, rpmI recombinant protein bridges fundamental microbiology with translational research, offering insights into bacterial survival mechanisms and therapeutic development.
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