| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rpmF |
| Uniprot No | P0A7N4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-57aa |
| 氨基酸序列 | AVQQNKPTRSKRGMRRSHDALTAVTSLSVDKTSGEKHLRHHITADGYYRGRKVIAK |
| 预测分子量 | 33.3 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. |
以下为3篇与rpmF(核糖体蛋白L32)重组蛋白相关的文献示例(注：部分内容为模拟概括，仅供参考)：
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1. **标题**: *Heterologous Expression and Purification of rpmF in Escherichia coli*
**作者**: Zhang, L. et al.
**摘要**: 本研究成功构建了携带rpmF基因的重组质粒，利用大肠杆菌BL21(DE3)表达系统实现高效可溶性表达，并通过镍柱亲和层析纯化获得高纯度重组蛋白，为后续功能研究奠定基础。
2. **标题**: *Structural Analysis of rpmF in Bacterial Ribosome Assembly*
**作者**: Tanaka, K. & Watanabe, S.
**摘要**: 通过X射线晶体学解析了重组rpmF蛋白的三维结构，发现其C端结构域在核糖体亚基组装中与23S rRNA特异性结合，揭示了其在翻译调控中的潜在作用。
3. **标题**: *Functional Characterization of rpmF in Antibiotic Resistance*
**作者**: Müller, R. et al.
**摘要**: 实验表明，重组rpmF蛋白与庆大霉素类抗生素存在直接相互作用，其过量表达可降低药物对核糖体的结合效率，提示rpmF可能参与细菌耐药性调控通路。
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**备注**：若需真实文献，建议通过PubMed或Google Scholar以关键词“rpmF recombinant protein”、“ribosomal protein L32 expression”进行检索，并筛选近年研究。
**Background of rpmF Recombinant Protein**
The rpmF gene encodes the ribosomal protein L32. a conserved component of the 50S subunit in bacterial ribosomes. As part of the ribosome, L32 plays a structural and functional role in protein synthesis, contributing to ribosome assembly, stability, and interaction with translational machinery. In *Escherichia coli* and other bacteria, rpmF is typically co-transcribed with adjacent genes in the *str* operon, reflecting its essential role in cellular viability.
Recombinant rpmF protein is produced via genetic engineering, often using heterologous expression systems like *E. coli*. The gene is cloned into expression vectors, allowing controlled overexpression under inducible promoters. Following purification (e.g., affinity chromatography with His-tags), the recombinant protein serves as a tool for studying ribosome structure, function, and biogenesis. Its applications extend to exploring antibiotic targets, as ribosomal proteins are critical for bacterial survival and are potential sites for drug development.
Research on rpmF also addresses its regulatory roles. In some bacteria, L32 autoregulates its expression by binding to its mRNA, inhibiting translation—a feedback mechanism to maintain protein homeostasis. Structural studies of recombinant rpmF have provided insights into RNA-protein interactions and ribosome assembly dynamics.
Challenges in working with rpmF include ensuring proper folding and solubility, as ribosomal proteins often require chaperones for stability. Despite this, recombinant rpmF remains valuable for elucidating bacterial translation mechanisms and developing antimicrobial strategies. Its study bridges fundamental microbiology and applied biotechnology, highlighting the importance of ribosomal components in both cellular processes and therapeutic innovation.
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