| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | rplF |
| Uniprot No | P0AG55 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-175aa |
| 氨基酸序列 | SRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGADKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAK |
| 预测分子量 | 45.5 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rplF重组蛋白的参考文献示例：
1. **"Cloning and Functional Analysis of Recombinant RplF in Escherichia coli Ribosome Assembly"**
*作者：Smith A, et al. (2020)*
摘要：本研究成功克隆并表达了重组RplF蛋白，验证其在大肠杆菌核糖体组装中的关键作用，并通过体外实验证明其与23S rRNA的结合能力。
2. **"Crystal Structure of RplF Reveals Antibiotic Binding Sites in Pathogenic Bacteria"**
*作者：Johnson B, et al. (2018)*
摘要：通过X射线晶体学解析了重组RplF蛋白的三维结构，发现其与四环素类抗生素的相互作用位点，为靶向核糖体的药物设计提供依据。
3. **"Role of Recombinant RplF in Stress Adaptation of Bacillus subtilis"**
*作者：Lee C, et al. (2019)*
摘要：利用重组RplF蛋白进行功能研究，发现其在高温和氧化应激条件下对细菌生存的调控作用，表明RplF可能参与应激响应通路。
4. **"Immunogenicity Evaluation of Recombinant RplF as a Novel Vaccine Candidate"**
*作者：Zhang D, et al. (2021)*
摘要：在小鼠模型中评估重组RplF蛋白的免疫原性，结果显示其可诱导特异性抗体产生，提示其作为抗细菌感染疫苗的潜在应用价值。
(注：以上文献信息为示例性质，实际引用时需核实真实文献。)
The RplF recombinant protein is derived from the rplF gene, which encodes the ribosomal protein L6. a critical component of the 50S subunit in bacterial ribosomes. As part of the translation machinery, L6 contributes to ribosome assembly, peptidyl transferase activity, and interactions with tRNA or translation factors. Its structural and functional conservation across prokaryotes makes it a target for studying ribosome biology and antibiotic mechanisms.
Recombinant RplF is typically produced via heterologous expression in systems like E. coli, enabling high-yield purification for biochemical studies. Researchers utilize it to probe ribosomal architecture, particularly its role in maintaining subunit integrity and facilitating subunit association. Structural analyses (e.g., X-ray crystallography, cryo-EM) often employ recombinant L6 to resolve molecular details of antibiotic binding sites, as certain drugs (e.g., macrolides) target regions near L6.
Additionally, RplF has implications in antimicrobial development. By studying interactions between recombinant L6 and inhibitors, scientists identify compounds that disrupt ribosome function, potentially overcoming antibiotic resistance. Its role in bacterial fitness also links it to stress response pathways, offering insights into pathogen adaptation.
Beyond therapeutics, RplF serves as a model for evolutionary studies of ribosomal protein conservation and horizontal gene transfer. Engineering mutant variants helps delineate functional domains and assess resistance mutations. Overall, RplF recombinant protein bridges fundamental ribosome research with applied microbiological and pharmacological investigations.
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