| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | efp |
| Uniprot No | P0A6N4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-188aa |
| 氨基酸序列 | ATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK |
| 预测分子量 | 22.5 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. |
以下是模拟的EFP重组蛋白相关文献示例，供参考：
1. **《重组EFP蛋白在大肠杆菌中的高效表达及功能分析》**
作者：Smith J, et al.
摘要：研究通过优化密码子及诱导条件，实现了EFP蛋白在大肠杆菌中的高效可溶性表达，并证实其能显著提升宿主细胞对特定抗生素的耐受性。
2. **《EFP晶体结构揭示其翻译延伸机制》**
作者：Chen L, Wang H.
摘要：利用X射线衍射解析EFP重组蛋白的三维结构，阐明其通过结合核糖体促进多肽链延伸的分子机制，为靶向EFP的抗菌药物设计提供依据。
3. **《EFP缺失对细菌蛋白质组的影响研究》**
作者：Kim S, et al.
摘要：通过基因敲除及蛋白质组学分析，发现EFP缺失会导致细菌多聚脯氨酸序列翻译停滞，影响关键代谢通路蛋白的合成。
4. **《基于EFP重组蛋白的新型抗菌剂筛选平台构建》**
作者：Gomez R, et al.
摘要：开发了以重组EFP为靶点的高通量筛选系统，成功鉴定出多个小分子抑制剂，为抗耐药菌药物研发提供新策略。
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注：以上为模拟文献，实际研究请通过PubMed、Web of Science等平台检索关键词(如"EFP recombinant protein"、"Elongation Factor P expression")。
**Background of EFP Recombinant Protein**
Elongation Factor P (EF-P) is a conserved translation elongation factor critical for protein synthesis in bacteria and archaea. It facilitates the formation of peptide bonds, particularly during the translation of polyproline motifs (e.g., PPP or XPPX sequences), where ribosomes are prone to stalling due to structural constraints. EF-P binds to the ribosome and stabilizes transfer RNA (tRNA) positioning, enabling efficient polymerization of proline-rich sequences. Its function is analogous to eukaryotic elongation factor eIF5A, underscoring its evolutionary significance.
EFP recombinant protein refers to EF-P produced via recombinant DNA technology. By cloning the *efp* gene into expression vectors (e.g., *E. coli* or yeast systems), researchers generate purified, functional EF-P for structural and mechanistic studies. This approach allows large-scale production, enabling detailed investigations into EF-P's interactions with ribosomes, tRNA, and antibiotics targeting bacterial translation.
The study of EF-P has broad implications. First, it elucidates fundamental mechanisms of translation elongation, particularly under stress conditions where polyproline-containing proteins are upregulated. Second, EF-P is a potential antimicrobial target since its inactivation impairs bacterial viability and virulence. Inhibitors disrupting EF-P-ribosome interactions could pave the way for novel antibiotics. Third, recombinant EF-P aids in biotechnological applications, such as optimizing expression systems for hard-to-express proteins containing proline-rich domains.
Recent structural studies (e.g., cryo-EM analyses) have revealed EF-P's binding sites on ribosomes and its conformational dynamics during translation. These insights, combined with recombinant protein availability, accelerate drug discovery and enhance our understanding of translational regulation across life domains.
In summary, EFP recombinant protein serves as a vital tool for dissecting translation mechanisms, developing antimicrobial strategies, and improving protein production technologies.
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