| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | yebF |
| Uniprot No | P33219 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-118aa |
| 氨基酸序列 | ANNETSKSVTFPKCEDLDAAGIAASVKRDYQQNRVARWADDQKIVGQADP VAWVSLQDIQGKDDKWSVPLTVRGKSADIHYQVSVDCKAGMAEYQRR |
| 预测分子量 | 16 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 **yebF重组蛋白** 的参考文献示例(部分文献信息为模拟概括，实际引用时请核对原文)：
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1. **文献名称**：*Efficient secretion of recombinant proteins in E. coli using a YebF signal peptide-based system*
**作者**：Zhang Y, et al.
**摘要**：研究报道了一种基于大肠杆菌yebF信号肽的重组蛋白分泌系统，通过将目标蛋白与yebF融合，成功实现蛋白高效分泌至胞外培养基，简化了后续纯化步骤，并显著提高可溶性蛋白产量。
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2. **文献名称**：*YebF-mediated secretion of antimicrobial peptides in Escherichia coli: A novel strategy for heterologous expression*
**作者**：Li H, et al.
**摘要**：本文利用yebF作为分泌载体，在大肠杆菌中实现了抗菌肽(如cecropin)的分泌表达，显著降低了宿主细胞毒性，同时证明了yebF系统在表达毒性蛋白中的潜在优势。
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3. **文献名称**：*Comparative analysis of YebF with other secretion signals for recombinant protein production*
**作者**：Wang X, et al.
**摘要**：研究比较了yebF信号肽与PelB、OmpA等传统分泌信号的效果，发现yebF在特定蛋白(如单链抗体)的分泌效率上更具优势，尤其在低诱导温度条件下可减少包涵体形成。
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4. **文献名称**：*Mechanistic insights into YebF-dependent protein secretion in E. coli*
**作者**：Chen L, et al.
**摘要**：通过分子机制研究揭示了yebF介导的蛋白分泌途径，提出其可能通过非经典分泌途径绕过周质空间直接释放至胞外，为优化重组蛋白分泌提供了理论依据。
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**注意**：以上文献信息为模拟生成，实际研究中建议通过 **PubMed**、**Google Scholar** 或 **Web of Science** 以关键词“yebF recombinant protein secretion”检索最新权威文献。
The YebF protein, originally identified in *Escherichia coli*, is a small, soluble bacterial secretory protein that has gained attention in biotechnology for its unique secretion properties. Discovered in the early 2000s, YebF is naturally secreted into the extracellular medium via a non-classical pathway independent of the Sec or Tat systems, bypassing energy-dependent mechanisms. This autonomous secretion feature makes YebF an attractive candidate for recombinant protein production and secretion engineering.
In recombinant protein technology, YebF is often utilized as a fusion partner to enhance the solubility and secretion efficiency of heterologous proteins. When fused to target proteins, the YebF domain facilitates their transport across the bacterial membrane into the culture supernatant, simplifying downstream purification processes. This is particularly advantageous for producing proteins prone to aggregation in the cytoplasm, such as disulfide-bonded eukaryotic proteins. Additionally, YebF-driven secretion reduces intracellular proteolytic degradation and minimizes inclusion body formation, improving overall yield.
Researchers have exploited YebF's properties in various expression systems, including *E. coli* and other Gram-negative bacteria, to produce industrially relevant enzymes, therapeutic proteins, and antigens. Its small size (12 kDa) and lack of post-translational modifications further streamline its application. Recent studies also explore engineered YebF variants with optimized secretion efficiency or tailored cleavage sites for precise tag removal. Beyond bioproduction, YebF secretion mechanisms continue to inform fundamental research on bacterial protein transport pathways, offering insights into unconventional secretion strategies in prokaryotes.
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