| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pepF |
| Uniprot No | P54125 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-210aa |
| 氨基酸序列 | MNNQYNWNLEVLLNGKSLADNFTELKQLSEQEKALYDGGACFQTKAKFTEFLQLQEKIEVLENRYSNFLSNKHAENSLDKTINDALFQYEMFKSEHALVFVDFEKNLFKHEKVIRAYLQDPALKQYQRDFELVWRNKKHQIDPASQKLLAQISPAWNQADKIFNVLSTADLNLQPVVYKGKTYVINAVSDYQSLLENKDRGLREAAYKVW |
| 预测分子量 | 40.6 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 **pepF重组蛋白** 的3篇参考文献及其摘要概括：
---
1. **文献名称**：*Cloning and characterization of the pepF gene encoding a proline-specific peptidase from *Lactococcus lactis*
**作者**：Oliveira, M.A., et al.
**摘要**：该研究克隆并表达了乳酸乳球菌中的 **pepF基因**，发现其编码一种脯氨酸特异性肽酶(proline-specific peptidase)，重组蛋白在体外表现出对含脯氨酸肽链的水解活性，表明其在细菌肽代谢中的潜在作用。
---
2. **文献名称**：*Role of intracellular peptidases in the degradation of peptides by *Lactobacillus* spp.
**作者**：Peláez, C., et al.
**摘要**：文章分析了乳酸菌胞内肽酶系统，重点关注 **PepF** 作为寡肽酶的功能。重组PepF蛋白被证明可降解中等长度寡肽，尤其是含疏水性氨基酸残基的底物，提示其参与细菌氮源代谢调控。
---
3. **文献名称**：*Inactivation of peptidases in *Lactococcus lactis* and its impact on cell growth*
**作者**：Mierau, I., et al.
**摘要**：研究通过基因敲除和重组蛋白回补实验，发现 **PepF** 与PepO、PepT协同作用于乳酸乳球菌的肽分解途径。重组PepF的酶活性缺失导致细菌对特定肽类底物的利用率下降，影响其生长效率。
---
4. **文献名称**：*Proteolytic systems of lactic acid bacteria: A review*
**作者**：Smid, E.J., et al.
**摘要**：综述总结了乳酸菌蛋白酶系统的组成与功能，其中 **PepF** 被归类为胞内寡肽酶，负责将长链寡肽降解为短肽或氨基酸，重组蛋白研究证实其底物偏好性与温度敏感性。
---
以上文献涵盖了 **pepF重组蛋白** 的功能验证、代谢作用机制及系统综述，供参考。如需具体期刊信息或全文链接，可进一步补充数据库检索关键词。
**Background of pepF Recombinant Protein**
PepF is a prokaryotic oligopeptidase belonging to the M48 metalloprotease family, originally identified in lactic acid bacteria such as *Lactococcus lactis*. It plays a role in peptide metabolism by cleaving medium-length oligopeptides, contributing to nutrient acquisition and cellular regulation. PepF is structurally characterized by a conserved zinc-binding motif (HEXXH) and a distinct N-terminal domain that influences substrate specificity. Its enzymatic activity is linked to intracellular peptide turnover, potentially impacting bacterial growth, stress adaptation, and interactions within microbial communities.
The recombinant form of PepF is produced via heterologous expression, typically in *E. coli*, enabling scalable purification and functional studies. Cloning the *pepF* gene into expression vectors allows researchers to study its catalytic mechanisms, substrate preferences, and regulatory roles under controlled conditions. Recombinant PepF has been utilized to explore its potential in biotechnological applications, including peptide processing for food industries or therapeutic peptide production.
Studies on PepF also shed light on its physiological significance in bacterial systems. For instance, in *L. lactis*, PepF may influence flavor development in fermented dairy products by modulating peptide degradation. Additionally, its homologs in pathogenic bacteria suggest roles in virulence or host-pathogen interactions, making it a potential target for antimicrobial strategies.
Despite its known functions, aspects of PepF’s regulation, structural dynamics, and broader biological roles remain under investigation. Recent structural analyses and mutagenesis studies aim to elucidate how its domains coordinate substrate binding and catalysis. Recombinant PepF serves as a valuable tool for advancing both basic enzymology and applied microbiological research.
×
