| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pepP |
| Uniprot No | P15034 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-441aa |
| 氨基酸序列 | SEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL TASVVKKPEE IEALMVAARK Q |
| 预测分子量 | 49,8 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pepP重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Cloning, expression, and enzymatic characterization of recombinant pepP from Lactobacillus helveticus"*
**作者**：Zhang Y. et al.
**摘要**：研究报道了通过在大肠杆菌中克隆并表达来自嗜酸乳杆菌的pepP基因，重组蛋白经纯化后表现出脯氨酸氨基肽酶活性，其最适pH为6.5.且在食品工业中具有潜在应用价值。
2. **文献名称**：*"Structural insights into the substrate specificity of pepP: X-ray crystallography of a recombinant enzyme from Streptococcus pneumoniae"*
**作者**：Lee S. et al.
**摘要**：通过解析肺炎链球菌pepP重组蛋白的晶体结构，揭示了其底物结合口袋的关键氨基酸残基，阐明了其对含脯氨酸肽链的特异性切割机制。
3. **文献名称**：*"Functional characterization of recombinant pepP in bacterial pathogenesis: A virulence factor analysis"*
**作者**：Wang H. et al.
**摘要**：研究发现，重组表达的pepP在病原菌李斯特菌中通过降解宿主细胞内的免疫调节肽，增强细菌存活能力，提示其可能作为新型抗菌治疗的靶点。
注：以上文献信息为模拟示例，实际引用需根据具体论文核实。
**Background of pepP Recombinant Protein**
The pepP gene encodes a proline-specific aminopeptidase, a metalloprotease belonging to the M24 family, which is widely conserved across bacteria and eukaryotes. This enzyme catalyzes the removal of N-terminal proline residues from peptides and proteins, playing a critical role in protein maturation, nitrogen metabolism, and cell wall biosynthesis. In pathogenic bacteria, pepP is often linked to virulence, as proline-rich motifs in host proteins are common targets for bacterial proteases during infection. For instance, in *Streptococcus* and *Staphylococcus* species, pepP contributes to pathogenicity by modulating host-pathogen interactions and evading immune responses.
Structurally, pepP contains a conserved catalytic domain with a binuclear metal center (typically zinc ions) essential for its enzymatic activity. Its α/β-hydrolase fold facilitates substrate binding and specificity for proline. Recombinant pepP proteins are engineered via heterologous expression systems (e.g., *E. coli*) for functional studies. These proteins are purified using affinity chromatography, enabling biochemical characterization, structural analysis, and inhibitor screening.
Research on pepP recombinant proteins has applications in antimicrobial drug development, as inhibiting pepP could disrupt bacterial survival or virulence. Additionally, it serves as a tool in biotechnology for peptide processing and protein engineering. Studies also explore its role in microbial stress adaptation, such as oxidative or osmotic stress, highlighting its broader physiological significance. Overall, pepP represents a promising target for therapeutic intervention and a model for understanding metalloprotease mechanisms.
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