| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | BPHL |
| Uniprot No | Q86WA6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 38-291aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSVTSAKVAVNGVQLHYQQTGEGDHAVLLL PGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFER DAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANA YVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQF KHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHL MPEGKHNLHLRFADEFNKLAEDFLQ |
| 预测分子量 | 31 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BPHL重组蛋白的3篇示例参考文献(注：以下文献为虚构示例，用于演示格式，实际文献需通过学术数据库查询)：
---
1. **文献名称**: *Expression and Characterization of Recombinant BPHL Enzyme in E. coli*
**作者**: Zhang L, et al.
**摘要**: 本研究报道了在大肠杆菌中高效表达BPHL重组蛋白的优化方法，通过亲和层析纯化获得高活性酶，并验证其水解特定酯类底物的功能，为工业化应用提供基础。
2. **文献名称**: *Structural Insights into BPHL: A Crystallographic Study*
**作者**: Patel R, et al.
**摘要**: 通过X射线晶体学解析了BPHL重组蛋白的三维结构，揭示了其催化活性中心的关键氨基酸残基，为设计靶向抑制剂提供了结构生物学依据。
3. **文献名称**: *BPHL Recombinant Protein in Drug Metabolism: In Vitro Analysis*
**作者**: Kim S, et al.
**摘要**: 利用体外肝细胞模型证明BPHL重组蛋白可显著代谢某类前体药物，提示其在药物激活中的潜在作用，为药代动力学研究提供了新方向。
---
如需真实文献，建议在PubMed或Web of Science搜索关键词“BPHL recombinant protein”或结合具体研究领域筛选。
**Background of BPHL Recombinant Protein**
BPHL (bifunctional phosphoesterase/hydrolase) is a bacterial enzyme that has garnered attention for its role in antibiotic resistance and metabolism. Initially identified in *Burkholderia pseudomallei*, the causative agent of melioidosis, BPHL exhibits dual enzymatic activity: it functions as a phosphoesterase, hydrolyzing organophosphate compounds, and as a β-lactamase, contributing to resistance against β-lactam antibiotics like penicillins and cephalosporins. This versatility positions BPHL as a critical survival factor for pathogens in hostile environments, including those with antibiotic or chemical stressors.
The recombinant form of BPHL is produced via heterologous expression systems, such as *E. coli*, enabling scalable purification for structural and functional studies. Crystallographic analyses reveal a distinctive α/β-hydrolase fold, with a catalytic triad (Ser-His-Asp) common to many hydrolases. Its β-lactamase activity, however, is atypical, showing limited hydrolysis efficiency compared to classical β-lactamases, suggesting a specialized ecological or metabolic role.
Research on recombinant BPHL focuses on understanding its mechanism in antibiotic resistance and detoxification, which could inform strategies to counteract multidrug-resistant infections. Additionally, its phosphoesterase activity has potential biotechnological applications, including bioremediation of organophosphate pollutants. Efforts to design inhibitors targeting BPHL’s active site are ongoing, aiming to restore the efficacy of β-lactams against resistant pathogens.
Overall, BPHL exemplifies the adaptive complexity of bacterial enzymes, bridging clinical challenges in infectious diseases and opportunities for biotechnological innovation. Its study underscores the interplay between microbial evolution and therapeutic development.
×
