| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pbpD |
| Uniprot No | P40750 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 213-450aa |
| 氨基酸序列 | PNNPTLYDPLKHFDYTKSRQERLLKGLKDAGVITDKELKKAVKQKIKLDVEKREDKYPDYVSYVNDEFTQLVSESEGFDKRLQKASGKQKEKIENELSARVSTLMKDGVKIYTALDPYMQNQVVAQMNSKLPYADVQGGAAVINHQTHQIIALSGGKNYQKYDFNRAYQAYRQPGSSIKPLLDYGPYIEQTGATTSSTIDASKFCSKDYCPQNYNNRTYGTVTLDTAFKNSYNTPAIR |
| 预测分子量 | 43.0 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pbpD重组蛋白的3篇参考文献的示例(注：文献信息为假设性描述，实际文献请通过学术数据库验证)：
---
1. **文献名称**: "Overexpression of PBP4 impairs β-lactam resistance in *Pseudomonas aeruginosa*"
**作者**: Moya, B. et al.
**摘要**: 本研究在大肠杆菌中重组表达了铜绿假单胞菌的PBP4(pbpD)，发现其过表达导致对β-内酰胺类抗生素敏感性增加，揭示了pbpD通过水解抗生素或竞争性结合影响耐药性的机制。
2. **文献名称**: "Cloning and enzymatic characterization of Pseudomonas aeruginosa penicillin-binding protein D"
**作者**: Juan, C. et al.
**摘要**: 报道了pbpD基因的克隆、重组蛋白表达及纯化过程，证实其具有羧肽酶和转肽酶活性，并证明其活性受金属离子调控，为研究细胞壁合成提供了基础。
3. **文献名称**: "Structural insights into the function of PBP4 in *Pseudomonas aeruginosa* biofilm resistance"
**作者**: Higgins, P.G. et al.
**摘要**: 通过X射线晶体学解析了pbpD重组蛋白的三维结构，发现其活性位点突变与生物膜内细菌对美罗培南的耐药性相关，为靶向药物设计提供了依据。
---
建议通过 **PubMed/Google Scholar** 搜索关键词 "pbpD recombinant protein" 或 "Pseudomonas aeruginosa PBP4" 获取真实文献。
**Background of pbpD Recombinant Protein**
The *pbpD* gene encodes a penicillin-binding protein (PBP), a class of enzymes critical for bacterial cell wall synthesis. PBPs facilitate peptidoglycan cross-linking, a process targeted by β-lactam antibiotics (e.g., penicillins). In many pathogenic bacteria, PBPs are linked to β-lactam resistance, either through mutations that reduce antibiotic binding or via overexpression. *pbpD* homologs are found in various species, including *Pseudomonas aeruginosa* and *Acinetobacter baumannii*, where they contribute to intrinsic resistance or adaptive responses under antibiotic stress.
Recombinant pbpD protein is produced via heterologous __expression (e.g., in *E. coli*) for functional and structural studies. Its production often involves cloning the *pbpD* sequence into expression vectors, followed by purification using affinity tags (e.g., His-tag). Researchers use the recombinant protein to investigate its enzymatic activity, interaction with β-lactams, and role in resistance mechanisms. Structural analyses (e.g., X-ray crystallography) reveal binding sites and conformational changes during antibiotic interaction.
Studies on pbpD are vital for understanding bacterial resistance evolution and guiding drug design. For instance, in *P. aeruginosa*, pbpD overexpression correlates with carbapenem resistance, highlighting its clinical relevance. Additionally, pbpD serves as a potential target for novel inhibitors or diagnostic markers. By characterizing its biochemical properties, researchers aim to develop strategies to counteract resistance, such as designing β-lactamase-resistant antibiotics or adjuvant therapies.
Overall, pbpD recombinant protein is a key tool in antimicrobial research, bridging molecular insights into cell wall biology with translational applications against multidrug-resistant pathogens.
×
