| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pbpE |
| Uniprot No | P32959 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-451aa |
| 氨基酸序列 | MKQNKRKHLQTLFETLGEKHQFNGTVLAAEGGDILYHHSFGYAEMTEKRPLKTNSLFELASLSKPFTALGIILLEEKGILGYEDKVDRWLPGFPYQGVTIRHLLNHTSGLPDYMGWFFANWDSHKIAVNQDIVDMLMNEGLSGYFEPNEGWMYSNTGYVLLAVIIEKASGMSYADFIKTSIFLPAGMNETRVYNRRLSPERIDHYAYGYVYDVHSETYVLPDELEETNYVVYLDGIQGDGTVNSVTSDLFRFDQALYQDDFISKASKESAFSPVRLNNGETIDYGFGWVLQNSPEKGRIVSHSGGWPGYSTMMIRYIDHRKTLIYLSNKEEDTEYEQAILKAAEHILFGQPYDVPERPADKKKKAIDTAIYSRYVGSYLLQDGTAAQVTTENERLYLEIAGQLRLELFPSSETRFFLRALSVEVEFTLGEDAAKSFILYEDGSEEEAVRTK |
| 预测分子量 | 67.4 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pbpE重组蛋白的3篇参考文献示例，内容基于典型研究方向概括：
1. **文献名称**: "Cloning and expression of the pbpE gene encoding a penicillin-binding protein in Escherichia coli"
**作者**: Smith J, et al.
**摘要**: 本研究成功克隆并表达了来自大肠杆菌的pbpE基因，重组蛋白在大肠杆菌系统中高效表达。通过SDS-PAGE和Western blot验证蛋白纯度与抗原性，为后续研究其与β-内酰胺类抗生素相互作用提供基础。
2. **文献名称**: "Structural analysis of recombinant PBP5 (pbpE) from Enterococcus faecalis and its role in β-lactam resistance"
**作者**: Lee H, et al.
**摘要**: 作者解析了粪肠球菌PBP5(由pbpE编码)的重组蛋白晶体结构，揭示其与青霉素结合的结构域特征。功能实验表明该蛋白低亲和力结合青霉素可能是肠球菌耐药性的关键机制之一。
3. **文献名称**: "Recombinant PbpE as a potential vaccine candidate against Staphylococcus aureus infections"
**作者**: Zhang Y, et al.
**摘要**: 研究评估了金黄色葡萄球菌重组PbpE蛋白的免疫原性，动物实验显示其可诱导高水平抗体并增强小鼠对致死剂量细菌攻击的存活率，提示其作为疫苗靶标的潜力。
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**注意**：以上文献为示例性概括，实际研究中可能需根据具体菌种或pbpE功能调整关键词检索(如结合耐药性、结构或疫苗开发方向)。若需真实文献，建议在PubMed/Google Scholar中检索：
**关键词**：
- "pbpE recombinant protein expression"
- "penicillin-binding protein E structure"
- "pbpE gene cloning antibiotic resistance"
**Background of pbpE Recombinant Protein**
The *pbpE* gene encodes penicillin-binding protein E (PbpE), a member of the penicillin-binding protein (PBP) family critical for bacterial cell wall biosynthesis. PBPs are enzymes involved in peptidoglycan assembly, a key structural component of bacterial cell walls. They catalyze transpeptidation and glycosyltransferase reactions, facilitating cross-linking of peptidoglycan strands. PbpE, specifically, is classified as a class B PBP, characterized by a non-penicillin-binding transpeptidase domain and a regulatory role in cell wall remodeling.
In pathogenic bacteria, such as *Streptococcus pneumoniae* or *Staphylococcus aureus*, PBPs are primary targets for β-lactam antibiotics (e.g., penicillin). However, mutations or horizontal gene transfer of altered *pbp* genes, including *pbpE*, can confer resistance by reducing antibiotic binding affinity. This mechanism underscores the clinical relevance of studying PbpE in antibiotic resistance.
Recombinant PbpE protein is produced via genetic engineering, typically by cloning the *pbpE* gene into expression vectors (e.g., *E. coli*), followed by purification. Its recombinant form enables structural and functional studies, such as crystallography to resolve antibiotic-PBP interactions or enzymatic assays to probe peptidoglycan synthesis mechanisms. Additionally, it serves as a tool for screening novel β-lactam analogs or inhibitors to combat resistant strains.
Research on PbpE also contributes to understanding bacterial physiology, including cell division and stress response pathways. Its role in virulence and survival mechanisms highlights potential applications in vaccine development or antimicrobial strategies. Overall, recombinant PbpE is a vital resource for addressing the global challenge of antimicrobial resistance and advancing bacterial pathogenesis research.
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