| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | pbp |
| Uniprot No | P07944 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 344-670aa |
| 氨基酸序列 | NDYGSGTAIHPQTGELLALVSTPSYDVYPFMYGMSNEEYNKLTEDKKEPLLNKFQITTSPGSTQKILTAMIGLNNKTLDDKTSYKIDGKGWQKDKSWGGYNVTRYEVVNGNIDLKQAIESSDNIFFARVALELGSKKFEKGMKKLGVGEDIPSDYPFYNAQISNKNLDNEILLADSGYGQGEILINPVQILSIYSALENNGNINAPHLLKDTKNKVWKKNIISKENINLLNDGMQQVVNKTHKEDIYRSYANLIGKSGTAELKMKQGETGRQIGWFISYDKDNPNMMMAINVKDVQDKGMASYNAKISGKVYDELYENGNKKYDIDE |
| 预测分子量 | 44.2 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PBP(青霉素结合蛋白)重组蛋白研究的3篇示例参考文献，格式为文献名称、作者和摘要概括：
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1. **文献名称**: *Expression and purification of recombinant penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus*
**作者**: Lim D, Strynadka NCJ
**摘要**: 该研究描述了一种在大肠杆菌中高效表达和纯化耐甲氧西林金黄色葡萄球菌(MRSA)PBP2a重组蛋白的方法。通过优化表达条件和亲和层析技术获得高纯度蛋白，并验证其与β-内酰胺类抗生素结合的活性降低，为研究耐药机制提供工具。
2. **文献名称**: *Structural analysis of a recombinant penicillin-binding protein 3 (PBP3) from Pseudomonas aeruginosa*
**作者**: Macheboeuf P, Di Guilmi AM, et al.
**摘要**: 通过X射线晶体学解析铜绿假单胞菌重组PBP3的蛋白结构，揭示其转肽酶活性位点的构象特征，并分析其与β-内酰胺类抗生素的相互作用模式，为开发新型抑制剂奠定结构基础。
3. **文献名称**: *Functional characterization of recombinant penicillin-binding protein 5 in Enterococcus faecium*
**作者**: Rice LB, Carias LL, et al.
**摘要**: 研究通过重组表达粪肠球菌PBP5蛋白，证明其低亲和力结合青霉素的特性是导致肠球菌固有耐药的关键因素，并通过定点突变实验验证特定氨基酸残基在耐药性中的作用。
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**备注**：以上文献信息为示例，实际引用时请以真实数据库(如PubMed、Web of Science)检索结果为准，并核对作者、标题及摘要的准确性。
**Background of Recombinant Penicillin-Binding Proteins (PBPs)**
Penicillin-binding proteins (PBPs) are essential bacterial enzymes involved in cell wall biosynthesis, particularly in the synthesis and remodeling of peptidoglycan, a critical component of bacterial cell walls. They catalyze transpeptidation and carboxypeptidation reactions, which are vital for cross-linking peptidoglycan strands to maintain structural integrity. PBPs are the primary targets of β-lactam antibiotics (e.g., penicillin, cephalosporins), which inhibit their enzymatic activity, leading to cell wall defects and bacterial death.
The emergence of antibiotic resistance, notably through mutations or acquisition of low-affinity PBPs (e.g., PBP2a in methicillin-resistant *Staphylococcus aureus*), has driven research into understanding PBP structure-function relationships. Recombinant DNA technology enables the production of purified PBPs by expressing their genes in heterologous systems (e.g., *E. coli*), allowing detailed biochemical and structural studies. These recombinant PBPs retain functional properties, facilitating assays to study antibiotic interactions, resistance mechanisms, and enzyme kinetics.
Structural analyses using X-ray crystallography and cryo-electron microscopy have revealed mechanisms of antibiotic resistance, such as altered active sites or allosteric regulation, guiding the design of novel β-lactamase inhibitors or β-lactam analogs. Recombinant PBPs also serve as tools for high-throughput drug screening and diagnostics, aiding in the detection of resistant bacterial strains.
Beyond therapeutics, recombinant PBPs contribute to vaccine development by exploring surface-exposed epitopes or immunogenic domains. Their study remains pivotal in addressing the global challenge of antimicrobial resistance and advancing targeted antibacterial strategies.
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