| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pbpA |
| Uniprot No | A5I6G4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 663-830aa |
| 氨基酸序列 | VDRISGKLPTQLSYRDPRGSTVYNEFFINGTIPTEYDDIHVEAQINKLTGKLASKFTPSFLVESRVFLRRDYSPGVELLDQQWLLPYSIDEGGSLPPTEEKNNSNTRDKNKDKNKNKNKDKNPSQDKPNNNNNDNNSNNNNNNNDNNNNTKPPENDSNQNHEDNKNKQ |
| 预测分子量 | 35.2 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pbpA重组蛋白的模拟参考文献示例(仅供参考，建议通过PubMed或Google Scholar验证具体文献)：
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1. **文献名称**: *"Cloning, Expression, and Purification of the Recombinant pbpA Gene from Escherichia coli K-12"*
**作者**: Smith J, et al.
**摘要**: 本研究报道了大肠杆菌K-12中pbpA基因的克隆与重组表达，通过构建表达载体并在大肠杆菌BL21(DE3)中诱导表达，纯化获得可溶性重组蛋白。酶活性分析表明，该蛋白具有羧肽酶活性，且对青霉素类抗生素敏感性降低。
2. **文献名称**: *"Structural Characterization of Recombinant pbpA from Streptococcus pneumoniae and Its Interaction with β-Lactams"*
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了肺炎链球菌重组pbpA蛋白的三维结构，揭示了其与青霉素结合的结构域特征。体外实验表明，pbpA突变可导致β-内酰胺类药物亲和力下降，为耐药机制提供结构依据。
3. **文献名称**: *"Functional Analysis of Recombinant pbpA in Staphylococcus aureus Cell Wall Synthesis"*
**作者**: Zhang R, et al.
**摘要**: 通过重组表达金黄色葡萄球菌pbpA蛋白，研究其在肽聚糖交联中的作用。基因敲除与回补实验证明，pbpA缺失导致细胞壁缺陷，重组蛋白可部分恢复表型，提示其在细胞分裂中的关键功能。
4. **文献名称**: *"Development of a Recombinant pbpA-Based ELISA for Serodiagnosis of Helicobacter pylori Infection"*
**作者**: Tanaka M, et al.
**摘要**: 利用重组表达的幽门螺杆菌pbpA蛋白建立血清学检测方法，验证其在临床样本中的敏感性和特异性，证明其作为诊断标志物的潜力。
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**备注**：以上内容为模拟生成，实际文献需通过学术数据库检索。建议使用关键词“pbpA recombinant protein”或结合特定病原体名称(如Escherichia coli pbpA)进行精确查询。
**Background of pbpA Recombinant Protein**
The penicillin-binding protein A (PbpA) is a bacterial enzyme critical for cell wall synthesis and remodeling, primarily in *Streptococcus pneumoniae* and related species. As a member of the penicillin-binding protein (PBP) family, PbpA exhibits transpeptidase and carboxypeptidase activities, facilitating cross-linking of peptidoglycan strands during cell division. Its role in maintaining cell wall integrity makes it a target for β-lactam antibiotics, which inhibit PbpA by covalently binding to its active site. However, widespread antibiotic resistance has emerged due to mutations in *pbpA* genes, reducing drug affinity and complicating treatment strategies.
Recombinant PbpA protein is produced via genetic engineering, typically by cloning the *pbpA* gene into expression vectors (e.g., *E. coli*), followed by purification. This approach enables large-scale production of the protein for structural, functional, and immunological studies. Researchers utilize recombinant PbpA to investigate mechanisms of antibiotic resistance, particularly how amino acid substitutions alter enzyme structure and β-lactam susceptibility. Structural analyses, such as X-ray crystallography, reveal conformational changes that underpin resistance phenotypes.
Additionally, recombinant PbpA serves as a candidate antigen for vaccine development. Antibodies targeting PbpA may enhance opsonophagocytic clearance of pneumococci, offering protection against infections. Its immunogenicity and conservation across pneumococcal strains make it a promising component for next-generation vaccines. Furthermore, PbpA-based assays are employed in diagnostics to detect resistant bacterial strains or evaluate novel β-lactamase inhibitors.
Overall, recombinant PbpA is a vital tool in understanding bacterial pathogenesis, advancing antimicrobial therapies, and addressing the global challenge of antibiotic resistance. Its study bridges microbiology, structural biology, and translational medicine, highlighting its multifaceted significance in both research and clinical applications.
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