| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mrcB |
| Uniprot No | P02919 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 444-736aa |
| 氨基酸序列 | SVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGA |
| 预测分子量 | 38.6 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 **mrcB重组蛋白** 的3篇参考文献示例(内容为模拟生成，供参考)：
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1. **文献名称**：*Expression and purification of recombinant mrcB protein in Escherichia coli*
**作者**：Smith, J. et al.
**摘要**：本研究报道了通过构建pET载体在大肠杆菌中高效表达mrcB重组蛋白，并利用亲和层析技术纯化获得高纯度蛋白。通过SDS-PAGE和Western blot验证了蛋白表达，为后续酶活性和结构研究奠定基础。
2. **文献名称**：*Structural analysis of mrcB-encoded penicillin-binding protein in bacterial cell wall synthesis*
**作者**：Lee, H. & García-Lara, J.
**摘要**：利用X射线晶体学解析了mrcB编码的青霉素结合蛋白(PBP)的三维结构，揭示了其与β-内酰胺类抗生素相互作用的活性位点，为新型抗菌药物设计提供了结构依据。
3. **文献名称**：*Functional characterization of mrcB deletion mutants in Bacillus subtilis*
**作者**：Wang, Y. et al.
**摘要**：通过基因敲除实验证明，mrcB缺失导致细菌细胞壁合成缺陷和形态异常。重组mrcB蛋白的体外回补实验恢复了肽聚糖交联酶活性，证实其在细胞分裂中的关键作用。
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如需真实文献，建议在 **PubMed** 或 **Google Scholar** 中检索关键词：`"mrcB recombinant protein"`、`"penicillin-binding protein expression"` 或 `"bacterial cell wall synthesis"`。
**Background of mrcB Recombinant Protein**
The *mrcB* gene encodes a penicillin-binding protein (PBP), specifically PBP2. which plays a critical role in bacterial cell wall biosynthesis. PBPs are essential for peptidoglycan synthesis, a key structural component of bacterial cell walls. In *Escherichia coli*, PBP2 (encoded by *mrcB*) works cooperatively with PBP1A (encoded by *mrcA*) to mediate cell elongation and maintain cell shape by crosslinking glycan strands during peptidoglycan assembly. Its activity is targeted by β-lactam antibiotics, such as penicillin, which inhibit transpeptidase function, leading to cell wall defects and bacterial death.
Recombinant mrcB protein is produced through genetic engineering, typically by cloning the *mrcB* gene into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. This allows researchers to study its structure, enzymatic activity, and interactions with antibiotics or inhibitors. The protein’s recombinant form is often purified using affinity tags (e.g., His-tag) for functional assays, crystallography, or drug discovery studies.
Interest in mrcB stems from its role in antibiotic resistance. Mutations in *mrcB* can alter PBP2’s affinity for β-lactams, contributing to resistance in pathogens like *Neisseria gonorrhoeae* and *Staphylococcus aureus*. Understanding its molecular mechanisms aids in developing novel antibiotics or potentiators to counteract resistance. Additionally, structural studies of recombinant mrcB have provided insights into substrate binding and catalytic sites, guiding rational drug design.
Beyond antimicrobial research, mrcB recombinant protein is used to explore bacterial physiology, including cell division and stress responses. Its study also extends to biotechnology applications, such as engineering cell wall synthesis pathways in industrial microbes. Overall, mrcB recombinant protein serves as a vital tool for addressing global health challenges posed by antibiotic-resistant bacteria.
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