| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ampC |
| Uniprot No | P24735 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-397aa |
| 氨基酸序列 | GEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR |
| 预测分子量 | 56.7kDa |
| 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AmpC重组蛋白的3篇代表性文献摘要示例(注：文献为虚构示例，实际引用需查询真实数据库)：
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1. **文献名称**: *"Heterologous Expression and Characterization of AmpC Beta-Lactamase from Pseudomonas aeruginosa"*
**作者**: Martinez, J. et al.
**摘要**: 本研究在大肠杆菌中成功克隆并表达了铜绿假单胞菌来源的AmpC β-内酰胺酶重组蛋白。通过亲和层析纯化获得高纯度酶，并测定其对三代头孢菌素的水解活性，证实其广谱耐药性机制。
2. **文献名称**: *"Structural Insights into AmpC-Mediated Antibiotic Resistance via X-ray Crystallography"*
**作者**: Thompson, R. & Lee, S.
**摘要**: 利用X射线晶体学解析了重组AmpC蛋白的三维结构，揭示了其活性位点与β-内酰胺类抗生素结合的分子细节，为设计新型酶抑制剂提供了结构基础。
3. **文献名称**: *"Development of a Recombinant AmpC-Based Biosensor for Rapid Detection of Cephalosporin Resistance"*
**作者**: Gupta, A. et al.
**摘要**: 将重组AmpC蛋白固定于纳米电极表面，构建了一种新型电化学生物传感器，可快速检测临床菌株对头孢菌素的耐药性，灵敏度达90%以上。
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如需真实文献，建议检索PubMed或Web of Science，关键词：**"recombinant AmpC beta-lactamase"**，并筛选近年研究。
AmpC β-lactamases are a class of enzymatically active bacterial proteins that confer resistance to β-lactam antibiotics, including cephalosporins and cephamycins. These enzymes hydrolyze the β-lactam ring, a critical structural component of these antibiotics, rendering them ineffective. AmpC is naturally encoded by chromosomal genes in many Gram-negative bacteria, such as *Enterobacteriaceae* and *Pseudomonas aeruginosa*, but can also be plasmid-mediated, facilitating horizontal gene transfer and spread of antibiotic resistance. Overexpression of AmpC, often induced by β-lactam exposure, is a major mechanism of multidrug resistance in clinical settings.
Recombinant AmpC proteins are engineered versions produced via molecular cloning and heterologous expression systems, typically in *E. coli*. These proteins are generated to study the enzyme’s structure, substrate specificity, and catalytic mechanisms, as well as to screen potential inhibitors. The recombinant expression allows for high-yield production, purification (e.g., via affinity tags), and functional characterization without interference from native bacterial components. Researchers utilize techniques like X-ray crystallography and kinetic assays to analyze mutant variants or inhibitor interactions, aiding in the development of novel antibiotics or β-lactamase inhibitors (e.g., avibactam).
AmpC’s clinical relevance drives demand for recombinant forms in diagnostic tools, such as rapid resistance detection assays, and in drug discovery pipelines. Studies on recombinant AmpC also explore evolutionary adaptations, including extended-spectrum mutations that broaden substrate profiles. However, variability in AmpC activity across bacterial species and regulatory mechanisms (e.g., ampR-ampC systems) complicates standardization, necessitating tailored approaches in recombinant protein design. Overall, recombinant AmpC serves as a critical tool in combating antimicrobial resistance by elucidating resistance mechanisms and guiding therapeutic innovations.
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