| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ARO |
| Uniprot No | P11511 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGP GYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKS SSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMK ALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSN TLFLRIPLDGTEIFTLTS |
| 预测分子量 | 50 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ARO重组蛋白的3篇示例参考文献(内容为虚构概括，仅供参考)：
1. **文献名称**：*"Cloning and Expression of ARO Recombinant Protein in E. coli for Antibiotic Resistance Studies"*
**作者**：Smith J, Lee R.
**摘要**：本研究成功克隆并表达了来自革兰氏阴性菌的ARO基因，通过大肠杆菌表达系统获得高纯度重组蛋白，验证其与β-内酰胺类抗生素水解活性的关联，为耐药机制研究提供工具。
2. **文献名称**：*"Structural Insights into ARO Protein Function via X-ray Crystallography"*
**作者**：Zhang H, et al.
**摘要**：通过X射线晶体学解析ARO重组蛋白的三维结构，揭示其活性位点关键氨基酸残基，结合分子动力学模拟阐明底物结合机制，为设计新型抑制剂奠定基础。
3. **文献名称**：*"ARO Recombinant Protein as a Therapeutic Target in Multidrug-Resistant Pathogens"*
**作者**：Garcia M, Patel S.
**摘要**：评估ARO重组蛋白在多重耐药菌中的表达水平，筛选小分子化合物库发现其抑制剂，体外实验证实可恢复传统抗生素疗效，提出靶向ARO的联合治疗策略。
(注：若需真实文献，建议通过PubMed或SciHub检索关键词“ARO recombinant protein”或结合具体研究背景细化查询。)
**Background of ARO Recombinant Proteins**
ARO (Antibiotic Resistance Ontology) recombinant proteins are engineered biomolecules designed to study or combat antibiotic resistance, a critical global health challenge. These proteins are typically derived from genes associated with antimicrobial resistance (AMR) mechanisms, such as β-lactamases, efflux pumps, or modifying enzymes, which pathogens use to evade antibiotics. Recombinant technology enables the production of purified ARO proteins by cloning target genes into expression systems (e.g., *E. coli*, yeast, or mammalian cells), followed by fermentation and purification. This approach allows researchers to analyze the structure, function, and interaction of resistance-related proteins at a molecular level.
The development of ARO recombinant proteins supports multiple applications. In drug discovery, they serve as targets for high-throughput screening of inhibitors or novel antibiotics. In diagnostics, they aid in detecting resistance markers in clinical samples. Additionally, these proteins are vital for understanding evolutionary trends in AMR and developing vaccines or antibody-based therapies.
Recent advances in synthetic biology, CRISPR-based editing, and bioinformatics have accelerated the design of ARO proteins with enhanced stability or modified activity, enabling tailored studies. However, challenges remain, including optimizing expression yields, minimizing misfolding in heterologous systems, and ensuring functional relevance to native pathogens.
Overall, ARO recombinant proteins represent a bridge between basic research and translational solutions, offering tools to decode resistance mechanisms and innovate therapies. Their continued development is essential to address the escalating threat of untreatable infections.
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