| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | narG |
| Uniprot No | P09152 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-110aa |
| 氨基酸序列 | MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLK |
| 预测分子量 | 20.5 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narG重组蛋白的3篇参考文献示例，包括文献名称、作者及摘要内容概述：
1. **文献名称**: "Heterologous Expression and Characterization of the Nitrate Reductase NarG from *Escherichia coli*"
**作者**: Smith, J.R., et al.
**摘要概述**: 该研究成功在大肠杆菌中异源表达了narG基因，纯化了重组NarG蛋白，并分析了其酶动力学特性。结果显示，重组NarG具有较高的硝酸盐还原活性，为后续研究其催化机制奠定了基础。
2. **文献名称**: "Crystal Structure and Functional Analysis of the Respiratory Nitrate Reductase NarG Subunit from *Pseudomonas stutzeri*"
**作者**: Lee, S.H., & Kim, K.J.
**摘要概述**: 通过X射线晶体学解析了来自*Pseudomonas stutzeri*的NarG亚基的三维结构，揭示了其活性位点的关键氨基酸残基。功能实验表明，这些残基对硝酸盐还原酶的催化效率至关重要。
3. **文献名称**: "Biotechnological Application of Recombinant NarG in Nitrate Detection Biosensors"
**作者**: García, M., et al.
**摘要概述**: 研究利用重组NarG蛋白开发了一种高灵敏度的硝酸盐生物传感器。该传感器在环境水样检测中表现出良好的稳定性和选择性，为环境污染监测提供了新工具。
**备注**：以上文献为示例性质，实际引用时建议通过数据库(如PubMed、Web of Science)以关键词“narG recombinant protein”、“nitrate reductase heterologous expression”等检索最新或高被引研究，以获取真实文献信息。
**Background of NarG Recombinant Protein**
NarG is a key subunit of the membrane-bound nitrate reductase (NarGHI complex), a critical enzyme in microbial anaerobic respiration. It catalyzes the reduction of nitrate (NO₃⁻) to nitrite (NO₂⁻), a pivotal step in the nitrogen cycle, enabling microorganisms to utilize nitrate as a terminal electron acceptor under oxygen-limited conditions. NarG harbors the active site containing a molybdopterin cofactor (Mo-bisPGD) essential for electron transfer during catalysis. The *narG* gene encodes this catalytic subunit, which is highly conserved among nitrate-reducing bacteria and archaea, making it a molecular marker for studying microbial nitrate metabolism in environmental and clinical contexts.
Recombinant NarG protein is produced through heterologous expression systems, typically in *Escherichia coli*, by cloning and expressing the *narG* gene with affinity tags (e.g., His-tag) for purification. This engineered protein retains enzymatic activity when properly folded and cofactor-loaded, allowing researchers to study its structure-function relationships, kinetics, and regulatory mechanisms. Challenges in production include ensuring proper post-translational insertion of the Mo-cofactor and stabilizing the protein’s large, multi-domain architecture.
Applications of recombinant NarG span environmental biotechnology, such as monitoring nitrate pollution in ecosystems, and biomedical research, including understanding pathogen metabolism in low-oxygen niches (e.g., biofilms). It also serves as a tool for engineering microbial consortia for bioremediation or sustainable agriculture. Studies leveraging recombinant NarG contribute to advancing anaerobic bioprocesses and elucidating microbial roles in global nitrogen cycling.
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