| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nifH |
| Uniprot No | P20623 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-47aa |
| 氨基酸序列 | MAALRQIAFYGKGGIGKSTTSQNTLAALVDHHVPRIPMIIRIGGYAQ |
| 预测分子量 | 35.0 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nifH重组蛋白的参考文献示例(注：以下内容为模拟示例，非真实文献，仅作参考格式示范)：
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1. **标题**: "Heterologous Expression and Functional Characterization of Recombinant NifH from *Azotobacter vinelandii*"
**作者**: Smith, J., Brown, K., & Wilson, T.
**摘要**: 本研究报道了在*E. coli*系统中高效表达并纯化来自固氮菌*A. vinelandii*的NifH蛋白。通过体外酶活实验证实重组蛋白能够与NifDK复合体结合，恢复固氮活性，为研究固氮酶复合体的组装机制提供了工具。
2. **标题**: "Structural Insights into Recombinant NifH: Role of Iron-Sulfur Clusters in Nitrogenase Activity"
**作者**: Kim, S., Lee, M., & Park, H.
**摘要**: 通过X射线晶体学解析了重组NifH蛋白的三维结构，揭示了其铁硫簇结合位点的关键氨基酸残基，并证明该位点的突变会显著降低固氮酶活性，阐明了NifH在电子传递中的分子机制。
3. **标题**: "Development of an ELISA-Based Diagnostic Assay Using Recombinant NifH for Detecting Symbiotic Nitrogen-Fixing Bacteria"
**作者**: Zhang, Y., Chen, L., & Wang, Q.
**摘要**: 研究利用重组NifH蛋白作为抗原，开发了一种高特异性的ELISA检测方法，成功用于土壤和植物根瘤样品中固氮菌的快速鉴定，灵敏度显著高于传统PCR方法。
4. **标题**: "Optimization of Soluble NifH Expression in *E. coli* Using a Tag-Free Purification Strategy"
**作者**: Gupta, R., & Rodríguez, J.
**摘要**: 通过密码子优化和低温诱导策略，显著提高了NifH蛋白在*E. coli*中的可溶性表达，建立了一种无标签纯化流程，为大规模制备功能性NifH提供了高效方案。
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这些示例涵盖了重组nifH蛋白的表达优化、结构功能研究、应用开发等方向，符合学术文献的典型结构。如需真实文献，建议通过PubMed或Google Scholar以“nifH recombinant protein expression/application”为关键词检索。
The nifH gene encodes the iron protein component (dinitrogenase reductase) of nitrogenase, a critical enzyme complex responsible for biological nitrogen fixation (BNF) in diazotrophic microorganisms. Nitrogenase catalyzes the ATP-dependent reduction of atmospheric nitrogen (N₂) to ammonia (NH₃), a process vital for sustaining global nitrogen cycles and soil fertility. The nifH protein forms a homodimer that binds MgATP and facilitates electron transfer to the catalytic MoFe protein (encoded by nifD and nifK), enabling the reduction of N₂. Due to its essential role in BNF, nifH has been extensively studied to understand the structure, mechanism, and regulation of nitrogenase activity.
Recombinant nifH protein is produced by cloning the nifH gene into expression vectors (e.g., E. coli) for overexpression and purification. This approach enables large-scale production of functional nifH, circumventing challenges in isolating the protein from native organisms, which often exhibit oxygen sensitivity or low expression levels. Recombinant nifH retains the ability to hydrolyze ATP and interact with the MoFe protein, making it indispensable for in vitro studies of nitrogenase kinetics, metal cofactor assembly, and electron transport mechanisms.
Research on recombinant nifH has advanced synthetic biology efforts to engineer nitrogen-fixing capabilities in non-diazotrophic crops, aiming to reduce reliance on synthetic fertilizers. Additionally, nifH serves as a molecular marker for detecting nitrogen-fixing microbial communities in environmental samples. Despite progress, challenges persist, such as maintaining protein stability and reconstituting fully active nitrogenase in heterologous systems. Ongoing studies focus on optimizing expression conditions, elucidating post-translational modifications, and engineering nifH variants with enhanced activity or oxygen tolerance. These efforts underscore nifH's central role in both fundamental biochemistry and sustainable agricultural innovation.
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