| 纯度 | >90%SDS-PAGE. |
| 种属 | Methanobacterium |
| 靶点 | nifH1 |
| Uniprot No | P51602 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-275aa |
| 氨基酸序列 | MVRKIAIYGKGGIGKSTTTQNTASAMAHFHNQRVMIHGCDPKADSTRMILGGKMQTTMMDTLREEGEEACMDLDNVMSTGFKDIKCVESGGPEPGVGCAGRGVITAITIMEHMKVYDDNDFVFFDVLGDVVCGGFAMPIRDGKAEEIYIVASGEMMALYAANNLCKGMVKYAEQSGVRLGGIICNSRNVDGEKELLEEFCKRIGTQMIHFVPRDNIVQKAEFNKRTVVDFDAECSQAHEYSELARKIIENDNFVIPDPMTMDELEEMVVSYGLMD |
| 预测分子量 | 37.4 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. |
以下是模拟的关于nifH1重组蛋白的参考文献示例(注：文献为虚构，仅供参考格式)：
1. **《Heterologous Expression and Functional Characterization of nifH1 in Escherichia coli》**
- 作者：Smith J. et al.
- 摘要：研究通过克隆nifH1基因并在大肠杆菌中成功表达重组蛋白，证实其具有固氮酶活性，并通过光谱分析验证铁硫簇的组装。
2. **《Structural Insights into nifH1 Recombinant Protein Using Cryo-EM》**
- 作者：Johnson R. & Patel S.
- 摘要：利用冷冻电镜解析nifH1重组蛋白的三维结构，揭示了其与ATP结合及电子传递相关的关键氨基酸位点。
3. **《Role of Recombinant nifH1 in Symbiotic Nitrogen Fixation in Rhizobia》**
- 作者：Lee H. et al.
- 摘要：通过基因工程手段回补nifH1缺陷型根瘤菌，证明重组蛋白可恢复宿主植物的结瘤能力及固氮效率。
4. **《Engineering Non-Legume Plants with nifH1 for Enhanced Nitrogen Utilization》**
- 作者：Zhang L. et al.
- 摘要：将重组nifH1导入水稻细胞，发现其与植物内源蛋白互作，显著提高了植株在低氮条件下的生长速率。
**建议**：实际文献需通过PubMed、Google Scholar等平台以关键词“nifH1 recombinant protein”或“nifH1 expression”检索，并筛选涉及基因表达、结构或功能研究的文章。
**Background of nifH1 Recombinant Protein**
The nifH1 gene encodes a critical component of nitrogenase, the enzyme complex responsible for biological nitrogen fixation—a process essential for converting atmospheric nitrogen (N₂) into ammonia (NH₃), a form usable by living organisms. This gene is part of the *nif* (nitrogen fixation) gene cluster, primarily studied in diazotrophic bacteria like *Azotobacter vinelandii* and *Klebsiella pneumoniae*, as well as in some archaea. The nifH1 protein is a homodimeric iron (Fe) protein that functions as the reductase component of nitrogenase, supplying electrons to the catalytic molybdenum-iron (MoFe) protein (encoded by *nifDK*) during the nitrogenase reaction.
Recombinant nifH1 protein is produced through heterologous expression systems, such as *E. coli*, enabling large-scale purification for structural, functional, and biochemical studies. Its recombinant form has been pivotal in elucidating the enzyme’s mechanism, including ATP-dependent electron transfer, interactions with other nitrogenase components, and the role of metal clusters (e.g., the [4Fe-4S] cluster) in catalysis. Research on nifH1 also explores its potential applications in sustainable agriculture, such as engineering crops or microbes to fix nitrogen autonomously, reducing reliance on synthetic fertilizers.
Challenges in working with recombinant nifH1 include maintaining protein stability, avoiding oxygen sensitivity, and ensuring proper post-translational modifications in heterologous hosts. Despite these hurdles, advances in protein engineering and synthetic biology continue to drive its study, offering insights into nitrogen fixation evolution and strategies for improving crop productivity in nitrogen-poor soils. Overall, nifH1 recombinant protein serves as a cornerstone for both basic research and biotechnological innovations aimed at addressing global food security and environmental sustainability.
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