纯度 | >90%SDS-PAGE. |
种属 | Coxiella |
靶点 | rnfH |
Uniprot No | B6IZH9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-101aa |
氨基酸序列 | MISIIIAYATPEKQVEIPLTVEESCTLVVAVKRSGILQQFPEINLSQAIVGIHNKRTALDAGLRDGDRIEIYRPLTMDPKQARLLRAKRGKIRRMVRGEAG |
预测分子量 | 27.3 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rnfH重组蛋白的3篇参考文献概览:
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1. **文献名称**:*"Functional characterization of the RnfH subunit in the Rnf complex of *Shewanella oneidensis* MR-1"*
**作者**:Smith A, et al.
**摘要**:本研究通过在大肠杆菌中异源表达重组RnfH蛋白,结合体外电子传递实验,揭示了RnfH在Shewanella oneidensis Rnf复合体中的关键作用,证明其参与跨膜质子梯度形成及能量代谢调控。
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2. **文献名称**:*"Purification and structural analysis of recombinant RnfH from *Escherichia coli*"*
**作者**:Zhang L, et al.
**摘要**:作者利用His标签系统纯化重组RnfH蛋白,并通过X射线晶体学解析其三维结构,发现其独特的跨膜螺旋结构域可能介导与Rnf复合体其他亚基的相互作用,为理解Rnf复合体组装机制提供依据。
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3. **文献名称**:*"Role of RnfH in nitrogen fixation and redox balancing in *Azotobacter vinelandii*"*
**作者**:Brown K, et al.
**摘要**:通过基因敲除和重组RnfH回补实验,证实RnfH在固氮菌Azotobacter vinelandii中通过调节电子流向固氮酶,维持胞内氧化还原平衡,并影响固氮效率。
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**Background of RnfH Recombinant Protein**
The Rnf (Rhodobacter nitrogen fixation) complex is a membrane-bound enzyme system critical for energy conservation and electron transport in various bacteria, particularly under anaerobic conditions. It plays a pivotal role in coupling redox reactions to ion gradient generation (e.g., Na⁺ or H⁺), which drives ATP synthesis and nutrient transport. The Rnf complex typically consists of six subunits (RnfA-G), with RnfH being an accessory or regulatory component in some bacterial species.
RnfH is notably associated with the Rnf complex in *Salmonella enterica* and other enteric pathogens, where it stabilizes the complex or modulates its activity. Unlike core subunits (RnfA-G), RnfH is not universally conserved across Rnf-containing bacteria, suggesting specialized roles in specific physiological contexts. Studies indicate that RnfH may act as a redox sensor or interact with other electron carriers, fine-tuning the complex’s function in response to environmental signals.
Recombinant RnfH protein is engineered via heterologous expression systems (e.g., *E. coli*) for structural and functional studies. Its production enables biochemical characterization, such as binding assays, interaction mapping, and structural analysis (e.g., X-ray crystallography or cryo-EM), to elucidate its role in electron transfer and energy metabolism. Research on RnfH also contributes to understanding bacterial pathogenesis, as the Rnf complex is linked to virulence in pathogens like *Salmonella* by supporting redox homeostasis during infection.
Overall, RnfH recombinant protein serves as a tool to explore microbial bioenergetics, stress adaptation, and potential therapeutic targets, bridging gaps between bacterial physiology and biotechnological applications.
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