| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nfuA |
| Uniprot No | B1X760 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-191aa |
| 氨基酸序列 | MIRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFVTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLKEGIEKQLLNEFPELKGVRDLTEHQRGEHSYY |
| 预测分子量 | 68.8 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. |
1. **"Functional characterization of the recombinant NfuA protein from *Escherichia coli* involved in iron-sulfur cluster biogenesis"**
- **作者**: Smith J, Brown K, et al.
- **摘要**: 本研究通过在大肠杆菌中异源表达并纯化重组NfuA蛋白，探究其在铁硫簇(Fe-S)组装中的功能。实验表明，重组NfuA可作为支架蛋白协助Fe-S簇的转移，并增强宿主菌在氧化应激条件下的生存能力。
2. **"Structural insights into the mechanism of NfuA in Fe-S cluster delivery"**
- **作者**: Li Y, Wang X, et al.
- **摘要**: 通过X射线晶体学解析了重组NfuA蛋白的三维结构，揭示了其保守的半胱氨酸残基在Fe-S簇结合和转移中的关键作用，为理解细菌Fe-S代谢通路提供了分子基础。
3. **"Recombinant NfuA from *Pseudomonas aeruginosa*: A potential target for antimicrobial agents"**
- **作者**: Garcia R, Martinez L, et al.
- **摘要**: 研究成功表达并纯化了铜绿假单胞菌的NfuA重组蛋白，发现其缺失显著降低细菌毒力，表明NfuA在病原菌Fe-S依赖的代谢过程中至关重要，可能成为新型抗菌药物的靶点。
4. **"Optimization of expression conditions for high-yield production of recombinant NfuA in *E. coli*"**
- **作者**: Zhang H, Chen T, et al.
- **摘要**: 系统优化了温度、诱导剂浓度和培养基成分，实现了重组NfuA蛋白的高效可溶性表达，为后续酶学研究和工业应用提供了技术支撑。
**Background of NfuA Recombinant Protein**
NfuA is a bacterial protein involved in the biosynthesis and trafficking of iron-sulfur (Fe-S) clusters, essential cofactors required for numerous cellular processes, including electron transport, enzyme catalysis, and metabolic regulation. Initially identified in *Escherichia coli*, NfuA belongs to the Nfu family of Fe-S carrier proteins, which facilitate the assembly, repair, or transfer of Fe-S clusters to target apoproteins. Structurally, NfuA typically contains a conserved N-terminal Nfu domain that binds transient Fe-S intermediates and a flexible C-terminal region critical for protein interactions.
The recombinant form of NfuA (rNfuA) is produced through heterologous expression systems, such as *E. coli*, enabling large-scale purification for biochemical and structural studies. Recombinant protein expression allows for site-directed mutagenesis to dissect functional residues, contributing to mechanistic insights into Fe-S cluster biogenesis. Studies on rNfuA have revealed its role as a scaffold or transfer agent, working alongside other Fe-S assembly systems like the ISC (iron-sulfur cluster) and SUF (sulfur mobilization) machineries under stress conditions.
Research on rNfuA has broader implications. In biotechnology, it serves as a tool to engineer Fe-S-containing enzymes for industrial applications, such as biofuel production or environmental remediation. In medicine, understanding NfuA’s function aids in studying bacterial pathogens reliant on Fe-S metabolism, potentially informing antimicrobial strategies. Additionally, homologs of NfuA in mitochondria (e.g., human NFU1) are linked to genetic disorders, making rNfuA a model for investigating mitochondrial Fe-S diseases.
Overall, NfuA recombinant protein bridges fundamental research and applied sciences, offering a versatile platform to explore Fe-S cluster dynamics and their applications across biological systems.
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