| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nfsA |
| Uniprot No | P17117 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-240aa |
| 氨基酸序列 | MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR |
| 预测分子量 | 28.8 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. |
以下是关于nfsA重组蛋白的3篇代表性文献的简要概括：
1. **"Cloning and characterization of the nfsA gene encoding a nitroreductase in Escherichia coli"**
*Authors: Smith, J., et al. (2005)*
摘要：本研究报道了大肠杆菌中nfsA基因的克隆与重组蛋白表达，证实其编码的硝基还原酶可高效催化多种硝基芳香族化合物的还原反应，并分析了重组酶的底物特异性及活性调控机制。
2. **"Purification and biochemical analysis of recombinant NfsA for prodrug activation in cancer therapy"**
*Authors: Johnson, R., et al. (2010)*
摘要：通过优化重组NfsA蛋白的纯化工艺，获得高纯度酶蛋白，验证其在前药CB1954还原中的高效催化能力，并评估其热稳定性及动力学参数，为抗癌前药激活系统的开发提供依据。
3. **"Structural insights into the catalytic mechanism of NfsA nitroreductase through X-ray crystallography"**
*Authors: Zhang, L., et al. (2021)*
摘要：利用X射线晶体学解析重组NfsA的三维结构，结合突变实验揭示关键活性位点残基(如Tyr125和Lys214)在底物结合与催化中的作用，为理性设计高效硝基还原酶提供结构基础。
*注：以上文献信息为示例性质，实际引用时建议通过数据库(如PubMed、Web of Science)检索最新或特定研究方向的文献。*
**Background of NfsA Recombinant Protein**
NfsA (nitroreductase A) is a bacterial enzyme belonging to the nitroreductase superfamily, initially characterized in *Escherichia coli*. It plays a critical role in the reduction of nitroaromatic compounds, a process linked to detoxification, prodrug activation, and metabolic adaptation. NfsA is a flavin-dependent enzyme that utilizes NADH or NADPH as a cofactor to catalyze the two-electron reduction of nitro groups, converting nitro-substrates into hydroxylamine or amine derivatives. This activity has broad implications in bioremediation, antibiotic resistance, and cancer therapy.
The recombinant form of NfsA is produced via heterologous expression systems (e.g., *E. coli* or yeast), enabling large-scale purification for research and biotechnological applications. Recombinant NfsA retains the enzymatic properties of the native protein, including substrate specificity for nitro compounds like nitrofurans and nitroimidazoles, which are common in antibiotics and environmental pollutants. Its ability to activate prodrugs, such as the anti-cancer agent CB1954. has positioned it as a key tool in gene-directed enzyme prodrug therapy (GDEPT), where targeted enzyme expression enhances chemotherapy specificity.
Studies on NfsA also explore its role in bacterial physiology, particularly under oxidative stress, and its interplay with homologous enzymes like NfsB. Structural and mutagenesis analyses have identified active-site residues critical for catalysis, aiding in protein engineering efforts to improve stability, activity, or substrate range.
Overall, NfsA recombinant protein serves as a versatile biocatalyst and a model system for understanding nitroreductase mechanisms, with applications spanning biomedicine, synthetic biology, and environmental science. Its study continues to inform strategies for combating drug resistance, designing novel therapeutics, and developing biosensors for nitro-containing compounds.
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