| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nrdD |
| Uniprot No | P28903 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-712aa |
| 氨基酸序列 | MTPHVMKRDGCKVPFKSERIKEAILRAAKAAEVDDADYCATVAAVVSEQMQGRNQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIEREKRGRLNQEIRGLVEQTNASLLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTASYNKHRKTAEEWNIPDAEGYANSRTIKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQESILRNRIAGLGKNRKTAVFPKLVFAIRDGLNHKKGDPNYDIKQLALECASKRMYPDILNYDQVVKVTGSFKTPMGCRSFLGVWENENGEQIHDGRNNLGVISLNLPRIALEAKGDEATFWKLLDERLVLARKALMTRIARLEGVKARVAPILYMEGACGVRLNADDDVSEIFKNGRASISLGYIGIHETINALFGGEHVYDNEQLRAKGIAIVERLRQAVDQWKEETGYGFSLYSTPSENLCDRFCRLDTAEFGVVPGVTDKGYYTNSFHLDVEKKVNPYDKIDFEAPYPPLANGGFICYGEYPNIQHNLKALEDVWDYSYQHVPYYGTNTPIDECYECGFTGEFECTSKGFTCPKCGNHDASRVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHLGNGQIG |
| 预测分子量 | 84.0 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nrdD重组蛋白的3篇参考文献示例(内容基于公开研究背景综合整理，非真实文献)：
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1. **文献名称**: "Cloning and functional characterization of the anaerobic ribonucleotide reductase nrdD from *Escherichia coli*"
**作者**: Smith J, et al.
**摘要**: 本研究克隆并表达了来自大肠杆菌的nrdD基因，验证其编码的α亚基在厌氧条件下催化核糖核苷酸还原为脱氧核糖核苷酸的功能。重组蛋白通过亲和层析纯化，酶活实验表明其依赖SAM辅因子且对氧敏感。
2. **文献名称**: "Structural insights into the mechanism of NrdD anaerobic ribonucleotide reductase"
**作者**: Lee C, et al.
**摘要**: 通过X射线晶体学解析了nrdD重组蛋白的三维结构，揭示了其活性中心独特的铁硫簇构型，阐明了其在低氧环境中通过自由基机制催化底物还原的分子基础。
3. **文献名称**: "Heterologous expression of *Salmonella* nrdD in *Bacillus subtilis* enhances anaerobic DNA synthesis"
**作者**: Zhang R, et al.
**摘要**: 将沙门氏菌nrdD基因在枯草芽孢杆菌中异源表达，发现重组蛋白显著提升了宿主在缺氧条件下的dNTP合成能力，为工程菌株的厌氧代谢改造提供了新策略。
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注：以上文献为示例，实际研究中建议通过PubMed或Google Scholar以关键词“nrdD recombinant protein”或“anaerobic ribonucleotide reductase”检索最新论文。
NrdD recombinant protein is derived from the nrdD gene, which encodes a class III anaerobic ribonucleotide reductase (RNR). Ribonucleotide reductases are essential enzymes responsible for the conversion of ribonucleotides to deoxyribonucleotides, a critical step in DNA synthesis and repair across all domains of life. Unlike oxygen-dependent class I and class II RNRs, class III enzymes, including NrdD, function under anaerobic conditions, making them vital for organisms inhabiting oxygen-limited environments such as certain bacteria, archaea, and pathogens.
NrdD operates through a unique radical-based mechanism involving a glycyl radical cofactor, generated by an activating enzyme (e.g., NrdG) using S-adenosylmethionine (AdoMet) and iron-sulfur clusters. This oxygen-sensitive radical enables NrdD to catalyze substrate reduction without requiring molecular oxygen, a key adaptation for anaerobic metabolism. Structurally, NrdD typically forms a homodimer with active sites coordinating essential metal ions and radical propagation pathways.
Recombinant NrdD is produced via heterologous expression in bacterial systems (e.g., *E. coli*), often with affinity tags for purification. Its study provides insights into anaerobic nucleotide metabolism, enzyme evolution, and radical-driven catalysis. Biotechnologically, NrdD has potential applications in elucidating antimicrobial drug targets, as pathogens reliant on anaerobic RNRs (e.g., *Clostridium*, *Bacteroides*) depend on NrdD for survival. Additionally, engineered NrdD variants are explored for industrial biocatalysis under oxygen-free conditions. Research continues to address challenges such as oxygen sensitivity during protein production and mechanistic nuances of radical initiation and transfer.
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