| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NOS2 |
| Uniprot No | P35228 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-200aa |
| 氨基酸序列 | MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPLVETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRC |
| 预测分子量 | 26.6 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3篇关于NOS2(诱导型一氧化氮合酶)重组蛋白研究的参考文献摘要概括：
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1. **标题**: *"Expression and purification of functional human inducible nitric oxide synthase in Escherichia coli"*
**作者**: Stuehr, D.J., et al.
**摘要**: 该研究首次在大肠杆菌中成功表达了具有酶活性的人源NOS2重组蛋白，通过优化表达条件和辅助因子(如血红素、四氢生物蝶呤)的添加，实现了可溶性蛋白的高效纯化，并验证其催化生成一氧化氮的功能。
2. **标题**: *"Crystal structure of the heme domain of inducible nitric oxide synthase bound with a selective inhibitor"*
**作者**: Crane, B.R., et al.
**摘要**: 本研究解析了小鼠NOS2重组蛋白血红素结构域的晶体结构，揭示了其与选择性抑制剂复合物的结合模式，为基于结构的药物设计(如抗炎治疗)提供了关键结构信息。
3. **标题**: *"Baculovirus-mediated expression of rat inducible nitric oxide synthase in insect cells: High-yield purification and characterization"*
**作者**: McMillan, K., et al.
**摘要**: 利用杆状病毒-昆虫细胞表达系统高效表达大鼠NOS2重组蛋白，通过亲和层析和离子交换层析获得高纯度蛋白，并证明其二聚体形式具有持续催化活性，适用于酶学机制研究。
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注：以上文献为示例，实际引用时需核对具体年份及期刊信息。如需更多文献，建议在PubMed或SciHub中以“recombinant NOS2/iNOS expression”为关键词检索。
Nitric oxide synthase 2 (NOS2), also known as inducible nitric oxide synthase (iNOS), is a critical enzyme responsible for catalyzing the production of nitric oxide (NO) from L-arginine. Unlike its constitutive isoforms (NOS1 and NOS3), NOS2 is typically absent under normal physiological conditions but is rapidly induced in response to inflammatory stimuli, such as cytokines (e.g., TNF-α, IFN-γ) or microbial pathogens. This induction occurs primarily in immune cells (e.g., macrophages), epithelial cells, and hepatocytes. NO generated by NOS2 plays dual roles: it serves as a key antimicrobial agent in host defense by disrupting pathogen metabolism, while excessive or prolonged production contributes to tissue damage in chronic inflammatory diseases, including sepsis, asthma, and neurodegenerative disorders.
Recombinant NOS2 protein is engineered through molecular cloning techniques, often expressed in heterologous systems like *E. coli*, insect cells, or mammalian cell lines. Its production enables detailed biochemical characterization, including studies on enzyme kinetics, post-translational modifications, and interactions with inhibitors or cofactors (e.g., tetrahydrobiopterin, calmodulin). Researchers utilize recombinant NOS2 to investigate regulatory mechanisms of NO signaling, screen potential therapeutic compounds targeting inflammatory pathways, and model disease-associated mutations. Challenges in producing functional recombinant NOS2 include maintaining solubility, stability, and proper dimerization, as the enzyme requires multiple cofactors for activity. Advances in protein engineering and purification strategies have improved yields and activity retention, facilitating its application in drug discovery and mechanistic studies. Current research focuses on modulating NOS2 activity to balance its protective and detrimental effects, offering potential therapies for inflammation-related conditions.
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