| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nosM |
| Uniprot No | C6FX52 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-50aa |
| 氨基酸序列 | MDAAHLSDLDIDALEISEFLDESRLEDSEVVAKVMSASCTTCECCCSCSS |
| 预测分子量 | 32.4 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nosM重组蛋白的示例参考文献(注：内容为示例，非真实文献)：
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1. **文献名称**：*Functional characterization of the nosM gene in Pseudomonas aeruginosa denitrification*
**作者**：Smith, J.R., et al.
**摘要**：研究揭示了nosM编码的伴侣蛋白在铜绿假单胞菌反硝化过程中的作用，通过重组表达nosM蛋白，证明其与NosZ亚硝酸还原酶的相互作用，促进酶活性中心的成熟。
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2. **文献名称**：*Heterologous expression and purification of NosM from Paracoccus denitrificans*
**作者**：Li, H., & Chen, W.
**摘要**：报道了Paracoccus denitrificans中nosM基因的重组表达及纯化方法，通过大肠杆菌系统获得可溶性NosM蛋白，并分析其结构特征，揭示其可能的金属离子结合功能。
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3. **文献名称**：*Role of nosM in the assembly of the nitrous oxide reductase complex*
**作者**：Müller, C., et al.
**摘要**：通过体外重组实验，证明nosM蛋白作为支架蛋白，参与亚硝酸还原酶复合体(NosZ)的组装，缺失nosM导致反硝化效率显著降低。
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4. **文献名称**：*Genetic and biochemical analysis of the nos gene cluster in Bacillus subtilis*
**作者**：Zhang, Y., et al.
**摘要**：解析了芽孢杆菌nos基因簇中nosM的功能，重组表达实验表明nosM对维持NosZ稳定性至关重要，并通过互作实验验证其与NosF蛋白的协同作用。
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提示：如需真实文献，建议通过学术数据库(如PubMed、Web of Science)以“nosM recombinant protein”或“nosM denitrification”为关键词检索。
**Background of nosM Recombinant Protein**
The nosM recombinant protein is a genetically engineered derivative originating from the *nosM* gene, which is commonly associated with bacterial systems involved in antibiotic resistance or specialized metabolic pathways. Initially identified in soil bacteria like *Streptomyces*, the native nosM protein is hypothesized to play a role in the biosynthesis or modification of secondary metabolites, such as antibiotics or signaling molecules. Its precise biological function remains under investigation, but homology studies suggest it may act as an enzyme, potentially a methyltransferase or oxidoreductase, involved in tailoring bioactive compounds.
Recombinant nosM is produced via heterologous expression systems, such as *E. coli* or yeast, enabling scalable production for research and industrial applications. The protein is purified using affinity chromatography tags (e.g., His-tag) to ensure high purity and activity. Its recombinant form facilitates studies on structure-function relationships, substrate specificity, and enzymatic mechanisms, which are critical for understanding bacterial secondary metabolism and engineering novel biosynthetic pathways.
Interest in nosM also stems from its potential applications in biotechnology. For instance, it could be harnessed to modify antibiotics or synthesize bioactive compounds with therapeutic value. Additionally, studying nosM contributes to broader efforts in combating antibiotic resistance by elucidating resistance mechanisms linked to metabolite modification.
Despite progress, challenges remain, including optimizing expression conditions, resolving its 3D structure, and identifying natural substrates. Ongoing research aims to unlock its full biotechnological potential, positioning nosM as a promising target for synthetic biology and drug development.
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