| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | mbnA |
| Uniprot No | E3YBA4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-30aa |
| 氨基酸序列 | MTVKIAQKKVLPVIGRAAALCGSCYPCSCM |
| 预测分子量 | 3.1kDa |
| 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mbnA重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Recombinant Production and Characterization of MbnA from Methylosinus trichosporium OB3b"
**作者**: Kim, H.J. et al.
**摘要**: 本研究成功在大肠杆菌中异源表达了来自甲烷氧化菌*Methylosinus trichosporium OB3b*的mbnA基因，并通过纯化获得了重组MbnA蛋白。功能分析表明，该蛋白在体外具有高亲和力的铜离子结合能力，为后续研究甲烷菌的铜代谢机制提供了基础。
2. **文献名称**: "Functional Analysis of the MbnA Protein in Methanobactin Biosynthesis"
**作者**: DiSpirito, A.A. et al.
**摘要**: 通过重组MbnA蛋白的体外实验，揭示了其在甲酰胺素(methanobactin)生物合成中的关键作用。研究证实，MbnA作为前体肽酶，参与切割前体肽并激活甲酰胺素的铜螯合功能，为理解微生物次级代谢产物合成途径提供了新视角。
3. **文献名称**: "Structural and Biochemical Insights into the MbnA Copper-Binding Domain"
**作者**: Semrau, J.D. et al.
**摘要**: 利用X射线晶体学解析了重组MbnA蛋白的铜结合结构域的三维结构，结合光谱学实验阐明了其独特的铜配位化学机制。研究为开发基于甲酰胺素的铜生物传感器或环保型金属回收技术提供了理论依据。
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**注**：上述文献信息为示例性质，具体研究内容可能需要根据实际发表的论文调整。建议通过数据库(如PubMed、Web of Science)以关键词“mbnA recombinant protein”或“methanobactin biosynthesis”检索最新文献。
**Background of MbnA Recombinant Protein**
MbnA is a metalloprotein associated with the biosynthesis and transport of methanobactin, a copper-binding chromopeptide produced by certain methanotrophic bacteria. These bacteria utilize methane as their primary carbon and energy source, and methanobactin plays a critical role in copper acquisition, essential for the function of methane monooxygenase (MMO), the enzyme responsible for methane oxidation. MbnA is part of the *mbn* operon, which encodes proteins involved in methanobactin synthesis, modification, and export.
The recombinant MbnA protein is engineered for heterologous expression, typically in *E. coli*, to study its structural and functional properties. Recombinant production allows researchers to purify MbnA in sufficient quantities for biochemical analyses, such as elucidating its role in copper binding, interactions with other operon-encoded proteins, or its contribution to metal homeostasis in methanotrophs. Studies on MbnA also explore its potential biotechnological applications, including environmental remediation (e.g., copper sequestration) or as a template for designing novel metal-chelating agents.
Interest in MbnA extends to understanding microbial adaptation to metal limitation, particularly in methanotrophs inhabiting copper-scarce environments. Additionally, recombinant MbnA serves as a tool to investigate the regulation of the *mbn* operon and its evolutionary conservation across bacterial species. Its characterization may further inform strategies to enhance methane-to-methanol conversion efficiency, a process with industrial relevance. Overall, MbnA recombinant protein bridges fundamental research on bacterial metallobiology and applied studies targeting sustainable bioprocesses.
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