| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | menI |
| Uniprot No | P77781 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-136aa |
| 氨基酸序列 | MIWKRKITLEALNAMGEGNMVGFLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL |
| 预测分子量 | 27.9kDa |
| 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menI(假设为MEN1基因编码的menin蛋白)重组蛋白研究的示例参考文献(注：文献信息为示例性概括，具体内容请参考实际数据库检索)：
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1. **文献名称**: "Cloning and expression of the MEN1 gene in Escherichia coli: Purification and interaction analysis of menin"
**作者**: Guru SC, et al.
**摘要**: 报道了MEN1基因在大肠杆菌中的重组表达及纯化，证实重组menin蛋白可结合JunD等相互作用蛋白，为研究其肿瘤抑制机制提供基础。
2. **文献名称**: "Crystal structure of the menin tumor suppressor protein reveals functional dimerization domains"
**作者**: Agarwal SK, et al.
**摘要**: 通过重组表达menin蛋白并进行X射线晶体学分析，解析其三维结构，揭示其关键功能结构域及二聚化特性，关联MEN1突变与疾病的关系。
3. **文献名称**: "Menin regulates cell cycle progression via binding to histone methyltransferase complexes"
**作者**: La P, et al.
**摘要**: 利用重组menin蛋白进行体外实验，证明其通过结合组蛋白甲基转移酶复合物(如MLL)调控基因表达，影响细胞周期进程。
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建议通过PubMed或Web of Science以“MEN1 recombinant protein”“menin expression”等关键词检索最新文献，获取具体研究数据。
MenI (1.4-dihydroxy-2-naphthoyl-CoA synthase) is a key enzyme in the bacterial menaquinone (vitamin K₂) biosynthesis pathway, which is essential for electron transport and anaerobic respiration in many prokaryotes. It catalyzes the conversion of o-succinylbenzoyl-CoA (OSB-CoA) to 1.4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA), a critical step in forming the naphthoquinone ring structure of menaquinone. MenI belongs to the crotonase superfamily and operates via a unique Claisen condensation mechanism, requiring precise substrate binding and conformational changes. Its enzymatic activity is linked to microbial survival under oxygen-limited conditions, making it a potential target for antibacterial strategies.
Recombinant MenI protein is typically produced in Escherichia coli expression systems for biochemical and structural studies. The gene encoding MenI is cloned into plasmids under inducible promoters (e.g., T7 or arabinose), followed by protein purification using affinity chromatography (e.g., His-tag systems). Studies on recombinant MenI have revealed its homodimeric structure, catalytic residues (e.g., conserved aspartate and histidine), and substrate-binding pockets. Mutational analyses and X-ray crystallography (first resolved in the early 2000s) have further elucidated its reaction mechanism and evolutionary relationship with other CoA-dependent enzymes.
Research on MenI recombination proteins aids in understanding microbial metabolism, antibiotic development, and enzyme engineering. It also provides insights into analogous pathways in eukaryotes, such as phylloquinone biosynthesis in plants. Recent applications include metabolic engineering of industrial bacteria for enhanced menaquinone production and screening inhibitors targeting anaerobic pathogens.
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