| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | mep |
| Uniprot No | P07711 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-333aa |
| 氨基酸序列 | TLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV |
| 预测分子量 | 37.2 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MEP(甲基赤藓糖醇磷酸途径)重组蛋白研究的示例参考文献，内容基于常见研究方向模拟，实际文献请通过学术数据库查询：
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1. **文献名称**：*Heterologous Expression and Characterization of 1-Deoxy-D-Xylulose 5-Phosphate Reductoisomerase from Arabidopsis thaliana*
**作者**：Zhang Y, et al.
**摘要**：本研究在大肠杆菌中重组表达了拟南芥来源的DXR酶(MEP途径关键酶)，优化了纯化条件并分析了酶动力学参数，为体外重构MEP途径提供基础。
2. **文献名称**：*Metabolic Engineering of E. coli for Isoprene Production via the MEP Pathway*
**作者**：Lee SY, et al.
**摘要**：通过过表达MEP途径中的重组DXS和IDI蛋白，改造大肠杆菌菌株，显著提高了异戊二烯产量，并探讨了限速步骤的调控策略。
3. **文献名称**：*Crystal Structure of IspH (LytB) in the MEP Pathway: Insights into [Fe4S4] Cluster Coordination*
**作者**：Gräwert T, et al.
**摘要**：解析了MEP途径末端酶IspH的晶体结构，揭示了其[Fe4S4]活性中心的作用机制，为设计针对病原微生物的抑制剂提供了结构基础。
4. **文献名称**：*Comparative Analysis of MEP and MVA Pathways in Recombinant Saccharomyces cerevisiae*
**作者**：Chen X, et al.
**摘要**：在酵母中同时引入重组MEP途径酶和甲羟戊酸(MVA)途径，比较了两条途径对萜类化合物合成的贡献，提出了协同代谢工程策略。
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**注意**：以上为模拟示例，具体研究需参考真实文献(如PubMed、ScienceDirect等平台)。MEP途径相关重组蛋白研究多聚焦于酶功能解析、代谢工程及工业生物技术应用。
**Background of MEP Recombinant Proteins**
The mevalonate-independent methylerythritol phosphate (MEP) pathway is a critical metabolic route for synthesizing isoprenoid precursors, such as isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP). Unlike the mevalonate (MVA) pathway found in animals, fungi, and some bacteria, the MEP pathway operates in most bacteria, apicomplexan parasites, and plant chloroplasts. This pathway produces essential building blocks for diverse isoprenoids, including terpenes, sterols, and carotenoids, which play vital roles in cellular function, defense, and adaptation.
Recombinant proteins derived from the MEP pathway have gained attention for biotechnological and pharmaceutical applications. By engineering microbial hosts (e.g., *E. coli* or yeast) to express MEP pathway enzymes, researchers aim to optimize the production of high-value isoprenoids, such as artemisinin (antimalarial) or taxol (anticancer). The MEP pathway’s higher theoretical yield and energy efficiency compared to the MVA pathway make it an attractive target for metabolic engineering.
However, reconstructing the MEP pathway in heterologous hosts faces challenges, including enzyme compatibility, metabolic flux imbalances, and toxicity of intermediates. Advances in synthetic biology, CRISPR-Cas9 editing, and systems biology have enabled precise tuning of pathway enzymes and host metabolism to enhance productivity. Additionally, MEP-derived recombinant proteins are explored for vaccine development, as some pathway enzymes in pathogens (e.g., *Plasmodium falciparum*) serve as potential drug targets.
Overall, MEP recombinant proteins bridge fundamental biochemistry and industrial applications, offering sustainable alternatives for producing complex natural compounds and addressing global health challenges. Ongoing research focuses on improving pathway efficiency, scalability, and adaptability across diverse host systems.
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