| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PMVK |
| Uniprot No | Q15126 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-192aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAPLGGAPRLVLLFSGKRKSGKDFVTEALQ SRLGADVCAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWG EEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFREAYGAVTQTVR VVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQ LENLIEFIRSRL |
| 预测分子量 | 24 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PMVK(磷酸甲羟戊酸激酶)重组蛋白的3篇示例参考文献(注：文献信息为虚构示例，仅供格式参考)：
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1. **文献名称**：*Heterologous Expression and Enzymatic Characterization of Recombinant PMVK from Arabidopsis thaliana*
**作者**：Chen L, Wang Y, et al.
**摘要**：本研究在大肠杆菌中成功表达了拟南芥来源的PMVK重组蛋白，并优化了纯化条件。酶动力学分析表明，该蛋白对ATP和磷酸甲羟戊酸具有高亲和力，为植物类异戊二烯代谢途径研究提供了工具。
2. **文献名称**：*Crystal Structure of Human PMVK Reveals Substrate Binding Mechanism*
**作者**：Rodriguez M, Kim S, et al.
**摘要**：通过X射线衍射解析了人源PMVK的晶体结构，揭示了其与底物和辅因子结合的关键氨基酸残基，为针对胆固醇合成异常的药物设计提供了结构依据。
3. **文献名称**：*Functional Complementation of PMVK Deficiency Using Recombinant Protein in a Bacterial System*
**作者**：Tanaka H, et al.
**摘要**：在PMVK缺陷型细菌中表达重组PMVK蛋白，恢复了甲羟戊酸途径的代谢通量，证实了该酶在类异戊二烯前体合成中的必要性。
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**建议**：实际文献可通过PubMed、Web of Science等平台，以关键词“PMVK recombinant expression”、“phosphomevalonate kinase purification”或“PMVK structural/functional analysis”检索获取。
**Background of PMVK Recombinant Protein**
Phosphomevalonate kinase (PMVK) is a critical enzyme in the mevalonate pathway, a metabolic route essential for synthesizing isoprenoids, cholesterol, and other sterols. This pathway is conserved across eukaryotes and certain bacteria, playing a central role in cellular metabolism. PMVK specifically catalyzes the ATP-dependent phosphorylation of mevalonate-5-phosphate (M5P) to produce mevalonate-5-diphosphate (M5PP), a key intermediate in isopentenyl pyrophosphate (IPP) biosynthesis. IPP serves as the building block for molecules like cholesterol, steroid hormones, and ubiquinone, underscoring PMVK's importance in maintaining cellular homeostasis and supporting growth.
Recombinant PMVK proteins are engineered using genetic engineering techniques, where the PMVK gene is cloned into expression vectors and produced in heterologous systems like *E. coli*, yeast, or mammalian cells. This approach enables large-scale production of highly pure, functional PMVK for research and industrial applications. Recombinant PMVK is particularly valuable for studying the mevalonate pathway's regulation, enzyme kinetics, and interactions with potential inhibitors or activators.
Interest in PMVK has grown due to its implications in human health. Dysregulation of the mevalonate pathway is linked to cardiovascular diseases, neurodegenerative disorders, and cancers. For instance, statins, widely used cholesterol-lowering drugs, target HMG-CoA reductase upstream of PMVK, but emerging research explores PMVK as a complementary therapeutic target. Additionally, PMVK's role in bacterial isoprenoid biosynthesis makes it a potential target for antimicrobial agents.
Structural studies using recombinant PMVK have revealed insights into its catalytic mechanism and conformational dynamics, aiding rational drug design. Industrial applications include optimizing microbial systems for isoprenoid-based biofuel or pharmaceutical production. Overall, PMVK recombinant protein serves as a vital tool for advancing both basic science and translational innovations in metabolism-related fields.
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