| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MVK |
| Uniprot No | Q03426 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-396aa |
| 氨基酸序列 | MLSEVLLVSA PGKVILHGEH AVVHGKVALA VSLNLRTFLR LQPHSNGKVD LSLPNIGIKR AWDVARLQSL DTSFLEQGDV TTPTSEQVEK LKEVAGLPDD CAVTERLAVL AFLYLYLSIC RKQRALPSLD IVVWSELPPG AGLGSSAAYS VCLAAALLTV CEEIPNPLKD GDCVNRWTKE DLELINKWAF QGERMIHGNP SGVDNAVSTW GGALRYHQGK ISSLKRSPAL QILLTNTKVP RNTRALVAGV RNRLLKFPEI VAPLLTSIDA ISLECERVLG EMGEAPAPEQ YLVLEELIDM NQHHLNALGV GHASLDQLCQ VTRARGLHSK LTGAGGGGCG ITLLKPGLEQ PEVEATKQAL TSCGFDCLET SIGAPGVSIH SATSLDSRVQ QALDGL |
| 预测分子量 | 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MVK(甲羟戊酸激酶)重组蛋白的3篇代表性文献的简要列举(内容基于模拟文献，仅供参考)：
1. **文献名称**：*Expression and Purification of Recombinant Human Mevalonate Kinase in Escherichia coli*
**作者**：Hergenreder, D.A., et al.
**摘要**：该研究报道了人源MVK基因在大肠杆菌中的高效表达及纯化方法，通过优化表达条件获得可溶性重组蛋白，并验证其酶活性，为后续功能研究提供了基础工具。
2. **文献名称**：*Crystal Structure of Mevalonate Kinase: Insights into Catalytic Mechanism and Disease-Causing Mutations*
**作者**：Ladenstein, R., et al.
**摘要**：本文解析了MVK的晶体结构，揭示了其ATP结合域和底物识别位点的特征，阐明了致病性突变(如V377I)导致酶活性降低的结构机制，为遗传性疾病研究提供分子基础。
3. **文献名称**：*Functional Characterization of Pathogenic Mutations in Mevalonate Kinase Deficiency Using Recombinant Enzyme Assays*
**作者**：Houten, S.M., et al.
**摘要**：研究通过体外重组MVK蛋白活性实验，分析了多种突变体(如D203N、H20P)的动力学参数，证明突变导致酶稳定性下降和底物亲和力改变，解释了甲羟戊酸尿症的病理机制。
4. **文献名称**：*Development of a High-Throughput Screening Assay for MVK Inhibitors Using Recombinant Protein*
**作者**：Zhang, Y., et al.
**摘要**：基于重组MVK蛋白构建了高通量抑制剂筛选平台，用于发现调控胆固醇代谢的小分子化合物，为治疗代谢性疾病提供潜在药物候选策略。
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注：以上文献信息为模拟生成，实际引用时请以真实数据库(如PubMed)检索结果为准。
**Background of MVK Recombinant Protein**
Mevalonate kinase (MVK) is a pivotal enzyme in the mevalonate pathway, a metabolic route essential for synthesizing isoprenoids and sterols, including cholesterol and non-sterol isoprenoids. MVK catalyzes the phosphorylation of mevalonate to mevalonate-5-phosphate, a rate-limiting step in this pathway. Dysregulation of MVK activity is linked to metabolic disorders such as mevalonic aciduria (MA) and hyperimmunoglobulinemia D syndrome (HIDS), both characterized by mutations in the *MVK* gene. These autosomal recessive conditions highlight MVK's critical role in maintaining cellular homeostasis.
Recombinant MVK protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, enabling large-scale purification for research and therapeutic applications. Its production involves cloning the *MVK* gene into expression vectors, followed by protein extraction, affinity chromatography, and quality validation (e.g., SDS-PAGE, enzymatic assays). Recombinant MVK retains catalytic activity, making it invaluable for studying enzyme kinetics, substrate specificity, and inhibitor interactions.
In drug discovery, recombinant MVK serves as a tool to screen small molecules targeting the mevalonate pathway, particularly for diseases like MA or cancers reliant on isoprenoid intermediates. Structural studies using recombinant MVK have revealed insights into its ATP-binding domain and conformational changes during catalysis, aiding the design of allosteric modulators. Additionally, it facilitates the study of disease-associated mutations, helping correlate genetic variants with functional deficits.
Despite progress, challenges remain in stabilizing the recombinant protein and mimicking its native cellular environment. Ongoing research focuses on optimizing expression systems and cryo-EM studies to resolve full-length MVK structures, which could unlock novel therapeutic strategies for MVK-related disorders and beyond.
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