| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MGLL |
| Uniprot No | Q99685 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-303aa |
| 氨基酸序列 | MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP |
| 预测分子量 | 60.3kDa |
| 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MGLL重组蛋白的3篇参考文献示例：
1. **《Structural and Functional Analysis of Recombinant Human Monoacylglycerol Lipase》**
- 作者：Long, J.Z. 等
- 摘要：通过在大肠杆菌中表达重组人源MGLL蛋白，解析其晶体结构并验证其水解单酰基甘油的酶活性，为开发靶向抑制剂提供结构基础。
2. **《Optimization of Recombinant MGLL Expression in Insect Cells for High-Throughput Drug Screening》**
- 作者：Nomura, D.K. 等
- 摘要：利用杆状病毒-昆虫细胞系统高效表达功能性MGLL蛋白，优化纯化流程并应用于高通量药物筛选，评估其在代谢疾病治疗中的应用潜力。
3. **《Functional Characterization of MGLL Knockout Models Using Recombinant Protein Rescue》**
- 作者：Cravatt, B.F. 等
- 摘要：通过重组MGLL蛋白回补实验，验证其在神经炎症调控中的关键作用，揭示其通过内源性大麻素信号通路影响痛觉调节的机制。
*注：上述文献为示例，实际引用时建议通过学术数据库核实具体信息。*
**Background of MGLL Recombinant Protein**
Monoacylglycerol lipase (MGLL), also known as MAG lipase, is a serine hydrolase that plays a critical role in lipid metabolism. It primarily catalyzes the hydrolysis of monoacylglycerols (MAGs), such as 2-arachidonoylglycerol (2-AG), into free fatty acids and glycerol. As a key enzyme in the endocannabinoid system, MGLL regulates 2-AG signaling, which influences physiological processes including pain perception, inflammation, and energy homeostasis. Dysregulation of MGLL activity has been linked to metabolic disorders, neurodegenerative diseases, and cancer, making it a therapeutic target of interest.
Recombinant MGLL protein is engineered using biotechnological methods, typically expressed in heterologous systems like *E. coli* or mammalian cells. This allows large-scale production of purified, active enzyme for research and drug discovery. The recombinant form retains the functional domains of native MGLL, including the catalytic triad (Ser122. Asp239. His269) and the lid domain that modulates substrate access. Structural studies using recombinant MGLL have revealed insights into its mechanism, substrate specificity, and interactions with inhibitors.
Applications of MGLL recombinant protein span *in vitro* assays to screen inhibitors, enzymology studies to characterize kinetic properties, and structural biology for rational drug design. Its role in degrading 2-AG also makes it a tool to study endocannabinoid signaling pathways. Furthermore, MGLL inhibitors, developed using recombinant protein, are being explored for treating conditions like obesity, chronic pain, and neurodegenerative disorders.
Overall, MGLL recombinant protein serves as a vital resource for understanding lipid metabolism and advancing therapies targeting the endocannabinoid system. Its study bridges biochemistry, pharmacology, and translational medicine, highlighting its multifaceted significance.
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