纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MGL |
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 | 60.3 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MGL(Monoglyceride Lipase)重组蛋白的3篇参考文献示例,包含文献名称、作者及摘要内容概括:
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1. **文献名称**:*Expression and Purification of Recombinant MGL in E. coli for Functional Studies*
**作者**:Chen L, et al.
**摘要**:本研究描述了一种高效在大肠杆菌中表达和纯化重组MGL蛋白的方法,验证了其酶活性和底物特异性,为脂代谢研究提供了工具。
2. **文献名称**:*Structural Insights into MGL Catalytic Mechanism by Cryo-EM Analysis*
**作者**:Smith J, et al.
**摘要**:通过冷冻电镜解析了重组MGL的三维结构,揭示了其催化位点的关键氨基酸及底物结合机制,为设计抑制剂提供结构基础。
3. **文献名称**:*MGL Knockout and Recombinant Protein Rescue in Neuronal Cell Models*
**作者**:Wang Y, et al.
**摘要**:利用CRISPR技术构建MGL基因敲除细胞系,并通过外源重组MGL蛋白恢复内源性2-AG水解功能,证实其在神经信号中的调控作用。
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注:以上文献为示例性质,实际引用时需以真实发表的论文为准。建议通过PubMed或Web of Science以“MGL recombinant protein”或“monoglyceride lipase expression”为关键词检索最新研究。
Monoacylglycerol lipase (MGL), a serine hydrolase encoded by the *MGLL* gene, is a key enzyme in lipid metabolism and the endocannabinoid system. It primarily catalyzes the hydrolysis of monoacylglycerols, including 2-arachidonoylglycerol (2-AG), a major endogenous cannabinoid neurotransmitter. By regulating 2-AG signaling, MGL modulates synaptic plasticity, pain perception, appetite, and inflammatory responses. Dysregulation of MGL activity has been implicated in metabolic disorders, neurodegenerative diseases, and cancer, making it a therapeutic target for drug development.
Recombinant MGL proteins are engineered using expression systems like *E. coli* or mammalian cells to enable large-scale production for biochemical and pharmacological studies. These systems allow precise control over protein folding, post-translational modifications, and functional characterization. The recombinant protein retains catalytic activity, featuring a conserved α/β-hydrolase fold and a catalytic triad (Ser122-His272-Asp240 in humans) critical for substrate binding and hydrolysis.
Research applications of recombinant MGL include inhibitor screening for metabolic or neurological therapies, structural studies (e.g., X-ray crystallography) to elucidate enzyme mechanisms, and cellular assays to study endocannabinoid signaling pathways. Challenges in its production include maintaining solubility and stability due to its hydrophobic substrate-binding regions. Recent advances in protein engineering and purification techniques (e.g., affinity tags, detergent optimization) have improved yield and functionality, facilitating drug discovery and mechanistic studies targeting MGL-related pathologies.
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