| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MOGS |
| Uniprot No | Q13724 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-837aa |
| 氨基酸序列 | MARGERRRRAVPAEGVRTAERAARGGPGRRDGRGGGPRSTAGGVALAVVVLSLALGMSGRWVLAWYRARRAVTLHSAPPVLPADSSSPAVAPDLFWGTYRPHVYFGMKTRSPKPLLTGLMWAQQGTTPGTPKLRHTCEQGDGVGPYGWEFHDGLSFGRQHIQDGALRLTTEFVKRPGGQHGGDWSWRVTVEPQDSGTSALPLVSLFFYVVTDGKEVLLPEVGAKGQLKFISGHTSELGDFRFTLLPPTSPGDTAPKYGSYNVFWTSNPGLPLLTEMVKSRLNSWFQHRPPGAPPERYLGLPGSLKWEDRGPSGQGQGQFLIQQVTLKIPISIEFVFESGSAQAGGNQALPRLAGSLLTQALESHAEGFRERFEKTFQLKEKGLSSGEQVLGQAALSGLLGGIGYFYGQGLVLPDIGVEGSEQKVDPALFPPVPLFTAVPSRSFFPRGFLWDEGFHQLVVQRWDPSLTREALGHWLGLLNADGWIGREQILGDEARARVPPEFLVQRAVHANPPTLLLPVAHMLEVGDPDDLAFLRKALPRLHAWFSWLHQSQAGPLPLSYRWRGRDPALPTLLNPKTLPSGLDDYPRASHPSVTERHLDLRCWVALGARVLTRLAEHLGEAEVAAELGPLAASLEAAESLDELHWAPELGVFADFGNHTKAVQLKPRPPQGLVRVVGRPQPQLQYVDALGYVSLFPLLLRLLDPTSSRLGPLLDILADSRHLWSPFGLRSLAASSSFYGQRNSEHDPPYWRGAVWLNVNYLALGALHHYGHLEGPHQARAAKLHGELRANVVGNVWRQYQATGFLWEQYSDRDGRGMGCRPFHGWTSLVLLAMAEDY |
| 预测分子量 | 91,9 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MOGS重组蛋白的3篇虚构示例文献(注：文献名称和作者为模拟示例，非真实存在)：
1. **文献名称**: "Structural and Functional Characterization of Recombinant Human MOGS"
**作者**: Zhang Y, et al.
**摘要**: 本研究通过杆状病毒-昆虫细胞系统重组表达了人源MOGS蛋白，解析了其晶体结构(分辨率2.8Å)，揭示了其催化结构域中关键氨基酸残基(如Asp123和Glu267)在糖苷水解酶活性中的作用机制。
2. **文献名称**: "MOGS Deficiency Correction by Recombinant Enzyme Replacement in Cellular Models"
**作者**: Müller S, et al.
**摘要**: 开发了CHO细胞表达的重组MOGS蛋白，通过体外酶活性实验证明其可恢复MOGS缺陷型成纤维细胞的内质网糖基化异常，为II型先天性糖基化病(CDG-IIb)的酶替代疗法提供了实验依据。
3. **文献名称**: "High-Yield Production of Active MOGS in E. coli Using Codon Optimization and Fusion Tags"
**作者**: Kim J, Park H.
**摘要**: 通过密码子优化及麦芽糖结合蛋白(MBP)融合标签策略，在大肠杆菌中实现可溶性重组MOGS的高效表达(产量达15 mg/L)，纯化产物在体外成功去除了Glc3Man9GlcNAc2脂质连接寡糖的末端葡萄糖残基。
MOGS (mannosyl-oligosaccharide glucosidase) is a critical enzyme involved in the processing of N-linked glycans during protein glycosylation. Found in the endoplasmic reticulum, MOGS catalyzes the removal of terminal α1.2-glucose residues from the Glc₃Man₉GlcNAc₂ oligosaccharide precursor, a step essential for proper glycoprotein folding and quality control. This trimming process enables interaction with lectin chaperones like calnexin/calreticulin, ensuring correct protein folding or targeting misfolded proteins for degradation.
The recombinant form of MOGS has gained attention for both research and therapeutic applications. Produced through heterologous expression systems (e.g., E. coli, mammalian cells), recombinant MOGS retains enzymatic activity and serves as a tool to study N-glycan processing mechanisms. Its significance extends to understanding congenital disorders of glycosylation (CDGs), particularly MOGS-CDG (formerly CDG-IIb), a rare autosomal recessive disease caused by mutations in the MOGS gene. Patients with this condition exhibit severe neurological impairments, immunodeficiency, and developmental delays due to defective glycan processing.
Recent advances have explored recombinant MOGS in enzyme replacement therapy (ERT) strategies, though challenges persist in cellular delivery and ER targeting. Structural studies using recombinant proteins have elucidated substrate-binding domains and catalytic residues, informing drug discovery efforts. Additionally, MOGS inhibitors are being investigated for antiviral applications, as some viruses exploit host glycosylation machinery. The development of recombinant MOGS variants with enhanced stability or modified activity continues to expand its utility in glycobiology research and potential clinical interventions.
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