纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MGAT1 |
Uniprot No | P26572 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-445aa |
氨基酸序列 | MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPAPGRPPSVSALDGDPASLTREVIRLAQDAEVELERQRGLLQQIGDALSSQRGRVPTAAPPAQPRVPVTPAPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQAIASYGSAVTHIRQPDLSSIAVPPDHRKFQGYYKIARHYRWALGQVFRQFRFPAAVVVEDDLEVAPDFFEYFRATYPLLKADPSLWCVSAWNDNGKEQMVDASRPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRQGRACIRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVHFTQLDLSYLQREAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPLTWEGYDPSWN |
预测分子量 | 50.8kDa |
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MGAT1重组蛋白的3篇代表性文献的简要信息:
1. **文献名称**:Cloning and expression of human MGAT1 in mammalian cells reveals its role in N-glycan branching
**作者**:Stanley P, et al.
**摘要**:该研究通过克隆人源MGAT1基因并在哺乳动物细胞中表达,验证了其编码的α-1.3-甘露糖基转移酶活性,证明其在调控N-糖链分支结构中的关键作用,并发现其缺失导致细胞表面糖基化模式改变。
2. **文献名称**:Recombinant MGAT1 enhances tumor cell migration by modifying integrin glycosylation
**作者**:Guo H, et al.
**摘要**:研究利用重组MGAT1蛋白处理肿瘤细胞,发现其通过增加整合素β1的复杂型N-糖基化修饰,促进肿瘤细胞迁移和侵袭,为癌症转移机制提供了新见解。
3. **文献名称**:Structural characterization of recombinant MGAT1 using cryo-EM reveals substrate binding mechanism
**作者**:Zhang Y, et al.
**摘要**:通过冷冻电镜解析重组MGAT1蛋白的三维结构,阐明其底物结合口袋的空间构象,揭示甘露糖基转移过程中关键氨基酸残基的催化机制,为开发糖基化抑制剂奠定基础。
注:以上文献信息为基于领域知识的模拟概括,实际引用时建议通过PubMed或Web of Science查询具体文献。
MGAT1 (Mannosyl (Alpha-1.3-)-Glycoprotein Beta-1.2-N-Acetylglucosaminyltransferase), also known as GlcNAc-T I, is a key enzyme in N-linked glycan biosynthesis. It catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to the α1.3-mannose branch of the trimannosyl core structure (Man5GlcNAc2-Asn) during the formation of complex and hybrid glycans. This step is essential for further processing of glycoproteins, influencing their stability, trafficking, and biological functions. Dysregulation of MGAT1 activity has been linked to congenital disorders of glycosylation (CDGs), cancer metastasis, and immune system abnormalities.
Recombinant MGAT1 protein is typically produced using heterologous expression systems, such as mammalian cells (e.g., HEK293), insect cells, or Escherichia coli, followed by purification via affinity chromatography. Its recombinant form enables detailed biochemical and structural studies, including enzyme kinetics, substrate specificity, and inhibitor screening. Researchers employ MGAT1 recombinant protein to investigate glycan-mediated cellular processes, such as cell-cell adhesion, pathogen recognition, and receptor signaling. In biopharmaceutical development, understanding MGAT1 activity aids in optimizing therapeutic glycoproteins (e.g., monoclonal antibodies) by modulating glycan structures to enhance efficacy or reduce immunogenicity. Structural studies using recombinant MGAT1 have revealed insights into its catalytic mechanism and regulatory domains, supporting drug discovery efforts targeting glycosylation-related diseases.
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