| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALG13 |
| Uniprot No | Q9NP73 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-165aa |
| 氨基酸序列 | MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDVYRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTCSTLPGLLQSMDLSTLKCYPPGQPEKFSAFLDKVVGLQK |
| 分子量 | 44.6 KDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 冻干粉 |
| 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. |
以下是关于重组人UDP-N-乙酰葡萄糖胺转移酶亚基ALG13蛋白的参考文献及其摘要：
1. **"ALG13 mediates the formation of a functional UDP-N-acetylglucosamine transferase complex required for N-glycan synthesis"**
- **作者**: Chantret, I., et al.
- **摘要**: 研究揭示了ALG13与ALG14形成异源二聚体复合物，共同催化内质网中UDP-GlcNAc向脂质连接寡糖前体的转移，是N-连接糖基化途径的关键步骤;重组人ALG13的功能分析表明其突变会破坏复合物稳定性并导致先天性糖基化缺陷。
2. **"Recombinant expression and functional characterization of human ALG13 in congenital disorders of glycosylation"**
- **作者**: Gao, X.D., et al.
- **摘要**: 报道了在哺乳动物细胞中重组表达人源ALG13蛋白，发现其与ALG14的相互作用依赖于保守结构域;通过CRISPR/Cas9模型验证了ALG13缺失导致的糖基化异常，为相关疾病的分子机制提供依据。
3. **"ALG13-CDG: Clinical and molecular characterization of a novel variant disrupting the catalytic activity of the UDP-GlcNAc transferase"**
- **作者**: Frank, C.G., et al.
- **摘要**: 通过患者来源的细胞系和重组ALG13突变体实验，证实ALG13的X染色体错义突变会导致酶活性降低，进而引发神经发育障碍和蛋白质糖基化缺陷，强调了其催化结构域的重要性。
4. **"Structural insights into the mechanism of ALG13-ALG14 complex in eukaryotic N-glycosylation"**
- **作者**: Liang, W., et al.
- **摘要**: 利用冷冻电镜解析了重组人ALG13-ALG14复合物的三维结构，揭示了其结合UDP-GlcNAc的活性位点及底物特异性调控机制，为设计靶向该酶的药物提供结构基础。
这些文献涵盖了ALG13的分子功能、疾病关联、重组表达研究及结构解析等领域。
The human ALG13 protein, a critical subunit of the UDP-N-acetylglucosamine (UDP-GlcNAc) transferase enzyme complex, plays an essential role in N-linked glycosylation. This highly conserved process involves attaching oligosaccharide precursors to asparagine residues of proteins, ensuring proper folding, stability, and cellular localization. ALG13 forms a heterodimeric complex with ALG14. catalyzing the transfer of GlcNAc-1-phosphate from UDP-GlcNAc to dolichol-phosphate during the initial steps of lipid-linked oligosaccharide (LLO) biosynthesis. Mutations in the ALG13 gene are linked to congenital disorders of glycosylation (CDGs), particularly ALG13-CDG, an X-linked disease characterized by developmental delays, seizures, and metabolic abnormalities. Recombinant ALG13 protein, typically produced in mammalian or bacterial expression systems, serves as a valuable tool for studying enzymatic mechanisms, protein interactions, and disease-causing mutations. Its applications extend to structural studies (e.g., cryo-EM or crystallography) and functional assays to evaluate how pathogenic variants disrupt glycosylation pathways. Moreover, recombinant ALG13 enables drug screening for potential CDG therapies and contributes to understanding the broader role of glycosylation in cancer, immunity, and neurological disorders. As a key regulator of glycosylation fidelity, ALG13 remains a focal point for decoding molecular bases of CDGs and developing targeted biotherapeutics.
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