| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALG5 |
| Uniprot No | Q9Y673 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-324aa |
| 氨基酸序列 | MAPLLLQLAVLGAALAAAALVLISIVAFTTATKMPALHRHEEEKFFLNAKGQKETLPSIWDSPTKQLSVVVPSYNEEKRLPVMMDEALSYLEKRQKRDPAFTYEVIVVDDGSKDQTSKVAFKYCQKYGSDKVRVITLVKNRGKGGAIRMGIFSSRGEKILMADADGATKFPDVEKLEKGLNDLQPWPNQMAIACGSRAHLEKESIAQRSYFRTLLMYGFHFLVWFLCVKGIRDTQCGFKLFTREAASRTFSSLHVERWAFDVELLYIAQFFKIPIAEIAVNWTEIEGSKLVPFWSWLQMGKDLLFIRLRYLTGAWRLEQTRKMN |
| 分子量 | 61.38 KDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人二棕榈酰磷酸葡萄糖基转酶(ALG5)的3篇示例文献摘要：
1. **文献名称**：*Functional Characterization of ALG5 in Yeast Glycosylation*
**作者**：Reiss et al. (1997)
**摘要**：首次在酿酒酵母中鉴定了ALG5基因，证明其编码的二棕榈酰磷酸葡萄糖基转移酶参与内质网中脂联寡糖(LLO)的生物合成，为后续研究真核生物N-糖基化机制奠定基础。
2. **文献名称**：*Structural Insights into ALG5 Catalytic Mechanism*
**作者**：Kämpf et al. (2005)
**摘要**：通过X射线晶体学解析了ALG5的三维结构，揭示了其底物结合位点及催化活性区域，阐明了该酶在将葡萄糖转移至磷酸多萜醇过程中的关键构象变化。
3. **文献名称**：*ALG5 Mutations and Congenital Disorders of Glycosylation*
**作者**：Himmelspach & Freeze (2018)
**摘要**：发现人类ALG5基因的罕见突变可导致先天性糖基化疾病(CDG)，临床表现为神经发育异常，研究通过细胞模型证实突变显著降低酶活性，影响蛋白质糖基化功能。
(注：上述文献为示例，实际引用需核实真实存在的论文信息。)
Recombinant human dolichyl-phosphate β-glucosyltransferase (ALG5) is a key enzyme involved in the early stages of N-linked protein glycosylation, a critical post-translational modification process conserved in eukaryotes. Encoded by the ALG5 gene, this endoplasmic reticulum (ER)-resident membrane protein catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate (Dol-P), generating dolichyl-phosphate glucose (Dol-P-Glc). Dol-P-Glc serves as a lipid-linked carbohydrate donor essential for the assembly of the oligosaccharide precursor Glc3Man9GlcNAc2. which is subsequently transferred to nascent proteins in the ER. Dysregulation of ALG5 activity has been linked to congenital disorders of glycosylation (CDGs), a group of metabolic diseases characterized by impaired protein and lipid glycosylation, often leading to multisystemic developmental and neurological abnormalities. The recombinant form of ALG5 is commonly expressed in heterologous systems (e.g., yeast, mammalian cells) for functional studies, enabling detailed investigation of its enzymatic mechanisms, substrate specificity, and interactions with other glycosyltransferases. Its biochemical characterization has provided insights into ER quality control systems, particularly in glucose-dependent protein folding verification. Additionally, recombinant ALG5 finds applications in biotechnology for synthesizing glycoengineered therapeutic proteins, where precise N-glycan profiles are crucial for drug efficacy and stability. Recent structural studies using recombinant ALG5 have revealed conserved motifs critical for UDP-glucose binding and catalytic activity, offering targets for pharmacological modulation in glycosylation-related pathologies.
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