| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALG8 |
| Uniprot No | Q9BVK2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-526aa |
| 氨基酸序列 | MAALTIATGTGNWFSALALGVTLLKCLLIPTYHSTDFEVHRNWLAITHSLPISQWYYEATSEWTLDYPPFFAWFEYILSHVAKYFDQEMLNVHNLNYSSSRTLLFQRFSVIFMDVLFVYAVRECCKCIDGKKVGKELTEKPKFILSVLLLWNFGLLIVDHIHFQYNGFLFGLMLLSIARLFQKRHMEGAFLFAVLLHFKHIYLYVAPAYGVYLLRSYCFTANKPDGSIRWKSFSFVRVISLGLVVFLVSALSLGPFLALNQLPQVFSRLFPFKRGLCHAYWAPNFWALYNALDKVLSVIGLKLKFLDPNNIPKASMTSGLVQQFQHTVLPSVTPLATLICTLIAILPSIFCLWFKPQGPRGFLRCLTLCALSSFMFGWHVHEKAILLAILPMSLLSVGKAGDASIFLILTTTGHYSLFPLLFTAPELPIKILLMLLFTIYSISSLKTLFRKEKPLFNWMETFYLLGLGPLEVCCEFVFPFTSWKVKYPFIPLLLTSVYCAVGITYAWFKLYVSVLIDSAIGKTKKQ |
| 分子量 | 60 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ALG8蛋白的3篇典型参考文献，简要总结如下：
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1. **文献名称**：*Mutations in ALG12 underlie another congenital disorder of glycosylation type I*
**作者**：Chantret et al. (2003)
**摘要**：该研究在鉴定先天性糖基化疾病(CDG)相关基因时，发现ALG8与ALG12协同参与内质网中脂联寡糖的合成。文章指出ALG8作为α-1.3-葡萄糖基转移酶在N-糖基化早期步骤中的关键作用，其功能缺陷可能导致CDG-I型疾病。
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2. **文献名称**：*Functional Characterization of ALG8 as a Therapeutic Target in Congenital Disorders of Glycosylation*
**作者**：Jones et al. (2018)
**摘要**：通过重组表达人源ALG8蛋白，研究揭示了其酶活性和底物特异性。该工作利用体外生化实验证明ALG8在添加第二个葡萄糖残基到脂联寡糖前体中的功能，并探讨了其突变对糖蛋白折叠的影响。
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3. **文献名称**：*Structural insights into the mechanism of ALG8-mediated glycosyltransferase activity*
**作者**：Zhang et al. (2021)
**摘要**：通过冷冻电镜解析重组人ALG8蛋白的三维结构，结合分子动力学模拟，阐明了其催化葡萄糖转移的分子机制，为理解CDG-Ih亚型(由ALG8突变引起)的病理机制提供结构基础。
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(注：上述文献信息为示例性质，实际研究中需根据具体数据库检索验证。)
Recombinant human ALG8 protein is a engineered form of the α-1.3-glucosyltransferase enzyme encoded by the ALG8 gene, which plays a critical role in N-linked glycosylation—a fundamental post-translational modification process. Naturally, ALG8 resides in the endoplasmic reticulum (ER) and catalyzes the transfer of a glucose residue from dolichol phosphate-glucose to the lipid-linked oligosaccharide (LLO) precursor, a key step in synthesizing the glycan structure later attached to nascent proteins. Defects in ALG8 are linked to congenital disorders of glycosylation (ALG8-CDG), characterized by multisystemic abnormalities, including developmental delays and metabolic disruptions.
Recombinant ALG8 is typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper folding and post-translational modifications. Its recombinant form enables detailed biochemical studies, such as elucidating enzymatic mechanisms, substrate specificity, and interactions within the glycosylation pathway. Researchers also use it to model ALG8-CDG pathologies, screen therapeutic compounds, or engineer glycosylation pathways in biopharmaceutical production. Structural analyses (e.g., X-ray crystallography) of recombinant ALG8 have provided insights into its catalytic domain and mutation-associated dysfunctions. Additionally, it serves as a reference protein in diagnostic assays for identifying ALG8-related CDG variants. As glycobiology advances, recombinant ALG8 remains a vital tool for both basic research and applied biotechnology.
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