| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALG9 |
| Uniprot No | Q9H6U8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-618aa |
| 氨基酸序列 | MASRGARQRLKGSGASSGDTAPAADKLRELLGSREAGGAEHRTELSGNKAGQVWAPEGSTAFKCLLSARLCAALLSNISDCDETFNYWEPTHYLIYGEGFQTWEYSPAYAIRSYAYLLLHAWPAAFHARILQTNKILVFYFLRCLLAFVSCICELYFYKAVCKKFGLHVSRMMLAFLVLSTGMFCSSSAFLPSSFCMYTTLIAMTGWYMDKTSIAVLGVAAGAILGWPFSAALGLPIAFDLLVMKHRWKSFFHWSLMALILFLVPVVVIDSYYYGKLVIAPLNIVLYNIFTPHGPDLYGTEPWYFYLINGFLNFNVAFALALLVLPLTSLMEYLLQRFHVQNLGHPYWLTLAPMYIWFIIFFIQPHKEERFLFPVYPLICLCGAVALSALQHSFLYFQKCYHFVFQRYRLEHYTVTSNWLALGTVFLFGLLSFSRSVALFRGYHGPLDLYPEFYRIATDPTIHTVPEGRPVNVCVGKEWYRFPSSFLLPDNWQLQFIPSEFRGQLPKPFAEGPLATRIVPTDMNDQNLEEPSRYIDISKCHYLVDLDTMRETPREPKYSSNKEEWISLAYRPFLDASRSSKLLRAFYVPFLSDQYTVYVNYTILKPRKAKQIRKKSGG |
| 分子量 | 97.2 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α-1.2-甘露糖基转移酶ALG9的3篇参考文献(示例基于领域典型研究，实际文献需根据具体数据库查询)：
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1. **文献名称**：*ALG9 甘露糖基转移酶的结构与功能分析揭示其在先天性糖基化疾病中的作用*
**作者**：Thiel C, et al.
**摘要**：研究通过重组表达人源ALG9蛋白，解析其催化机制及底物特异性，发现ALG9突变导致甘露糖添加异常，与先天性糖基化病(CDG-IL)直接相关。
2. **文献名称**：*重组ALG9酶活性的体外重建及其在酵母模型中的功能互补*
**作者**：Grubenmann S, et al.
**摘要**：利用重组ALG9蛋白在酵母突变体中恢复N-糖基化缺陷，证明其在内质网中催化早期甘露糖链延伸的关键作用。
3. **文献名称**：*ALG9蛋白的晶体结构揭示其底物结合域特征*
**作者**：Mohorko E, et al.
**摘要**：通过X射线衍射解析重组ALG9的晶体结构，发现其特有的α-螺旋结构域参与底物识别，为开发小分子调控剂提供理论依据。
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*注：以上为模拟示例，实际文献需通过PubMed、Web of Science等数据库以关键词“ALG9”、“mannosyltransferase”、“recombinant”检索确认。*
Recombinant human α-1.2-mannosyltransferase ALG9 is a key enzyme involved in N-linked glycosylation, a critical post-translational modification process in eukaryotic cells. ALG9 catalyzes the transfer of mannose residues from dolichol-phosphate-mannose to lipid-linked oligosaccharide (LLO) precursors during the assembly of the glycan core in the endoplasmic reticulum (ER). Specifically, it mediates the addition of the seventh and ninth mannose moieties in a stepwise manner, contributing to the formation of the Man₉GlcNAc₂-PP-Dol structure. This process is essential for proper protein folding, quality control, and cellular secretion.
Mutations in the ALG9 gene are linked to congenital disorders of glycosylation (ALG9-CDG), characterized by developmental delays, neurological abnormalities, and multi-systemic defects. Recombinant ALG9 is produced using heterologous expression systems (e.g., mammalian or insect cells) to study its enzymatic activity, structure, and role in disease mechanisms. Its recombinant form enables in vitro reconstitution of glycosylation pathways, advancing research on ER-associated processes and therapeutic strategies for CDG. Studies also explore its interactions with other glycosyltransferases (e.g., ALG12) and chaperones, shedding light on LLO biosynthesis regulation. ALG9’s conserved function across eukaryotes underscores its evolutionary importance in maintaining proteostasis.
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