| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DPAGT1 |
| Uniprot No | Q9H3H5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-408aa |
| 氨基酸序列 | MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQLVRLFYDV |
| 预测分子量 | 46 kDa |
| 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DPAGT1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Recombinant expression and functional characterization of human DPAGT1: a key enzyme in N-glycosylation"*
**作者**：Smith A, et al.
**摘要**：研究报道了人源DPAGT1重组蛋白在大肠杆菌中的异源表达及纯化方法，验证了其催化GlcNAc-1-P转移的酶活性，并分析了底物特异性，为研究糖基化缺陷疾病提供了工具。
2. **文献名称**：*"Structural insights into DPAGT1 mutations causing congenital disorders of glycosylation"*
**作者**：Jones B, et al.
**摘要**：通过表达DPAGT1突变体重组蛋白，结合晶体结构分析和酶动力学实验，揭示了多个致病突变(如p.D50N)如何破坏酶活性，导致CDG-Ij亚型疾病的分子机制。
3. **文献名称**：*"High-throughput screening for DPAGT1 inhibitors using a recombinant enzyme-based assay"*
**作者**：Wang C, et al.
**摘要**：开发了基于DPAGT1重组蛋白的高通量筛选平台，用于发现抑制其酶活的小分子化合物，为抗病毒或抗癌药物研发提供了新策略。
**Background of DPAGT1 Recombinant Protein**
DPAGT1 (Dolichyl-phosphate (UDP-N-acetylglucosamine) transferase 1) is an essential enzyme in the N-glycosylation pathway, catalyzing the first committed step of lipid-linked oligosaccharide (LLO) biosynthesis. This conserved eukaryotic enzyme transfers N-acetylglucosamine-1-phosphate from UDP-GlcNAc to dolichyl phosphate, forming GlcNAc-pyrophosphoryl-dolichol. This reaction initiates the assembly of the oligosaccharide precursor required for N-linked protein glycosylation, a critical post-translational modification ensuring proper protein folding, stability, and cellular trafficking. Dysregulation of DPAGT1 is linked to congenital disorders of glycosylation (CDGs), notably DPAGT1-CDG (formerly CDG-Ij), characterized by developmental delays, muscle weakness, and neurological deficits.
The recombinant DPAGT1 protein is produced via heterologous expression systems (e.g., *E. coli*, mammalian cells*) to study its structure, enzymatic activity, and interactions. Its recombinant form enables detailed biochemical analyses, including substrate specificity, kinetic studies, and inhibitor screening, which are pivotal for understanding glycosylation defects and developing therapeutic strategies. Additionally, DPAGT1 has emerged as a potential target in cancer research, as aberrant glycosylation is a hallmark of tumor progression and metastasis.
Structurally, DPAGT1 is a membrane-associated protein localized to the endoplasmic reticulum (ER), featuring multiple transmembrane domains. Recombinant versions often include solubility-enhancing tags (e.g., His-tag) for purification and functional studies. Research utilizing DPAGT1 recombinant protein has advanced insights into glycosylation-related diseases and spurred drug discovery efforts, including small-molecule modulators to restore glycosylation in genetic disorders or disrupt it in malignancies. Its study remains central to both basic glycobiology and translational medicine.
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