| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GNPNAT1 |
| Uniprot No | Q96EK6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMKPDETPMFDPSLLKEVDWSQNTATFS PAISPTHPGEGLVLRPLCTADLNRGFFKVLGQLTETGVVSPEQFMKSFEH MKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDE CRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENY MCRRFLK |
| 预测分子量 | 23 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GNPNAT1重组蛋白的模拟参考文献示例(信息为虚构概括，实际文献需通过学术数据库验证)：
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1. **标题**: *"Cloning and Functional Characterization of Recombinant GNPNAT1 in Saccharomyces cerevisiae"*
**作者**: Smith A, et al.
**摘要**: 研究报道了通过酵母表达系统成功克隆并纯化GNPNAT1重组蛋白，证实其催化UDP-GlcNAc向磷酸多萜醇转移的活性，为糖基化途径研究提供工具。
2. **标题**: *"Structural Insights into GNPNAT1 Catalytic Mechanism via X-ray Crystallography"*
**作者**: Lee B, et al.
**摘要**: 通过X射线晶体学解析GNPNAT1重组蛋白的三维结构，揭示其底物结合位点及关键氨基酸残基，阐明其N-乙酰葡萄糖胺转移的分子机制。
3. **标题**: *"GNPNAT1 Deficiency in Congenital Disorders of Glycosylation: Recombinant Protein Rescue Studies"*
**作者**: Garcia C, et al.
**摘要**: 利用重组GNPNAT1蛋白修复患者细胞模型中的糖基化缺陷，证明该酶在先天性糖基化疾病(CDG)中的关键作用，提示潜在治疗策略。
4. **标题**: *"High-throughput Screening of GNPNAT1 Inhibitors Using Recombinant Enzyme Assays"*
**作者**: Patel R, et al.
**摘要**: 开发基于重组GNPNAT1的高通量筛选平台，鉴定出小分子抑制剂，为调控异常糖基化相关疾病(如癌症)提供候选化合物。
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**注意**：以上内容为模拟生成，实际文献需通过PubMed、Google Scholar等平台检索。建议结合关键词“GNPNAT1”、“recombinant protein”、“GlcNAc-1-P transferase”进一步查找。
**Background of GNPNAT1 Recombinant Protein**
Glucosamine-phosphate N-acetyltransferase 1 (GNPNAT1) is a key enzyme in hexosamine biosynthesis, catalyzing the acetylation of glucosamine-6-phosphate (GlcN-6-P) to form N-acetylglucosamine-6-phosphate (GlcNAc-6-P). This reaction is a critical step in the production of UDP-N-acetylglucosamine (UDP-GlcNAc), an essential substrate for protein glycosylation, lipid modification, and nucleotide sugar metabolism. GNPNAT1 is localized in the cytoplasm and is ubiquitously expressed across tissues, reflecting its fundamental role in cellular processes linked to nutrient sensing, signaling, and post-translational modifications. Dysregulation of GNPNAT1 activity has been implicated in metabolic disorders, cancer progression, and neurodegenerative diseases, underscoring its biological and clinical relevance.
Recombinant GNPNAT1 protein is engineered for in vitro studies to explore its enzymatic mechanisms, structure-function relationships, and interactions with inhibitors or modulators. Produced using heterologous expression systems (e.g., *E. coli* or mammalian cells), the recombinant protein is typically purified via affinity tags to ensure high specificity and activity. Its applications span biochemical assays, high-throughput drug screening, and structural biology (e.g., crystallography or cryo-EM) to elucidate catalytic sites or design targeted therapies. Research on GNPNAT1 also intersects with studies on insulin resistance and hyperglycemia, as UDP-GlcNAc levels influence O-GlcNAcylation—a nutrient-sensitive regulatory modification linked to diabetes. Furthermore, its role in cancer cell survival and metastasis highlights potential as a therapeutic target. By enabling precise analysis of GNPNAT1. recombinant protein tools advance understanding of glycosylation-related pathways and their disease connections.
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