| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCNT3 |
| Uniprot No | O95395 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-126aa |
| 氨基酸序列 | KLSFRLKCDSDHLGLESRESQSQYCRNILYNFLKLPAKRSINCSGVTRGDQEAVLQAILNNLEVKKKREPFTDTHYLSLTRDCEHFKAERKFIQFPLSK |
| 分子量 | 36.63 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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3篇与重组人GCNT3蛋白相关研究的参考文献示例(注：文献信息为模拟生成，实际引用请核对真实文献)：
1. **《Functional characterization of recombinant human GCNT3 in gastric cancer progression》**
- 作者：Zhang Y, et al.
- 摘要：研究通过大肠杆菌表达系统成功获得重组人GCNT3蛋白，并发现其β-1.3-葡萄糖氨基转移酶活性促进胃癌细胞表面黏蛋白O-糖基化修饰，增强肿瘤细胞侵袭转移能力。
2. **《Structural analysis of human GCNT3 enzyme reveals key domains for substrate recognition》**
- 作者：Lee S, Kim JH
- 摘要：通过X射线晶体学解析重组GCNT3蛋白结构，鉴定其催化结构域和底物结合位点，为开发靶向GCNT3的糖基化抑制剂提供理论基础。
3. **《GCNT3-mediated glycosylation in inflammatory bowel disease: Insights from recombinant protein models》**
- 作者：Chen L, Wang X, et al.
- 摘要：利用重组GCNT3蛋白模拟肠上皮细胞糖基化过程，发现其通过调控MUC2黏蛋白的O-糖链结构影响肠道菌群黏附，与炎症性肠病的发展相关。
如需查找真实文献，建议在PubMed或SciFinder中以"recombinant human GCNT3"、"GCNT3 glycosyltransferase"为关键词检索，重点关注其参与肿瘤微环境调控、黏蛋白糖基化修饰及免疫逃逸机制的研究。
Recombinant human GCNT3 (glucosaminyl (N-acetyl) transferase 3) is a glycosyltransferase critical for synthesizing core 2 and core 4 branched O-glycans, which are essential post-translational modifications of mucins and other glycoproteins. This enzyme catalyzes the formation of β1.6-GlcNAc branches on N-acetyllactosamine structures, influencing cell-cell adhesion, immune responses, and pathogen interactions. GCNT3 is primarily expressed in intestinal and respiratory epithelial cells, with dysregulation linked to diseases such as inflammatory bowel disease, cancer metastasis, and immune disorders.
Produced via recombinant DNA technology in mammalian or bacterial expression systems, recombinant GCNT3 enables studies on O-glycan biosynthesis and its pathophysiological roles. Its activity is crucial for generating specialized glycoforms involved in leukocyte trafficking (via selectin ligands) and mucosal barrier function. Emerging evidence connects altered GCNT3 expression to chemotherapy resistance in gastrointestinal cancers and defective mucin glycosylation in cystic fibrosis. Researchers utilize recombinant GCNT3 to develop glycan-based biomarkers and explore therapeutic strategies targeting aberrant glycosylation. Its biochemical characterization (optimal pH 7-8. Mn²⁺ dependency) and structural features (type II transmembrane protein with catalytic domain) remain active investigation areas, particularly for designing glycoengineering applications.
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