| WB | 1/1000 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3, C2GnT-mucin type, C2GnT-M, hC2GnT-M, Core 2/core 4 beta-1,6-N-acetylglucosaminyltransferase, C2/4GnT, GCNT3 |
| Entrez GeneID | 9245 |
| WB Predicted band size | 50.9kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human |
| Immunogen | This GCNT3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 73-102 amino acids from the N-terminal region of human GCNT3. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于GCNT3 (N-term)抗体的3篇示例文献(内容为模拟概括，非真实文献)：
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1. **文献名称**: "GCNT3-mediated O-glycosylation promotes tumor progression in colorectal cancer"
**作者**: Li X, et al.
**摘要**: 本研究利用GCNT3 (N-term)特异性抗体，通过免疫组化和Western blot分析，发现GCNT3在结肠癌组织中高表达，并通过调控粘蛋白O-糖基化促进肿瘤转移。抗体验证实验显示其特异性识别N端表位，为后续功能研究提供工具。
2. **文献名称**: "Characterization of GCNT3 expression and its role in gastric cancer stem cells"
**作者**: Wang Y, et al.
**摘要**: 文章通过GCNT3 (N-term)抗体检测胃癌干细胞中GCNT3的蛋白表达，发现其通过调节CD44糖基化增强肿瘤干性。抗体特异性通过siRNA敲低实验验证，证实其在流式细胞术和免疫荧光中的可靠性。
3. **文献名称**: "Development and validation of a novel anti-GCNT3 antibody for studying glycosylation in pancreatic cancer"
**作者**: Chen H, et al.
**摘要**: 研究团队开发并验证了一种针对GCNT3 N端的多克隆抗体，通过肽段竞争实验和质谱分析证明其特异性。该抗体成功应用于胰腺癌组织芯片，揭示GCNT3与患者不良预后的相关性。
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注：以上文献为示例，实际引用需检索PubMed或Google Scholar等数据库获取真实文献。如需进一步协助定位具体论文，可提供更详细的研究背景。
The GCNT3 (N-term) antibody is a research tool designed to target the N-terminal region of the GCNT3 protein, a member of the glucosaminyl (N-acetyl) transferase family. GCNT3. also known as core 2 β-1.6-N-acetylglucosaminyltransferase, plays a critical role in O-glycan biosynthesis by catalyzing the formation of branched core 2 and core 4 structures in mucin-type glycoproteins. These glycans are essential for cell-cell interactions, immune responses, and epithelial barrier function. Dysregulation of GCNT3 has been implicated in diseases such as cancer, inflammatory disorders, and immune deficiencies, with studies highlighting its overexpression in gastrointestinal cancers and potential links to metastasis and drug resistance.
The antibody is commonly used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to study GCNT3 expression, localization, and function in biological samples. By targeting the N-terminal domain, it helps researchers investigate post-translational modifications, protein-protein interactions, or regulatory mechanisms affecting GCNT3 activity. Validated for specificity, the antibody aids in exploring how altered glycosylation patterns driven by GCNT3 contribute to disease pathogenesis, offering insights for therapeutic targeting. Its applications extend to both basic research and preclinical studies, particularly in models of cancer and mucosal inflammation.
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