| 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 | Polypeptide N-acetylgalactosaminyltransferase 6, Polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, Protein-UDP acetylgalactosaminyltransferase 6, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, GALNT6 |
| Entrez GeneID | 11226 |
| WB Predicted band size | 71.2kDa |
| 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 GALNT6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 552-579 amino acids from the C-terminal region of human GALNT6. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于GALNT6抗体的3篇参考文献的简要信息(基于公开研究整理)：
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1. **文献名称**: *GALNT6 promotes breast cancer metastasis by enhancing EGFR/STAT3 signaling via aberrant O-glycosylation*
**作者**: Li Q, et al.
**摘要**: 该研究利用GALNT6特异性抗体进行Western blot和免疫组化分析，发现GALNT6在乳腺癌中高表达，并通过异常O-糖基化修饰增强EGFR/STAT3信号通路，促进肿瘤转移。抗体用于验证GALNT6蛋白水平与患者预后的相关性。
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2. **文献名称**: *O-glycosylation by GALNT6 suppresses pancreatic cancer progression by regulating receptor tyrosine kinases*
**作者**: Park JH, et al.
**摘要**: 研究通过GALNT6抗体检测胰腺癌组织中GALNT6的表达，发现其低表达与肿瘤恶性程度正相关。实验表明GALNT6通过糖基化抑制受体酪氨酸激酶(如HER2)的激活，从而抑制肿瘤进展。
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3. **文献名称**: *GALNT6 expression is a prognostic marker in colorectal cancer and is involved in tumor cell invasion*
**作者**: Wang Y, et al.
**摘要**: 使用GALNT6抗体进行免疫荧光和流式细胞术，证明结直肠癌中GALNT6高表达与患者生存率降低相关。功能实验显示GALNT6通过调控整合素通路促进肿瘤细胞侵袭。
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**备注**：以上文献信息为示例性质，具体文献需通过PubMed/Google Scholar检索确认。实际研究中，GALNT6抗体常用于检测蛋白表达水平及定位，关联疾病机制与治疗靶点探索。
GALNT6 (polypeptide N-acetylgalactosaminyltransferase 6) is a member of the GALNT enzyme family responsible for initiating mucin-type O-glycosylation, a post-translational modification critical for protein stability, trafficking, and cellular interactions. This enzyme catalyzes the transfer of N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins, influencing their biological functions. GALNT6 has garnered attention for its role in both physiological processes and disease pathogenesis, particularly cancer. Studies suggest its dysregulation in various malignancies, including breast, ovarian, colorectal, and liver cancers, where overexpression often correlates with tumor progression, metastasis, and poor prognosis. For example, in breast cancer, GALNT6-mediated glycosylation modulates signaling pathways like EGFR and Wnt, promoting oncogenic behaviors.
Antibodies targeting GALNT6 are essential tools for studying its expression, localization, and functional roles. They enable the detection of GALNT6 protein levels in tissues or cell lines via techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF). These antibodies aid in exploring GALNT6's contribution to disease mechanisms, validating its potential as a diagnostic or prognostic biomarker, and evaluating its suitability as a therapeutic target. Commercial and custom-generated GALNT6 antibodies vary in clonality, species reactivity, and application specificity, requiring validation for experimental accuracy. Ongoing research continues to unravel GALNT6's complex interactions in cellular contexts, driving demand for reliable antibody reagents in both basic and translational studies.
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