| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | IHC:1/100-1/200;IHF:1/50-1/200 | Human,Mouse,Rat |
| ICC | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 1/20-1/100 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | HRNT1; O-GLCNAC;;OGT |
| WB Predicted band size | Calculated MW: 117 kDa ; Observed MW: 110 kDa |
| 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,Mouse,Rat |
| Immunogen | A synthesized peptide derived from human OGT |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.05% BSA and 50% glycerol. |
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以下是关于OGT抗体的3篇文献示例，涵盖不同研究方向，供参考：
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**1. 文献名称**：*O-GlcNAc Transferase (OGT) Regulates Proteasome Function via Site-Specific Ubiquitination*
**作者**：Wang, Z., et al. (2020)
**摘要**：该研究利用OGT特异性抗体，通过免疫共沉淀(Co-IP)和Western blot技术，揭示了OGT通过调控蛋白酶体亚基的O-GlcNAc修饰影响其功能。研究发现，抑制OGT活性会降低细胞中泛素化蛋白的降解效率，提示OGT在蛋白质稳态中的关键作用。
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**2. 文献名称**：*Tissue-Specific OGT Knockout Mice Reveal Neuronal Insulin Resistance and Cognitive Impairment*
**作者**：Liu, Y., et al. (2019)
**摘要**：研究利用OGT抗体进行脑组织免疫组化分析，发现神经元特异性OGT敲除小鼠出现胰岛素信号通路异常及认知功能下降。结果强调了OGT介导的糖基化在神经代谢疾病中的潜在机制。
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**3. 文献名称**：*Development of a High-Affinity Monoclonal Antibody for OGT Detection in Cancer Biomarker Screening*
**作者**：Chen, H., et al. (2021)
**摘要**：该团队开发了一种新型OGT单克隆抗体，具有高特异性和敏感性，适用于ELISA和免疫荧光。通过对比多种癌症组织样本，发现OGT表达水平与肿瘤侵袭性呈正相关，为癌症诊断提供了新工具。
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**注**：以上文献信息为模拟示例，实际引用时建议通过PubMed或专业数据库核对原文。如需具体文献，可提供研究方向(如疾病模型、技术开发等)，将补充更精准的参考文献。
O-GlcNAc transferase (OGT) is an essential enzyme that catalyzes the addition of O-linked β-N-acetylglucosamine (O-GlcNAc) modifications to serine and threonine residues of target proteins. This post-translational modification, termed O-GlcNAcylation, plays a critical role in regulating cellular processes such as nutrient sensing, transcription, stress response, and epigenetic regulation. As a key mediator of the hexosamine biosynthetic pathway, OGT links metabolic flux to cellular signaling by dynamically modifying nuclear, cytoplasmic, and mitochondrial proteins. Dysregulation of OGT activity or O-GlcNAc cycling has been implicated in metabolic disorders, cancer, neurodegenerative diseases, and cardiovascular conditions.
OGT antibodies are indispensable tools for studying the enzyme's expression, localization, and functional interactions. They enable detection of OGT protein levels via Western blotting, immunohistochemistry, or immunofluorescence, and facilitate research into its substrate specificity and regulatory mechanisms. Due to OGT's structural complexity (including multiple isoforms and a tetratricopeptide repeat domain for protein interactions), generating specific antibodies requires careful validation to avoid cross-reactivity. These antibodies have advanced understanding of OGT's dual roles as a nutrient sensor and epigenetic modulator, particularly its interplay with phosphorylation signaling and involvement in insulin resistance, aging, and chromatin remodeling. Recent studies also explore OGT's potential as a therapeutic target, emphasizing the continued importance of high-quality antibodies in both basic and translational research.
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