| 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 | Single-strand selective monofunctional uracil DNA glycosylase, 322-, SMUG1 |
| Entrez GeneID | 23583 |
| WB Predicted band size | 29.9kDa |
| 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 SMUG1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 43-71 amino acids from the N-terminal region of human SMUG1. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于SMUG1 (N-term)抗体的3篇参考文献及其摘要内容的简要总结：
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1. **文献名称**: *"Human SMUG1 DNA glycosylase: Key player in repair of oxidative DNA damage"*
**作者**: Kavli, B., et al.
**摘要**: 本研究揭示了SMUG1在修复氧化性DNA损伤(如5-羟甲基尿嘧啶)中的核心作用，通过Western blot和免疫荧光技术，利用N端特异性抗体证实了SMUG1在细胞核内的定位及其在碱基切除修复(BER)通路中的功能。
2. **文献名称**: *"Substrate specificity of human SMUG1 in vitro and its interaction with DNA repair proteins"*
**作者**: Hagen, L., et al.
**摘要**: 文章通过免疫沉淀和蛋白质相互作用分析，使用抗SMUG1 N端抗体验证了SMUG1与AP内切酶(APE1)等修复因子的结合，阐明其底物选择性和修复机制协同性，为理解BER通路提供实验依据。
3. **文献名称**: *"SMUG1 expression and prognostic value in colorectal cancer"*
**作者**: An, Q., et al.
**摘要**: 利用抗SMUG1 N端抗体进行免疫组化分析，发现SMUG1在结直肠癌组织中表达显著下调，且低表达与患者不良预后相关，提示其可能作为DNA修复缺陷型癌症的潜在生物标志物。
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**备注**：上述文献为示例性内容，实际文献需通过PubMed或Google Scholar以关键词“SMUG1 antibody N-term”或“SMUG1 N-terminal epitope”检索获取。部分抗体厂商(如Abcam、CST)的产品说明书也可能引用相关研究，可结合具体需求参考。
The SMUG1 (N-term) antibody targets the N-terminal region of SMUG1 (Single-strand-selective Monofunctional Uracil-DNA Glycosylase 1), a DNA repair enzyme involved in base excision repair (BER). SMUG1 primarily excises uracil residues from DNA, including deaminated cytosine (forming uracil) and oxidized 5-hydroxymethyluracil, playing a critical role in maintaining genomic stability. Unlike other uracil-DNA glycosylases (e.g., UNG), SMUG1 exhibits specificity for single-stranded DNA and is cell cycle-independent, suggesting unique regulatory roles.
The N-terminal domain of SMUG1 is essential for its enzymatic activity and interaction with other DNA repair proteins. Antibodies targeting this region are widely used to study SMUG1 expression, localization, and function in cellular contexts, including cancer, neurodegeneration, and aging. They are applied in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to assess protein levels or post-translational modifications linked to disease mechanisms.
Research using SMUG1 (N-term) antibodies has highlighted its dual roles in tumor suppression (preventing mutagenesis) and potential oncogenic activity (via aberrant repair). Dysregulation of SMUG1 is implicated in chemotherapy resistance and neurological disorders, underscoring its therapeutic relevance. These antibodies serve as vital tools for elucidating SMUG1's complex biology and its interplay with other DNA damage response pathways.
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