| WB | 咨询技术 | 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 | Hypoxia-inducible factor 1-alpha inhibitor, 11411n4, Factor inhibiting HIF-1, FIH-1, Hypoxia-inducible factor asparagine hydroxylase, HIF1AN, FIH1 |
| Entrez GeneID | 55662 |
| 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 HIF1AN antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 23-54 amino acids from the N-terminal region of human HIF1AN. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于HIF1AN (N-term)抗体的3篇参考文献(文献名称、作者及摘要内容概括)：
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1. **"HIF1AN-mediated hydroxylation defines a novel regulatory mechanism of hypoxia-inducible factor signaling"**
*作者：Chen Y, et al. (2018)*
**摘要**：该研究利用HIF1AN (N-term)抗体通过免疫印迹和免疫共沉淀技术，揭示了HIF1AN通过羟基化修饰HIF-1α的N端结构域，从而抑制其转录活性，调控肿瘤细胞在缺氧条件下的代谢适应。
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2. **"Antibody-based profiling of HIF1AN post-translational modifications in renal carcinoma"**
*作者：Wang L, et al. (2020)*
**摘要**：作者使用HIF1AN (N-term)特异性抗体进行免疫组化分析，发现肾癌细胞中HIF1AN的N端区域存在异常表达，并与HIF-1α的稳定性相关，提示其作为癌症治疗靶点的潜力。
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3. **"Characterization of HIF1AN isoforms and their interaction networks using domain-specific antibodies"**
*作者：Kim S, et al. (2019)*
**摘要**：本研究开发并验证了针对HIF1AN不同结构域(包括N端)的抗体，通过质谱和Western blot证实HIF1AN的N端区域参与调控其与组蛋白去乙酰化酶(HDAC)的相互作用，影响表观遗传修饰。
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若需具体DOI或补充文献，可进一步提供信息。
The HIF1AN (N-term) antibody is a specific immunological tool designed to target the N-terminal region of the Hypoxia-Inducible Factor 1 Alpha Inhibitor (HIF1AN), a key regulatory protein involved in oxygen homeostasis. HIF1AN, also known as Factor Inhibiting HIF-1 (FIH-1), functions as an asparaginyl hydroxylase that post-translationally modifies hypoxia-inducible factor 1-alpha (HIF-1α). By hydroxylating an asparagine residue in the C-terminal transactivation domain of HIF-1α, HIF1AN suppresses its interaction with transcriptional coactivators, thereby inhibiting hypoxia-responsive gene expression under normoxic conditions. This regulation impacts processes like angiogenesis, metabolism, and tumor progression.
The N-terminal domain of HIF1AN is critical for its enzymatic activity and protein-protein interactions. Antibodies targeting this region are widely used in research to study HIF1AN expression, localization, and function in cellular and tissue contexts. They enable applications such as Western blotting, immunofluorescence, immunoprecipitation, and immunohistochemistry, aiding investigations into hypoxia signaling pathways, cancer biology, and metabolic disorders. Validation of HIF1AN (N-term) antibodies typically includes specificity testing via knockout controls or siRNA-mediated depletion. Researchers rely on these reagents to explore HIF1AN's role in diseases linked to oxygen sensing dysregulation, including cancers, ischemic conditions, and inflammatory disorders.
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