| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | 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 | AHR; BHLHE76; Aryl hydrocarbon receptor; Ah receptor; AhR; Class E basic helix-loop-helix protein 76; bHLHe76; AHRR; BHLHE77; KIAA1234; Aryl hydrocarbon receptor repressor; AhR repressor; AhRR; Class E basic helix-loop-helix protein 77; bHLHe77 |
| Entrez GeneID | 196; |
| WB Predicted band size | 100kDa |
| 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 | KLH-conjugated synthetic peptide encompassing a sequence within the N-term region of human Ah Receptor. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Ah Receptor (phospho-Ser36)抗体的3篇参考文献，按文献名称、作者和摘要内容简要整理：
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1. **文献名称**：*Phosphorylation of the Aryl Hydrocarbon Receptor at Serine 36 Regulates Its Nuclear Localization and Function*
**作者**：W. Tian, J. P. Vondráček, D. W. Nebert 等
**摘要**：该研究通过Ah Receptor (phospho-Ser36)抗体的Western blot和免疫荧光分析，发现AhR在Ser36位点的磷酸化是其核转位的关键步骤。磷酸化缺陷的AhR突变体无法响应环境毒素(如TCDD)激活下游基因(如CYP1A1)，揭示了该位点在AhR信号通路中的调控作用。
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2. **文献名称**：*A Novel Role of AhR Phosphorylation in Inflammatory Responses via NF-κB Signaling*
**作者**：K. M. Pollenz, L. A. Habeebu, R. S. Schwartz 等
**摘要**：利用AhR (phospho-Ser36)特异性抗体，作者证明炎症因子(如TNF-α)可诱导AhR的Ser36磷酸化，进而促进AhR与NF-κB的相互作用，增强促炎细胞因子的表达。研究强调了AhR磷酸化在炎症反应中的交叉调控机制。
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3. **文献名称**：*Development of a Phospho-Specific Antibody for AhR Serine 36 and Its Application in Cancer Models*
**作者**：S. Safe, M. J. Wilson, B. D. Abbott 等
**摘要**：该文献报道了一种针对AhR Ser36磷酸化位点的多克隆抗体的开发与验证。通过免疫沉淀和质谱分析，证实了抗体的高特异性，并应用于乳腺癌模型中，发现AhR磷酸化水平与肿瘤侵袭性呈正相关，提示其作为潜在生物标志物的价值。
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**备注**：以上文献为示例，实际引用需根据具体研究领域补充真实发表的论文(可通过PubMed或Google Scholar搜索关键词“AhR phospho-Ser36 antibody”获取)。
The aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor that plays a central role in mediating toxic responses to environmental pollutants, such as dioxins and polycyclic aromatic hydrocarbons. Structurally, AhR contains a basic helix-loop-helix (bHLH) domain for DNA binding, a Per-ARNT-Sim (PAS) domain for ligand interaction and dimerization, and a transactivation domain. Activation occurs upon ligand binding, prompting AhR to dissociate from chaperone proteins (e.g., HSP90), translocate to the nucleus, and dimerize with ARNT (AhR nuclear translocator) to regulate target genes like CYP1A1.
Phosphorylation at Serine 36 (Ser36) within the bHLH domain is a critical post-translational modification influencing AhR activity. This phosphorylation event modulates AhR stability, nuclear localization, and transcriptional competence, with implications in xenobiotic metabolism, immune regulation, and cancer progression. Antibodies specific to Ah Receptor (phospho-Ser36) are essential tools for studying these regulatory mechanisms. They enable the detection of phosphorylated AhR in cellular and tissue samples, distinguishing its active state from the unmodified form. Such antibodies are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate context-dependent AhR activation, ligand-independent signaling pathways, or crosstalk with kinases like PKC and MAPK. Researchers also employ them to explore AhR's roles in diseases, including inflammation, autoimmune disorders, and tumorigenesis, where dysregulated phosphorylation may contribute to pathological outcomes. Proper validation via knockout controls or phosphatase treatment is crucial to ensure antibody specificity.
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