| 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 | 1/100-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | I kappa-B kinase alpha; I-kappa-B kinase 1; IKK-A; IKK-alpha; IKK1 |
| Entrez GeneID | 1147; |
| WB Predicted band size | 85kDa |
| 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 | Peptide sequence around phosphorylation site of threonine 23 (L-G-T(p)-G-G) derived from Human IKK a. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于IKKα(Phospho-Thr23)抗体的3篇参考文献(注：由于具体文献检索受限，以下内容为模拟示例)：
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1. **文献名称**: *"Phosphorylation of IKKα at Thr23 Contributes to Tumor Necrosis Factor-Induced NF-κB Activation"*
**作者**: Chen L et al.
**摘要**: 本研究通过质谱分析和定点突变技术，发现IKKα在Thr23位点的磷酸化是TNFα信号激活NF-κB的关键步骤。研究使用Phospho-Thr23特异性抗体证实该修饰在炎症反应中的功能，并揭示其与IKK复合物活化的关联。
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2. **文献名称**: *"IKKα Thr23 Phosphorylation Regulates Epidermal Differentiation via Non-Canonical NF-κB Signaling"*
**作者**: Descargues P et al.
**摘要**: 该文献利用Phospho-Thr23抗体在小鼠模型中发现，IKKα的Thr23磷酸化通过非经典NF-κB通路调控表皮细胞分化。实验表明，该位点的磷酸化缺陷会导致皮肤屏障功能异常。
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3. **文献名称**: *"A Novel Role of IKKα Phosphorylation at Thr23 in DNA Damage Response"*
**作者**: Yamamoto M et al.
**摘要**: 研究报道了IKKα在DNA损伤后发生Thr23磷酸化，并通过Phospho-Thr23抗体验证其核内定位变化。该修饰促进ATM激酶介导的修复通路，提示IKKα在基因组稳定性中的新功能。
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**备注**：以上文献为示例，实际引用需通过PubMed、Web of Science等平台以关键词“IKKα Thr23 phosphorylation antibody”检索并核实。部分真实研究可能涉及类似主题(如IKKα的N端磷酸化调控机制)，但需结合具体抗体使用说明确认。
The IKKα (Phospho-Thr23) antibody is a crucial tool for studying the activation and function of IKKα (Inhibitor of κB kinase α), a key component of the IKK complex in the NF-κB signaling pathway. IKKα, along with IKKβ and NEMO (IKKγ), regulates NF-κB transcription factors, which control immune responses, inflammation, and cell survival. Phosphorylation at specific residues, such as Thr23. modulates IKKα activity, subcellular localization, and interactions with other signaling molecules.
Thr23 phosphorylation is implicated in IKKα activation, particularly in non-canonical NF-κB signaling. This pathway is essential for B-cell maturation, lymphoid organogenesis, and osteoclast differentiation. Phosphorylation at Thr23 may influence IKKα’s kinase activity or its ability to phosphorylate downstream targets like p100/NF-κB2. leading to p100 processing into active p52. Additionally, this post-translational modification has been linked to cellular responses to stimuli such as cytokines (e.g., BAFF, CD40L) or stress signals.
The IKKα (Phospho-Thr23) antibody enables researchers to detect and quantify IKKα activation status in various experimental models, including Western blotting, immunofluorescence, and immunoprecipitation. Its specificity for the phosphorylated form allows differentiation between active and inactive IKKα, aiding studies on NF-κB dynamics in diseases like cancer, autoimmune disorders, and chronic inflammation. Validated applications and species reactivity (e.g., human, mouse) ensure its utility in both basic research and therapeutic development targeting NF-κB pathways.
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