| 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 | CHUK; IKKA; TCF16; Inhibitor of nuclear factor kappa-B kinase subunit alpha; I-kappa-B kinase alpha; IKK-A; IKK-alpha; IkBKA; IkappaB kinase; Conserved helix-loop-helix ubiquitous kinase; I-kappa-B kinase 1; IKK1; Nuclear factor NF-kappa-B |
| Entrez GeneID | 1147 |
| WB Predicted band size | Calculated MW: 85 kDa; Observed MW: 85 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 | Synthetic peptide of human CHUK |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是关于Phospho-IKK alpha/beta (Ser176/Ser177)抗体的3篇参考文献及其摘要：
1. **文献名称**：*IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation*
**作者**：Karin, M. et al.
**摘要**：该研究首次阐明IKKα和IKKβ在NF-κB信号通路中的核心作用，通过检测Ser176/177磷酸化位点，证实其在炎症因子(如TNF-α)刺激下激活，进而介导IκBα降解和NF-κB核转位。
2. **文献名称**：*Viral Infection Induces Phosphorylation of IKKα/β through TRAF6 Signaling*
**作者**：Häcker, H. et al.
**摘要**：研究发现病毒RNA通过Toll样受体(TLR3)激活TRAF6.诱导IKKα/β在Ser176/177位点的磷酸化，利用特异性抗体验证了该修饰是抗病毒免疫反应中NF-κB活化的关键步骤。
3. **文献名称**：*Targeting IKKβ Activity through Allosteric Inhibition in Inflammatory Diseases*
**作者**：Mankan, A.K. et al.
**摘要**：通过小分子抑制剂靶向IKKβ的活性，该研究使用Phospho-IKKα/β (Ser176/177)抗体评估抑制效果，证明阻断磷酸化可减轻类风湿性关节炎模型中的炎症反应。
4. **文献名称**：*Phosphorylation Dynamics of IKKα/β in Tumor Microenvironment-Driven NF-κB Activation*
**作者**：Luo, J.L. et al.
**摘要**：分析肿瘤微环境中细胞因子(如IL-6)对IKKα/β磷酸化的调控，发现Ser176/177位点的持续激活促进肿瘤细胞存活和化疗耐药性，为靶向治疗提供依据。
这些文献涵盖了该抗体在机制研究、病毒感染、药物开发和肿瘤生物学中的应用。
The Phospho-IKK alpha/beta (Ser176/Ser177) antibody detects the activated form of the inhibitor of nuclear factor kappa-B kinase (IKK) complex, a central regulator of the NF-κB signaling pathway. The IKK complex, composed of catalytic subunits IKKα (IKK1) and IKKβ (IKK2) along with the regulatory scaffold protein NEMO (IKKγ), plays a critical role in inflammatory, immune, and stress responses. Activation of the complex occurs through phosphorylation of specific serine residues (Ser176 in IKKα and Ser177 in IKKβ) within their activation loops. This phosphorylation event, often triggered by pro-inflammatory cytokines (e.g., TNF-α, IL-1) or pathogen-associated molecular patterns, enables the IKK complex to phosphorylate the inhibitor of NF-κB (IκB), marking it for proteasomal degradation. Subsequent NF-κB nuclear translocation initiates transcription of target genes involved in inflammation, cell survival, and proliferation.
The Phospho-IKK alpha/beta (Ser176/Ser177) antibody is widely used in research to study NF-κB pathway activation under various conditions, such as infection, autoimmune disorders, or cancer. It specifically recognizes the phosphorylated state of IKKα/β, distinguishing active from inactive kinase forms. Applications include Western blotting, immunofluorescence, and immunohistochemistry to assess pathway activity in cell lines, tissues, or disease models. Its utility extends to drug discovery, where it helps evaluate compounds targeting IKK or upstream regulators. Validated in multiple experimental systems, this antibody is essential for elucidating mechanisms linking IKK activation to pathologies like chronic inflammation, neurodegeneration, and tumor progression.
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