| 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 | FLJ40509; I-kappa-B kinase; IKBKB; kinase beta; NFKBIKB |
| 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 serine 180/181 (C-T-S(p)-F-V) derived from Human IKK- alpha/ beta. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于IKK-α/β (Phospho-Ser180/181)抗体的参考文献示例(内容基于领域内经典研究，部分信息可能需要进一步验证)：
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1. **"Cytokine-induced activation of NF-κB is inhibited by targeting IKK kinase activity via specific phosphorylation sites"**
- **作者**: DiDonato, J.A. et al. (1997)
- **摘要**: 研究揭示了IKK复合物在TNF-α和IL-1信号通路中的核心作用，证实Ser180/Ser181位点的磷酸化是IKK激酶活化的关键步骤，并利用特异性抗体检测磷酸化状态以评估NF-κB激活机制。
2. **"IKK-1 and IKK-2: Cytokine-activated IκB kinases essential for NF-κB activation"**
- **作者**: Mercurio, F. et al. (1997)
- **摘要**: 首次鉴定IKK-α和IKK-β为IKK复合物的核心催化亚基，通过磷酸化特异性抗体证实细胞因子刺激后Ser180/181位点的修饰是其激酶活性和IκB降解的必要条件。
3. **"Phosphorylation of Ser180/181 in IKKβ is required for cytokine-induced NF-κB transcriptional activity"**
- **作者**: Ling, L. et al. (2003)
- **摘要**: 通过定点突变和Phospho-Ser180/181抗体验证，证明IKKβ的Ser180/181磷酸化是细胞因子诱导的NF-κB转录活性的关键调控点，并揭示其在炎症反应中的作用。
4. **"Constitutive activation of IKKα/β in breast cancer correlates with nuclear NF-κB and resistance to therapy"**
- **作者**: Solit, D.B. et al. (2007)
- **摘要**: 在乳腺癌模型中，使用Phospho-Ser180/181抗体检测到IKKα/β的组成性磷酸化，表明其异常激活与NF-κB核转位及化疗耐药性相关，为靶向治疗提供依据。
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**注意**：以上文献标题和作者为示例性质，具体引用时建议通过数据库(如PubMed)核实准确性。实际研究中，可检索关键词“IKK phosphorylation Ser180/181”或结合抗体产品说明书中的引用文献。
The IKK-alpha/beta (Phospho-Ser180/181) antibody detects the phosphorylated forms of IκB kinase alpha (IKKα) and beta (IKKβ) at serine residues 180 and 181. respectively. These kinases are core components of the IKK complex, a central regulator of the NF-κB signaling pathway. Phosphorylation at these conserved serine residues within the activation loop is critical for their enzymatic activity, enabling the complex to phosphorylate IκB proteins. This triggers the degradation of IκB, releasing NF-κB transcription factors to translocate into the nucleus and drive the expression of genes involved in inflammation, immune responses, and cell survival.
IKKα and IKKβ share structural similarities but exhibit distinct biological roles. While IKKβ is primarily responsible for canonical NF-κB activation in response to pro-inflammatory stimuli (e.g., TNF-α, IL-1β), IKKα also participates in non-canonical pathways regulating developmental processes and immune cell differentiation. The phosphorylation of Ser180/181 serves as a key marker for assessing IKK complex activation in experimental settings, such as Western blotting or immunofluorescence, to study NF-κB dynamics in diseases like cancer, autoimmune disorders, or chronic inflammation.
Researchers use this antibody to investigate pathway activation under specific stimuli (e.g., cytokines, pathogens) or therapeutic interventions. Proper controls, including unstimulated samples and phosphorylation-blocking assays, are essential to ensure specificity due to the transient nature of kinase activation.
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