| 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 | NFKBIA; IKBA; MAD3; NFKBI; NF-kappa-B inhibitor alpha; I-kappa-B-alpha; IkB-alpha; IkappaBalpha; Major histocompatibility complex enhancer-binding protein MAD3 |
| Entrez GeneID | 4792 |
| WB Predicted band size | Calculated MW: 36 kDa; Observed MW: 39 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 |
| Immunogen | A synthetic phosphopeptide corresponding to residues surrounding Ser36 of human IKB alpha |
| Formulation | Purified antibody in TBS with 0.05% sodium azide,0.05%BSA and 50% glycerol. |
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以下是关于 **Phospho-IKB alpha (Ser36)** 抗体的3篇参考文献，按文献名称、作者和摘要内容概括列出：
1. **"IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation"**
*作者：DiDonato, J. A. et al. (1997)*
摘要：该研究阐明了IKK复合物(IKK-1/IKK-2)在炎症因子刺激下直接磷酸化IKBα蛋白的**Ser32和Ser36位点**，触发其泛素化降解，从而激活NF-κB信号通路。文中使用Phospho-IKBα (Ser36)抗体验证了磷酸化事件，证实了IKK激酶的特异性作用。
2. **"Phosphorylation of Human IκB-α on Serines 32 and 36 Controls IκB-α Proteolysis and NF-κB Activation"**
*作者：Brown, K. et al. (1995)*
摘要：通过突变分析和磷酸化特异性抗体(包括抗Ser36抗体)，证明IKBα的**Ser32/Ser36双位点磷酸化**是NF-κB激活的必要条件。研究揭示了TNF-α刺激后，IKBα磷酸化与蛋白酶体降解的直接关联。
3. **"Specific Inhibition of NF-κB-Dependent Transcription by a Novel Dioxin Analog in Human Breast Cancer Cells"**
*作者：Pratt, M. A. C. et al. (2003)*
摘要：利用Phospho-IKBα (Ser36)抗体检测乳腺癌细胞中NF-κB通路的抑制效果，发现特定化合物通过阻断IKBα磷酸化(Ser36)抑制NF-κB转录活性，为靶向治疗提供了实验依据。
**备注**：经典研究中常同时检测Ser32/Ser36双位点磷酸化(如文献1、2)，部分抗体可能针对双位点设计。若需专一Ser36文献，建议查阅抗体供应商(如CST、Abcam)的技术手册或应用案例。
The Phospho-IKB alpha (Ser36) antibody detects the phosphorylated form of Inhibitor of Nuclear Factor Kappa-B Alpha (IKBα) at serine residue 36. a key regulatory site in the NF-κB signaling pathway. IKBα normally binds to NF-κB transcription factors in the cytoplasm, preventing their nuclear translocation. Upon cellular stimulation (e.g., cytokines, pathogens, or stress), the IKK (IκB kinase) complex phosphorylates IKBα at Ser32 and Ser36. marking it for ubiquitination and proteasomal degradation. This releases NF-κB, enabling its entry into the nucleus to activate genes involved in inflammation, immunity, and cell survival.
The Phospho-IKB alpha (Ser36) antibody is widely used to study NF-κB activation dynamics in conditions like cancer, autoimmune diseases, and infections. It helps researchers assess pathway activity in response to stimuli or therapeutic interventions. Specificity for Ser36 phosphorylation ensures accurate detection of the activated IKBα degradation pathway. Applications include Western blotting, immunofluorescence, and immunoprecipitation in cell lines, tissues, or primary cells. This antibody is critical for understanding dysregulated NF-κB signaling in disease mechanisms and evaluating inhibitors targeting IKK or upstream regulators. Proper controls, such as unphosphorylated IKBα and stimulation with TNF-α or IL-1β, are recommended to validate results.
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