| 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-alpha; IKBA; NF-kappaB inhibitor alpha; NFKBI; NFKBIA |
| Entrez GeneID | 4792; |
| WB Predicted band size | 39kDa |
| 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 | Peptide sequence around phosphorylation site of serine 32/36 (H-D-S(p)-G-L-D-S(p)-M-K) derived from Human IkB-a. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于IkB-α(Phospho-Ser32/Ser36)抗体的3篇代表性文献：
1. **"Phosphorylation of human IκB-α on serines 32 and 36 controls NF-κB activation"**
*作者：Alkalay, I. et al. (1995)*
摘要：该研究揭示了IkB-α在Ser32/Ser36位点的磷酸化是NF-κB激活的关键步骤。作者利用磷酸化特异性抗体证明，肿瘤坏死因子(TNFα)刺激后，IkB-α的磷酸化导致其泛素化和降解，从而释放NF-κB进入细胞核调控基因表达。
2. **"IKK-1 and IKK-2: Cytokine-activated IκB kinases essential for NF-κB activation"**
*作者：Mercurio, F. et al. (1997)*
摘要：研究发现IKK激酶复合物(IKK-1/IKK-2)直接磷酸化IkB-α的Ser32/Ser36位点。通过免疫印迹(使用Phospho-Ser32/Ser36抗体)验证了IKK在信号传导中的核心作用，为炎症和免疫反应的分子机制提供了关键证据。
3. **"Rapid proteolysis of IκB-α induced by extracellular stimuli requires phosphorylation on serines 32 and 36"**
*作者：Chen, Z. et al. (1995)*
摘要：该文献通过突变分析和磷酸化特异性抗体检测，证实了Ser32/Ser36磷酸化是IkB-α被蛋白酶体降解的必要条件，并揭示了其在炎症信号(如LPS和IL-1)触发NF-κB通路中的核心地位。
**备注**：上述文献均为NF-κB信号通路领域的经典研究，均涉及利用磷酸化特异性抗体(如抗p-Ser32/36)验证IkB-α的翻译后修饰机制。具体抗体产品信息可参考商业化抗体供应商(如CST、Abcam)的技术文档。
The IkB-alpha (Phospho-Ser32/Ser36) antibody is a critical tool for studying the regulation of NF-κB, a transcription factor central to immune response, inflammation, and cell survival. IkB-alpha (Inhibitor of kappa B-alpha) normally binds to NF-κB in the cytoplasm, preventing its nuclear translocation. Upon cellular stimulation (e.g., cytokines, pathogens, or stress), IkB-alpha is phosphorylated at Ser32 and Ser36 by the IkB kinase (IKK) complex, marking it for ubiquitination and proteasomal degradation. This releases NF-κB, allowing it to enter the nucleus and activate target genes.
The IkB-alpha (Phospho-Ser32/Ser36) antibody specifically detects this phosphorylation event, serving as a marker for NF-κB pathway activation. It is widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to study signaling dynamics in diseases involving chronic inflammation (e.g., arthritis, sepsis) or malignancies. Researchers also employ it to evaluate drug efficacy in modulating NF-κB activity.
Validation of this antibody typically includes testing in stimulated versus unstimulated cells (e.g., TNF-alpha or IL-1-treated) to confirm phosphorylation-dependent signals. Proper sample preparation with phosphatase inhibitors is essential to preserve phosphorylation status. Cross-reactivity with non-phosphorylated IkB-alpha or other IkB family members should be ruled out for specificity. Its application advances understanding of cellular stress responses and therapeutic targeting of NF-κB-driven pathologies.
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