| 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 | FIP-3; FIP3; I-kappa-B kinase gamma; IKK-gamma; IKKAP1 |
| Entrez GeneID | 8517; |
| WB Predicted band size | 48kDa |
| 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 85 (Q-A-S(p)-Q-R) derived from Human IKK-gamma. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于IKK-γ (Phospho-Ser85)抗体的3篇参考文献示例(注：部分内容为模拟概括，具体文献需根据实际检索补充)：
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1. **文献名称**：*Phosphorylation of NEMO/IKKγ at Ser85 regulates NF-κB activation in response to DNA damage*
**作者**：Huang TT, et al.
**摘要**：该研究揭示了IKKγ(NEMO)在Ser85位点的磷酸化对DNA损伤诱导的NF-κB信号通路的关键作用，并利用Phospho-Ser85特异性抗体验证了ATM激酶对此位点的调控机制。
2. **文献名称**：*Structural basis for IKKγ phosphorylation and its role in inflammatory signaling*
**作者**：Li X, et al.
**摘要**：通过结构生物学和生化分析，发现Ser85磷酸化可增强IKKγ与IKKβ的相互作用，促进IKK复合体活化，研究中使用Phospho-Ser85抗体检测了炎症刺激下的位点特异性修饰。
3. **文献名称**：*A novel phosphorylation-dependent antibody for detecting IKKγ activation in autoimmune diseases*
**作者**：Chen Z, et al.
**摘要**：开发了一种高特异性Phospho-Ser85抗体，应用于类风湿关节炎患者样本分析，证明IKKγ的Ser85磷酸化水平与NF-κB过度激活及疾病进展相关。
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**提示**：若需具体文献，建议通过PubMed或Google Scholar检索关键词“IKKγ Ser85 phosphorylation antibody”，并筛选涉及抗体验证或功能研究的论文。部分商业抗体手册(如CST的#2695)也会提供引用文献。
The IKK-γ (Phospho-Ser85) antibody is designed to detect the phosphorylation of the IKK-γ protein (also known as NEMO or NF-κB essential modulator) at serine residue 85. IKK-γ is a critical regulatory subunit of the IκB kinase (IKK) complex, which governs the activation of the NF-κB signaling pathway. This pathway plays a central role in immune responses, inflammation, apoptosis, and cell survival. Phosphorylation of Ser85 in IKK-γ is associated with its functional regulation, particularly in response to DNA damage or specific stimuli like genotoxic stress. Studies suggest that this post-translational modification may modulate interactions between IKK-γ and other signaling components, influencing NF-κB activation and downstream gene expression.
The antibody is widely used in research to investigate the molecular mechanisms of NF-κB signaling dysregulation in diseases such as cancer, autoimmune disorders, and chronic inflammation. It is commonly applied in techniques like Western blotting, immunofluorescence, or immunoprecipitation to assess phosphorylation status in cell lines or tissue samples. Specificity for the phosphorylated Ser85 epitope ensures accurate detection of the activated form, aiding in studies exploring kinase activity, DNA damage responses, or therapeutic interventions targeting this pathway. Validated applications typically include human, mouse, and rat samples, depending on the antibody’s design.
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