| 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 | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | TACTILE |
| Entrez GeneID | 10225 |
| clone | 5E6C12 |
| WB Predicted band size | 65.6kDa |
| Host/Isotype | Mouse IgG2b |
| 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 | Purified recombinant fragment of human CD96 (AA: extra 321-519) expressed in E. Coli. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide |
+ +
以下是关于IkB-e (Phospho-Ser22)抗体的参考文献概览，包含文献名称、作者及摘要内容概括：
1. **"Site-specific phosphorylation of IkB-e regulates its degradation and NF-κB signaling"**
*作者：Chen et al.*
**摘要**：研究揭示了IkB-e在Ser22位点的磷酸化通过泛素-蛋白酶体途径调控其稳定性，并利用特异性抗体(Phospho-Ser22)证明该修饰在炎症因子诱导的NF-κB激活中的关键作用。
2. **"A phospho-specific antibody targeting IkB-e Ser22 reveals dynamic phosphorylation in immune responses"**
*作者：Martinez et al.*
**摘要**：本文报道了一种针对IkB-e Ser22磷酸化位点的单克隆抗体的开发与验证，通过流式细胞术和免疫印迹证实其在检测Toll样受体激活后IkB-e磷酸化动力学中的应用。
3. **"Phosphorylation-dependent interactions of IkB-e with TRAF2 in TNF-α signaling"**
*作者：Kimura et al.*
**摘要**：研究发现TNF-α刺激诱导IkB-e Ser22磷酸化，利用Phospho-Ser22抗体揭示其与TRAF2蛋白的结合增强，从而负调控NF-κB的过度激活。
4. **"IkB-e phosphorylation modulates dendritic cell maturation"**
*作者：Rodriguez et al.*
**摘要**：通过Phospho-Ser22抗体检测发现，IkB-e在Ser22的磷酸化抑制树突状细胞成熟，并降低促炎细胞因子分泌，表明该位点可能是免疫治疗的潜在靶点。
*注：上述内容为模拟生成的文献概括，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。*
The IkB-epsilon (Phospho-Ser22) antibody is designed to detect the phosphorylated form of IkB-epsilon (IκBε) at serine residue 22. a key post-translational modification involved in regulating NF-κB signaling. IκBε is a member of the inhibitor of κB (IκB) family, which binds to NF-κB transcription factors in the cytoplasm, preventing their nuclear translocation and activation of target genes. Phosphorylation of IκBε at Ser22. often mediated by upstream kinases such as IKK (IκB kinase), triggers its ubiquitination and proteasomal degradation, releasing NF-κB to initiate immune, inflammatory, and stress responses. This phosphorylation event is critical for dynamic control of NF-κB activity in response to stimuli like cytokines, pathogens, or stress signals.
The IkB-epsilon (Phospho-Ser22) antibody is widely used in research to study the activation status of the NF-κB pathway, particularly in contexts like inflammation, cancer, and immune disorders. It enables specific detection of the phosphorylated, active form of IκBε via techniques such as Western blotting, immunofluorescence, or immunoprecipitation. Validation typically includes testing in cell lines treated with NF-κB activators (e.g., TNF-α or LPS) or inhibitors (e.g., proteasome blockers) to confirm phosphorylation-dependent signals. Understanding IκBε phosphorylation dynamics aids in elucidating mechanisms of NF-κB dysregulation in diseases and evaluating therapeutic interventions targeting this pathway.
×
