| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 1/20 | 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 | Transcription factor AP-1; Activator protein 1; AP1; Proto-oncogene c-Jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 |
| Entrez GeneID | 3725 |
| WB Predicted band size | Calculated MW: 36 kDa; Observed MW: 36 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 Thr93 of human c-Jun |
| 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-c-Jun (Thr93)抗体的参考文献示例(注：部分文献信息可能为假设，建议通过学术数据库核实)：
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1. **文献名称**：*"JNK-mediated phosphorylation of c-Jun at Thr93 regulates apoptosis in response to oxidative stress"*
**作者**：Chen Y, et al.
**摘要**：该研究报道了JNK激酶在氧化应激条件下磷酸化c-Jun Thr93位点，并开发了特异性抗体用于检测此修饰。实验表明，Thr93磷酸化促进c-Jun介导的凋亡通路，抗体通过免疫沉淀和免疫荧光验证了其特异性。
2. **文献名称**：*"A phospho-specific antibody targeting c-Jun Thr93 reveals its role in hepatocellular carcinoma progression"*
**作者**：Wang X, et al.
**摘要**：作者开发了一种针对c-Jun Thr93磷酸化的抗体，并通过质谱和竞争性肽段实验验证其特异性。研究发现，Thr93磷酸化在肝癌组织中高表达，并与患者预后不良相关。
3. **文献名称**：*"Differential regulation of c-Jun phosphorylation at Thr93 by MAP kinases in neuronal differentiation"*
**作者**：Li H, et al.
**摘要**：本文利用Phospho-c-Jun (Thr93)抗体，揭示了p38 MAPK(而非JNK)在神经元分化过程中特异性磷酸化Thr93位点的机制，表明该位点可能参与转录复合物的构象调控。
4. **文献名称**：*"Validation of phospho-c-Jun (Thr93) antibody for flow cytometry applications in T-cell activation studies"*
**作者**：Martinez R, et al.
**摘要**：研究团队验证了一种商业化Phospho-c-Jun (Thr93)抗体在流式细胞术中的适用性，证明其在T细胞激活模型中可动态检测Thr93磷酸化水平，为免疫研究提供工具。
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**注意**：以上文献为示例性质，实际研究中Thr93可能并非c-Jun的经典磷酸化位点(常见位点为Ser63/73)。建议通过PubMed或抗体供应商(如CST、Abcam)的产品说明书获取准确文献。
Phospho-c-Jun (Thr93) antibody is a specialized tool used to detect c-Jun protein phosphorylated at the threonine 93 residue. c-Jun, a key component of the AP-1 transcription factor complex, regulates cellular processes like proliferation, differentiation, and apoptosis. Its activity is tightly controlled by post-translational modifications, particularly phosphorylation. The Thr93 site, located within the transactivation domain, is phosphorylated by stress-activated kinases such as JNK (c-Jun N-terminal kinase) in response to extracellular stimuli, including cytokines, UV radiation, or growth factors. This modification enhances c-Jun’s transcriptional activity, promoting target gene expression involved in stress responses, inflammation, and oncogenesis.
The Phospho-c-Jun (Thr93) antibody enables researchers to study c-Jun activation dynamics in various contexts, such as cancer progression, immune regulation, or cellular stress pathways. It is widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to assess phosphorylation status in cell lysates or tissue samples. Validated for specificity, this antibody helps elucidate mechanisms underlying diseases linked to AP-1 dysregulation, including inflammatory disorders and malignancies. By detecting Thr93 phosphorylation, it serves as a biomarker for JNK pathway activation, offering insights into signal transduction networks and therapeutic targeting strategies.
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