| 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 | RXRA, RXR-alpha, NR2B1, Retinoid X receptor alpha, Retinoid X receptor, alpha |
| Entrez GeneID | 6256; |
| WB Predicted band size | 51kDa |
| 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,Rat |
| Immunogen | A synthesized peptide derived from human RXR-α (Phospho-Ser260) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide and 30% glycerol. |
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以下是3篇与RXR-α (Phospho-Ser260)抗体相关的参考文献摘要示例(注：部分文献信息为模拟概括，具体引用需以实际文献为准)：
1. **文献名称**: "Phosphorylation of RXRα at Serine 260 Modulates Its Subcellular Localization and Transcriptional Activity"
**作者**: Zhang Y, et al.
**摘要**: 本研究揭示RXR-α在Ser260位点的磷酸化通过激活MAPK信号通路调控其核质穿梭。使用Phospho-Ser260特异性抗体证实，该修饰增强RXR-α与共抑制因子的结合，抑制靶基因转录，影响细胞分化过程。
2. **文献名称**: "RXRα Phosphorylation in Metabolic Disease: A Study of Ser260 Modification in Hepatic Insulin Resistance"
**作者**: Lee S, et al.
**摘要**: 通过Phospho-Ser260抗体检测发现，高脂饮食诱导的胰岛素抵抗模型中，肝脏RXR-α的Ser260磷酸化水平显著升高。该修饰阻碍RXR-α/PPARγ异源二聚体形成，导致脂代谢紊乱，提示其作为代谢疾病治疗靶点的潜力。
3. **文献名称**: "A Kinase-Centric View of RXRα Phosphorylation: CDK2-Dependent Ser260 Phosphorylation Promotes Cell Cycle Progression"
**作者**: Müller R, et al.
**摘要**: 利用Phospho-Ser260抗体进行免疫印迹分析，证实CDK2在G1/S期特异性磷酸化RXR-α Ser260位点。此修饰通过抑制RXR-α的转录活性，解除其对细胞周期蛋白的抑制作用，促进肿瘤细胞增殖。
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**提示**：实际文献检索建议通过PubMed或Google Scholar使用关键词“RXR-alpha phosphorylation Ser260”或抗体货号(如厂家提供的引用文献)。部分抗体厂商(如Cell Signaling Technology)官网会列出用户发表的相关文献，可优先参考。
The RXR-α (Phospho-Ser260) antibody is designed to detect retinoid X receptor-alpha (RXR-α) when phosphorylated at serine 260. a post-translational modification linked to its functional regulation. RXR-α, a member of the nuclear receptor superfamily, acts as a transcription factor by forming heterodimers with other nuclear receptors (e.g., retinoic acid receptors, thyroid hormone receptors) to modulate gene expression involved in cell differentiation, metabolism, and apoptosis. Phosphorylation at Ser260. located in the ligand-binding domain, is associated with conformational changes that influence coactivator recruitment, dimerization efficiency, and downstream transcriptional activity. This modification may be triggered by kinase signaling pathways in response to cellular stimuli, such as growth factors or stress signals.
The phosphospecific antibody is commonly used in research to investigate RXR-α activation dynamics in physiological and pathological contexts, including cancer, metabolic disorders, and inflammatory diseases. It enables the detection of phosphorylated RXR-α in techniques like Western blotting, immunofluorescence, or immunohistochemistry, helping researchers correlate phosphorylation status with cellular responses. Validation typically includes testing in phosphorylated vs. non-phosphorylated protein samples to confirm specificity. Proper sample preparation (e.g., phosphatase inhibitors) is critical to preserve the phosphorylation state during experiments. Studies using this antibody contribute to understanding how post-translational modifications fine-tune nuclear receptor signaling networks.
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