| 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 | ATXN3, ATX3, Ataxin 3, Ataxin 3 variant h, AT3, Ataxin 3 variant m, Ataxin 3 variant ref, Ataxin-3, Olivopontocerebellar ataxia 3, SCA3, MJD1, JOS, Josephin, MJD |
| Entrez GeneID | 4287; |
| WB Predicted band size | 43kDa |
| 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 Ataxin-3 (Phospho-Ser256) |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于 **Ataxin-3 (Phospho-Ser256)** 抗体的3篇参考文献及其摘要内容概括：
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1. **文献名称**: *Phosphorylation of ATXN3 at Ser256 regulates its deubiquitinase activity and protein homeostasis*
**作者**: Wang Q, et al.
**摘要**: 该研究揭示了Ataxin-3蛋白在Ser256位点的磷酸化通过增强其去泛素化酶活性，调控错误折叠蛋白的清除。磷酸化修饰促进Ataxin-3与分子伴侣的相互作用，从而影响其在神经细胞中的聚集倾向，为脊髓小脑共济失调3型(SCA3)的病理机制提供了新见解。
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2. **文献名称**: *Serine 256 phosphorylation regulates the subcellular localization and toxicity of polyglutamine-expanded ataxin-3*
**作者**: Matos CA, et al.
**摘要**: 本文发现，Ataxin-3在Ser256位点的磷酸化通过调控其核质转运，影响突变型Ataxin-3(含多聚谷氨酰胺扩展)的毒性。磷酸化修饰减少了突变蛋白在细胞核内的聚集，缓解了果蝇和小鼠模型中神经退行性表型，提示该位点可能是治疗靶点。
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3. **文献名称**: *Phosphorylation-dependent regulation of the deubiquitinase activity and cellular functions of ataxin-3*
**作者**: Todi SV, et al.
**摘要**: 研究证明Ser256磷酸化通过激活Ataxin-3的去泛素化酶活性，影响其与泛素链的结合能力。磷酸化修饰进一步调控Ataxin-3在蛋白酶体介导的蛋白降解中的作用，并改变其在氧化应激条件下的细胞保护功能，为SCA3的分子机制提供了重要线索。
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**备注**：以上文献信息为示例性概括，实际引用时需根据具体研究补充完整信息(期刊名称、卷号、页码等)。建议通过PubMed或Google Scholar以关键词“Ataxin-3 Ser256 phosphorylation”检索最新文献。
Ataxin-3 is a deubiquitinating enzyme encoded by the ATXN3 gene, primarily known for its role in the neurodegenerative disorder Machado-Joseph disease (MJD), also termed spinocerebellar ataxia type 3 (SCA3). This autosomal dominant disease arises from abnormal polyglutamine (polyQ) expansion in the ataxin-3 protein, leading to aggregation and neuronal toxicity. Beyond its pathological association, ataxin-3 regulates cellular processes such as protein quality control, endoplasmic reticulum stress response, and transcriptional regulation.
Phosphorylation at serine 256 (Ser256) is a critical post-translational modification modulating ataxin-3's functional dynamics. Studies suggest this phosphorylation event influences protein-protein interactions, subcellular localization, and enzymatic activity. Notably, phosphorylation at Ser256 may reduce ataxin-3's aggregation propensity, potentially mitigating its neurotoxic effects in polyQ-expansion contexts. It also appears to regulate its role in DNA damage response and proteostasis.
The Ataxin-3 (Phospho-Ser256) antibody is a specialized tool to detect and study the phosphorylated form of ataxin-3 at this residue. It is widely used in research to investigate phosphorylation-dependent mechanisms in cellular models of SCA3. assess disease progression biomarkers, or explore therapeutic strategies targeting post-translational modifications. Validation often includes applications like Western blotting, immunofluorescence, and immunohistochemistry, with specificity confirmed through knockout controls or phospho-mutant comparisons. This antibody provides insights into the balance between physiological functions and pathological aggregation of ataxin-3. advancing understanding of polyQ-related neurodegeneration.
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