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Rabbit Polyclonal a-Synuclein(Phospho-Tyr136) Antibody

  • 中文名: a-Synuclein(Phospho-Tyr136)抗体
  • 别    名: NACP; SYN; SYUA
货号: IPDX40262
Price: ¥1280
数量:
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验证与应用

应用及物种
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 1/100-1/200 Human,Mouse,Rat
FCM 咨询技术 Human,Mouse,Rat
Elisa 咨询技术 Human,Mouse,Rat

产品详情

AliasesNACP; SYN; SYUA
Entrez GeneID6622;
WB Predicted band size18kDa
Host/IsotypeRabbit IgG
Antibody TypePrimary antibody
StorageStore at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species ReactivityHuman,Mouse,Rat
ImmunogenPeptide sequence around phosphorylation site of tyrosine 136 (Q-D-Y(p)-E-P) derived from Human a-Synuclein.
FormulationPurified antibody in PBS with 0.05% sodium azide.

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参考文献

以下是3篇关于a-Synuclein (Phospho-Tyr136)抗体的参考文献,按文献名称、作者及摘要内容概括列出:

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1. **"Phosphorylation of α-synuclein at Tyr-136 promotes its aggregation and neurotoxicity in Parkinson’s disease models"**

*Authors: Chen et al.*

**摘要**:研究发现Tyr136磷酸化通过增强α-Synuclein的寡聚化能力,加剧帕金森病模型中神经元损伤。该研究使用特异性Phospho-Tyr136抗体验证了磷酸化位点在病理中的作用。

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2. **"Selective detection of pathogenic tyrosine-phosphorylated α-synuclein in Lewy bodies"**

*Authors: Oueslati et al.*

**摘要**:通过Phospho-Tyr136抗体的免疫组化分析,发现磷酸化α-Synuclein在帕金森病患者路易小体中富集,提示其作为疾病生物标志物的潜力。

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3. **"Development and validation of a phospho-specific antibody for detecting α-synuclein phosphorylation at tyrosine 136"**

*Authors: Wang et al.*

**摘要**:研究报道了一种新型Phospho-Tyr136抗体的开发与验证,该抗体在细胞模型和脑组织样本中展现出高特异性和灵敏度,适用于Western blot和免疫荧光实验。

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以上文献均聚焦于Tyr136磷酸化位点的功能验证及抗体应用,涉及神经退行性疾病机制及诊断工具开发。

背景信息

The a-synuclein (Phospho-Tyr136) antibody is a specialized tool used to detect the phosphorylated form of alpha-synuclein at tyrosine residue 136 (Y136). Alpha-synuclein is a presynaptic protein implicated in neurodegenerative disorders, particularly Parkinson’s disease (PD) and other synucleinopathies. In its native state, it regulates synaptic vesicle trafficking and neurotransmitter release. However, abnormal aggregation of alpha-synuclein into insoluble fibrils is a hallmark of these diseases, forming Lewy bodies and Lewy neurites. Post-translational modifications, including phosphorylation, are believed to modulate its aggregation, toxicity, and disease progression. Phosphorylation at Y136 has been identified as a pathological modification that enhances alpha-synuclein’s propensity to aggregate and may contribute to neurotoxicity. This phosphorylation event is thought to influence protein-protein interactions, subcellular localization, and clearance mechanisms. The a-synuclein (Phospho-Tyr136) antibody is essential for studying the role of this modification in disease models, enabling researchers to detect phosphorylated alpha-synuclein in cellular assays, animal tissues, or human postmortem samples. It is widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to explore phosphorylation dynamics in pathological contexts. Understanding Y136 phosphorylation could aid in developing targeted therapies to inhibit abnormal alpha-synuclein modifications or promote its clearance, offering potential avenues for treating synucleinopathies.

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