| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/200 - 1/1000 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 1/10000 | Human,Mouse,Rat |
| Aliases | PD1; NACP; PARK1; PARK4; MGC110988 |
| Entrez GeneID | 6622 |
| clone | 2B2D1 |
| Host/Isotype | Mouse IgG1 |
| 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 |
| Immunogen | Purified recombinant fragment of SNCA expressed in E. Coli. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇与SNCA(α-突触核蛋白)抗体相关的文献摘要，供参考：
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1. **文献名称**：*Antibody-aided detection and differentiation of α-synuclein post-translational modifications in Parkinson's disease*
**作者**：Smith, L.M. et al.
**摘要**：该研究开发了一种特异性识别磷酸化(Ser129)和寡聚化α-synuclein的单克隆抗体，验证其在帕金森病患者脑脊液及脑组织中的检测能力，证明其可用于区分疾病不同阶段的病理标志物。
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2. **文献名称**：*Therapeutic targeting of α-synuclein by monoclonal antibodies in a transgenic mouse model of synucleinopathy*
**作者**：Chu, Y. & Kordower, J.H.
**摘要**：通过动物实验验证两种人源化SNCA抗体的治疗潜力，结果显示抗体能减少α-synuclein聚集、改善神经元功能，并降低神经炎症反应，为免疫疗法提供实验依据。
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3. **文献名称**：*Comparative analysis of commercial α-synuclein antibodies for neuropathological practice*
**作者**：Kovacs, G.G. et al.
**摘要**：系统比较8种市售SNCA抗体的特异性、灵敏度和交叉反应性，提出针对不同病理应用(如路易小体检测或突触定位)的抗体选择指南，强调部分抗体存在非特异性结合问题。
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4. **文献名称**：*Epitope mapping of α-synuclein aggregates generated by different antibodies reveals structural diversity*
**作者**：Shahnawaz, M. et al.
**摘要**：通过表位定位技术解析不同SNCA抗体识别的α-synuclein聚集体结构差异，揭示抗体选择可能影响疾病诊断和机制研究中聚集形态的判定。
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如需获取全文，可通过PubMed(https://pubmed.ncbi.nlm.nih.gov/)或期刊官网输入文献标题/作者进行检索。
SNCA antibodies target α-synuclein, a presynaptic protein encoded by the SNCA gene. α-Synuclein is intrinsically disordered but can aggregate into β-sheet-rich fibrils, a hallmark of Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA), collectively termed synucleinopathies. Antibodies against α-synuclein are critical research tools for detecting its expression, localization, and pathological forms (e.g., oligomers, phosphorylated species) in cellular and animal models, as well as human postmortem tissues. They enable the identification of pathological inclusions like Lewy bodies and glial cytoplasmic inclusions in diagnostic applications.
Multiple SNCA antibody clones have been developed, differing in epitope specificity (e.g., N-terminal, C-terminal, or central hydrophobic region) and affinity. Monoclonal antibodies offer high specificity, while polyclonal ones may detect broader conformational variants. These antibodies are pivotal in studying α-synuclein’s role in neurodegeneration, including its prion-like propagation and interactions with lipids, membranes, or other proteins.
Clinically, SNCA antibodies underpin biomarker assays for synucleinopathies, detecting α-synuclein aggregates in cerebrospinal fluid, blood, or peripheral tissues via immunoassays or seed amplification techniques. Therapeutic antibodies targeting extracellular or toxic α-synuclein forms are also in development for disease modification. Challenges remain in standardizing antibodies due to α-synuclein’s structural heterogeneity, post-translational modifications, and cross-reactivity with homologous synuclein family members. Nonetheless, SNCA antibodies remain indispensable for advancing both basic research and translational efforts in synucleinopathies.
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