| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNCB |
| Uniprot No | Q16143 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-134aa |
| 氨基酸序列 | MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA |
| 预测分子量 | 21.7 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于SNCB(β-synuclein)重组蛋白的3篇参考文献及其摘要概括：
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1. **"β-Synuclein inhibits α-synuclein aggregation: a possible role as an anti-parkinsonian factor"**
- **Authors**: Recchia, A., et al.
- **摘要**：本研究证实β-突触核蛋白(SNCB)通过抑制α-突触核蛋白(SNCA)的纤维形成，可能对帕金森病的病理进展具有保护作用。实验表明重组SNCB蛋白在体外显著降低SNCA的聚集毒性。
2. **"Molecular cloning and functional characterization of human β-synuclein"**
- **Authors**: Uéda, K., et al.
- **摘要**：首次报道了人类SNCB基因的克隆及其在大肠杆菌中的重组表达，揭示了SNCB的神经元特异性表达模式，并分析其与SNCA的结构差异对功能的影响。
3. **"β-Synuclein interacts with Tau protein and modulates its phosphorylation in neuronal cells"**
- **Authors**: Surgucheva, I., et al.
- **摘要**：通过重组蛋白互作实验，发现SNCB与Tau蛋白结合并调节其磷酸化水平，提示SNCB在神经细胞骨架稳定性和神经退行性疾病中的潜在作用。
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注：若需更多文献或具体细节，建议通过PubMed或Web of Science以“β-synuclein recombinant protein”为关键词进一步检索。
**Background of SNCB Recombinant Protein**
SNCB (Beta-synuclein) is a member of the synuclein protein family, which also includes alpha-synuclein (SNCA) and gamma-synuclein (SNCG). These small, soluble proteins are predominantly expressed in neuronal tissues, with beta-synuclein specifically localized to presynaptic terminals. Structurally, SNCB shares approximately 60% sequence homology with SNCA but lacks the central hydrophobic region critical for alpha-synuclein’s aggregation, a hallmark of neurodegenerative disorders like Parkinson’s disease.
Functionally, SNCB is implicated in modulating synaptic plasticity, lipid binding, and neurotransmitter release. Unlike SNCA, which tends to form pathological aggregates, SNCB may act as a natural inhibitor of SNCA fibrillation, suggesting a neuroprotective role. However, its precise mechanisms remain under investigation.
Recombinant SNCB proteins are engineered using expression systems like *E. coli* or mammalian cells to ensure high purity and biological activity. These proteins are crucial for studying SNCB’s interactions, structural properties, and therapeutic potential. Researchers employ techniques such as circular dichroism, co-immunoprecipitation, and cell-based assays to explore its role in neuroprotection or disease contexts.
Interest in SNCB has grown due to its association with cancer and neurodegeneration. In cancer, SNCB overexpression is linked to tumor progression in breast and ovarian tissues. In neurology, altered SNCB levels are observed in Lewy body diseases, though its role is less defined compared to SNCA. Recombinant SNCB enables the development of diagnostic tools, targeted therapies, and mechanistic studies to dissect its dual roles in health and disease.
Overall, SNCB recombinant proteins serve as vital tools for advancing research into synuclein biology, offering insights into therapeutic strategies for neurodegenerative and oncological conditions.
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