Analytical Data
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基因名
SNCA Pre-formed Fibrils
- Application
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别名
Alpha-Synuclein; Non-A Beta Component of AD Amyloid; Non-A4 Component of Amyloid Precursor; NACP; SNCA; NACP; PARK1
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种属
Human
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表达系统
E. coli
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标签
C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P37840-1
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表达区间
M1-A140,A53T
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SNCA pre-formed fibrils (PFFs) have garnered significant attention in neuroscientific research due to their role in the pathogenesis of neurodegenerative disorders, particularly Parkinson's disease. Alpha-synuclein (SNCA), a presynaptic protein predominantly found in the brain, is implicated in synaptic function and neurotransmitter release. However, misfolding and aggregation of SNCA into fibrillar structures are linked to neurotoxicity and neuronal cell death, hallmark features of Parkinson's disease. The generation of recombinant SNCA pre-formed fibrils provides a valuable tool for studying the molecular mechanisms underlying alpha-synuclein aggregation and its pathological effects. Researchers can use these PFFs to induce aggregation in cellular and animal models, thus facilitating the exploration of disease progression, potential biomarkers, and therapeutic targets. Furthermore, the study of SNCA PFFs can shed light on the propagation of misfolded proteins across neural networks, enhancing our understanding of intercellular transmission of neurodegenerative conditions. Insights gained from this research may lead to the development of novel strategies for intervention and treatment, addressing the urgent need for effective therapies for patients affected by Parkinson's disease and related synucleinopathies. Overall, SNCA pre-formed fibrils represent a critical focus area in efforts to unravel the complexities of protein misfolding and aggregation in neurodegenerative diseases, bridging basic science with translational research.












