Analytical Data
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基因名
SNCA
- Application
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别名
SNCA; Alpha-synuclein
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种属
Pig
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q3I5G7
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表达区间
1-140aa
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分子量
18.6 kDa
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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
The study of SNCA (Alpha-synuclein) recombinant proteins has gained significant attention due to their pivotal role in neurodegenerative diseases, particularly Parkinson's disease. Alpha-synuclein is a neuronal protein that is predominantly found in the brain, where it is involved in synaptic function and neurotransmitter release. Misfolding and aggregation of SNCA into insoluble fibrils are hallmark features of Parkinson’s disease and certain other synucleinopathies, leading to the formation of Lewy bodies, which are toxic to neurons. Understanding the structure and dynamics of SNCA at the molecular level is crucial for elucidating the mechanisms underlying its pathogenesis. Researchers utilize recombinant techniques to produce SNCA protein in a controlled environment, enabling detailed studies of its biochemical properties and aggregation behavior. These investigations are essential for developing therapeutic strategies aimed at mitigating SNCA-related toxicities, such as small molecules that can prevent aggregation or enhance the natural clearance of misfolded proteins. Additionally, recombinant SNCA is instrumental in the development of animal models and in vitro systems that replicate the disease state, facilitating drug discovery and the exploration of potential interventions. Overall, the study of SNCA recombinant proteins provides critical insights into the molecular pathways of neurodegeneration and holds promise for novel therapeutic approaches in targeting synucleinopathies.












