Analytical Data
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基因名
Butyrylcholinesterase/BCHE
- Application
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别名
Acylcholine acylhydrolaseButyrylcholine esteraseCholine esterase IIPseudocholinesterase
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种属
Dog
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表达系统
Yeast
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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
P32750
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表达区间
1-141aa
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分子量
17.1 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
Butyrylcholinesterase (BChE) is a key enzyme in the hydrolysis of neurotransmitters such as acetylcholine, playing a vital role in the cholinergic system and maintaining synaptic cleft homeostasis. Its relevance extends beyond neurotransmission; BChE is also implicated in detoxification processes, specifically in the hydrolysis of various xenobiotics and organophosphate compounds, making it a focal point in studies of neuroprotection and antidote development. Research has highlighted BChE's potential therapeutic applications in treating Alzheimer's disease and other cognitive disorders, as well as its role in mitigating the effects of nerve agents. The recombinant production of BChE has garnered interest due to the challenges in obtaining the enzyme from natural sources, where it exists in relatively low concentrations. Advances in genetic engineering and recombinant DNA technology now enable the efficient expression of BChE in various host systems, paving the way for the production of this enzyme in quantities adequate for therapeutic and research applications. Additionally, studies on the structural and functional properties of recombinant BChE can lead to the development of novel inhibitors or modulators, contributing to precision medicine approaches in neuropharmacology. Understanding BChE's kinetics, specificity, and interaction with small molecules is crucial for designing effective treatments against neurotoxic agents and neurodegenerative diseases, underscoring the importance of continued research in this area.
