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 crucial enzyme involved in the hydrolysis of acetylcholine and various other ester-containing compounds, playing a vital role in the regulation of neurotransmission and drug metabolism. The enzyme's significance extends to clinical applications, particularly in the detoxification of certain organophosphate compounds and as a biomarker for various neurological disorders. Recent research has increasingly focused on the production of recombinant BCHE to overcome limitations associated with native enzyme sources, such as low yield and stability issues. Recombinant BCHE offers several advantages, including improved enzymatic activity, enhanced stability under varying conditions, and the potential for large-scale production through biotechnological methods. Advances in genetic engineering and protein expression systems have facilitated the generation of recombinant BCHE with tailored properties suitable for industrial and therapeutic applications. Understanding the structure-function relationship of BCHE is also essential, as modifications can optimize its effectiveness in clinical scenarios, particularly in organophosphate poisoning treatment and as a potential therapeutic target in neurodegenerative diseases. Overall, the exploration of recombinant BCHE represents a significant step toward harnessing its potential in both research and clinical settings, providing a platform for further advancements in pharmacology and toxicology.
