关键信息
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基因名
ADH4
- 应用
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别名
Alcohol dehydrogenase class II pi chain
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P08319
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表达区间
1-380aa
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分子量
67.2 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.
质检流程
相关产品
背景信息
The study of recombinant ADH4 (alcohol dehydrogenase 4), an enzyme belonging to the alcohol dehydrogenase family, is crucial due to its significant role in metabolizing alcohol and contributing to various physiological processes. ADH4 is primarily expressed in the human liver and has been associated with the metabolism of short-chain alcohols and retinol, influencing both energy production and fetal development. Understanding the structure and function of ADH4 at the molecular level can provide insights into its enzymatic activity, regulatory mechanisms, and potential implications in alcohol-related disorders. Furthermore, recombinant ADH4 can serve as a valuable tool in biotechnological applications, such as biosensors for alcohol detection or in the biotransformation of pharmaceutical compounds. Recent advances in genetic engineering techniques enable the production of high-yield recombinant ADH4, allowing for detailed biochemical characterization and exploration of its therapeutic potentials. This research lays the foundation for further studies aiming to manipulate ADH4 activity, which may lead to novel therapeutic strategies for alcohol dependence and other metabolic diseases.
