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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human ADH5 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 41.89 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Met1-Ile374 |
Aliases /Synonyms | ADHX, ADH5, FDH, Alcohol dehydrogenase class chi chain, Alcohol dehydrogenase class-3, Alcohol dehydrogenase class-III, GSH-FDH, S-(hydroxymethyl)glutathione dehydrogenase, FALDH, Glutathione-dependent formaldehyde dehydrogenase, Alcohol dehydrogenase 5 |
Reference | ARO-P12575 |
Note | For research use only. |
Recombinant Human ADH5 Protein, also known as Alcohol Dehydrogenase 5, is a type of protein that is produced through genetic engineering techniques. It is a highly specialized enzyme that plays a crucial role in the metabolism of alcohol in the human body. This protein has a specific structure and activity that allows it to efficiently catalyze the conversion of alcohol into acetaldehyde, a toxic substance that is then further metabolized into harmless compounds. In this article, we will delve deeper into the structure, activity, and applications of Recombinant Human ADH5 Protein.
Recombinant Human ADH5 Protein is a homodimer, meaning it is composed of two identical subunits. Each subunit consists of 375 amino acids and has a molecular weight of approximately 40 kDa. The protein has a globular shape with a central active site where the catalytic reaction takes place. The active site contains a zinc ion, which is essential for the protein’s activity. The structure of Recombinant Human ADH5 Protein is highly conserved across different species, indicating its vital role in alcohol metabolism.
The primary function of Recombinant Human ADH5 Protein is to catalyze the oxidation of alcohol to acetaldehyde. This process involves the transfer of a hydride ion from alcohol to the coenzyme NAD+, forming NADH and acetaldehyde. The enzyme’s activity is highly specific, as it can only bind to and metabolize certain types of alcohol, such as ethanol, methanol, and propanol. This specificity is due to the complementary shape of the enzyme’s active site and the alcohol molecule.
Apart from its role in alcohol metabolism, Recombinant Human ADH5 Protein also has other activities. It has been shown to have a protective effect against oxidative stress by reducing the levels of reactive oxygen species in cells. Additionally, the enzyme has been found to play a role in the metabolism of other compounds, such as retinol and xenobiotics.
Recombinant Human ADH5 Protein has various applications in both research and industrial settings. In research, the enzyme is used to study the mechanism of alcohol metabolism and its role in diseases such as alcoholism. It is also used in drug discovery and development, as many drugs are metabolized by ADH enzymes.
In the industrial sector, Recombinant Human ADH5 Protein is used in the production of biofuels. The enzyme is used to convert ethanol into acetaldehyde, which is then further converted into ethylene, a key component in the production of plastics. This process is more efficient and environmentally friendly compared to traditional methods, making Recombinant Human ADH5 Protein a valuable tool in the biotechnology industry.
In summary, Recombinant Human ADH5 Protein is a specialized enzyme with a specific structure and activity that allows it to efficiently metabolize alcohol and other compounds. Its applications in research and industry make it a valuable tool in understanding alcohol metabolism and developing new technologies. Further studies on this enzyme could lead to a better understanding of alcohol-related diseases and the development of new treatments.
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