Alcohol dehydrogenase Protein, Lentilactobacillus curieae

The alcohol dehydrogenase protein is part of the zinc-containing alcohol dehydrogenase family and catalyzes the oxidation of alcohol, which is critical in various metabolic processes. It is primarily active in the liver, where it converts ethanol into acetaldehyde during the breakdown of ethanol. Alcohol dehydrogenase Protein, Lentilactobacillus curieae is the recombinant Alcohol dehydrogenase protein, expressed by E. coli , with tag free. The total length of Alcohol dehydrogenase Protein, Lentilactobacillus curieae is 345 a.a., .

Alcohol dehydrogenase protein belongs to the zinc-containing alcohol dehydrogenase family, playing a crucial role in catalyzing the oxidation of alcohols to aldehydes or ketones. This protein is involved in various metabolic processes, including the breakdown of ethanol in the liver, where it converts ethanol to acetaldehyde. Additionally, alcohol dehydrogenase protein participates in the metabolism of other alcohols and xenobiotics, contributing to their detoxification and elimination from the body. Its enzymatic activity and expression levels can be influenced by genetic variations, environmental factors, and alcohol consumption patterns, thereby affecting an individual's susceptibility to alcohol-related disorders and responses to alcohol exposure. Overall, alcohol dehydrogenase protein represents an essential component in alcohol metabolism and the maintenance of cellular homeostasis.

Others

E. coli

Tag Free

A0A1S6QHZ8 (M1-K345)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.