ADH1A Human

ADH1A is predominantly active in the liver, especially during fetal and infant stages. Its primary physiological function is the elimination of ethanol produced by microorganisms in the intestinal tract . As individuals age, the activity of ADH1A decreases, becoming only weakly active during adulthood .

The human recombinant form of ADH1A is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 395 amino acids. It has a molecular mass of approximately 42 kDa . The recombinant enzyme is often fused to a 20 amino acid His-tag at the N-terminus to facilitate purification through chromatographic techniques .

For optimal stability, the ADH1A solution should be stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to freeze the solution at -20°C, preferably with a carrier protein such as 0.1% HSA (Human Serum Albumin) or BSA (Bovine Serum Albumin) to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity.

ADH1A is widely used in laboratory research, particularly in studies related to ethanol metabolism and its effects on the human body. It is also utilized in various biochemical assays to understand the enzyme’s kinetics and its interaction with different substrates and inhibitors .

The ADH1A gene is located on the long arm of chromosome 4 and is part of a cluster that includes six additional alcohol dehydrogenase genes. These genes encode different subunits of the enzyme, including alpha, beta, and gamma subunits, which can form various homo- and heterodimers . Mutations in the ADH1A gene have been associated with variations in certain personality traits and substance dependence .