ADH1A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
ADH1A is composed of several homo- and heterodimers of alpha, beta, and gamma subunits. The alpha subunit, encoded by the ADH1A gene, is particularly significant in the liver during early fetal development but shows only weak activity in adult liver . The enzyme’s primary function is to oxidize alcohols to aldehydes, using the coenzyme NAD (Nicotinamide Adenine Dinucleotide) as a cofactor .
The recombinant form of ADH1A is produced in Sf9 Baculovirus cells. This method involves the expression of the human ADH1A gene in insect cells, resulting in a glycosylated polypeptide chain containing 381 amino acids and having a molecular mass of approximately 40.6 kDa . The recombinant protein is often used in research to study the enzyme’s properties and its role in alcohol metabolism.