ALDH1A1 Human, Active
Description
Product Specs
Product Science Overview
Aldehyde Dehydrogenase 1A1 (ALDH1A1) is a member of the aldehyde dehydrogenase family of enzymes. These enzymes play a crucial role in the metabolism of aldehydes, converting them into their corresponding carboxylic acids. ALDH1A1 is particularly significant due to its involvement in the oxidation of retinaldehyde to retinoic acid, a vital process in the regulation of gene expression during embryonic development and in adult tissues.
The human recombinant ALDH1A1 protein is typically produced in Escherichia coli (E. coli) expression systems. It is a single, non-glycosylated polypeptide chain with a molecular weight of approximately 54.8 kDa and consists of 501 amino acids . The enzyme is predominantly found in the cytosol of cells and is expressed in various tissues, including the liver, brain, testis, eye lens, and cornea .
ALDH1A1 is involved in the major oxidative pathway of alcohol metabolism. It catalyzes the oxidation of aldehydes to their corresponding carboxylic acids, using NAD+ as a cofactor. This reaction is crucial for detoxifying aldehydes, which can be highly reactive and toxic to cells. The enzyme’s activity is measured by its ability to produce NADH during the oxidation of substrates such as propionaldehyde .
There are two major isoforms of aldehyde dehydrogenase in the liver: cytosolic and mitochondrial. These isoforms can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations . Interestingly, genetic variability in the ALDH1A1 gene can lead to differences in enzyme activity among individuals. For example, approximately 50% of individuals of East Asian descent lack the mitochondrial isoform, which is associated with a higher frequency of acute alcohol intoxication .
Recombinant ALDH1A1 is widely used in research to study its role in alcohol metabolism, retinoic acid biosynthesis, and its potential involvement in various diseases, including cancer. The enzyme’s activity can be assessed using various biochemical assays, and its recombinant form allows for detailed structural and functional studies .
