ALDH1A1 Human

ALDH1A1 is a homotetrameric protein, meaning it consists of four identical subunits. Each subunit has a molecular mass of approximately 56 kDa . The enzyme is NAD(P)±dependent, which means it requires nicotinamide adenine dinucleotide (phosphate) as a cofactor to carry out its catalytic activity . ALDH1A1 has a high affinity for the oxidation of both all-trans and 9-cis-retinal molecules, which are forms of vitamin A .

The ALDH1A1 gene is located on the long arm of human chromosome 9, specifically in subregion 13 of region 21 . The enzyme is expressed in various tissues, including the liver, where it plays a significant role in alcohol metabolism. There are two major liver isoforms of aldehyde dehydrogenase: cytosolic and mitochondrial. These isoforms can be distinguished by their electrophoretic mobility, kinetic properties, and subcellular localization .

Recombinant human ALDH1A1 is produced using an expression system, typically in Escherichia coli (E. coli). The recombinant protein is often tagged with a histidine tag (6-His tag) to facilitate purification . The recombinant form of ALDH1A1 retains its enzymatic activity and is used in various research applications, including studies on alcohol metabolism, oxidative stress, and cancer .

ALDH1A1 is widely studied for its role in cancer. It is considered a marker for cancer stem cells and has been implicated in drug resistance. The enzyme’s ability to detoxify aldehydes and its involvement in retinoic acid signaling pathways make it a target for cancer therapy research . Additionally, ALDH1A1 is used in studies related to alcohol metabolism and the effects of oxidative stress on cells .

Recombinant ALDH1A1 is typically supplied as a filtered solution in a buffer containing Tris, NaCl, DTT, and glycerol. It is shipped with dry ice and should be stored at -70°C to maintain its stability. The enzyme should be handled carefully to avoid repeated freeze-thaw cycles, which can reduce its activity .