ADH5 Human

Recombinant Human Alcohol Dehydrogenase 5 is typically produced in E. coli and features a N-Terminal His-tag. The recombinant protein corresponds to the amino acids 1-374 of the human ADH5 . The theoretical molecular weight of this protein is approximately 42.3 kDa, although the observed molecular weight may vary due to post-translational modifications and other experimental factors .

ADH5 is unique among the alcohol dehydrogenase family because it has virtually no activity for ethanol oxidation. Instead, it exhibits high activity for the oxidation of long-chain primary alcohols and S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione . This enzyme plays a crucial role in cellular metabolism by eliminating formaldehyde, a potent irritant and sensitizing agent that can cause lacrimation, rhinitis, pharyngitis, and contact dermatitis .

Recombinant Human Alcohol Dehydrogenase 5 is used in various research applications, including studies on formaldehyde metabolism, detoxification processes, and the role of alcohol dehydrogenases in human health and disease . Its ability to metabolize formaldehyde makes it an important tool for understanding cellular responses to this toxic compound.

The recombinant protein is typically stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain the protein’s stability and activity .