ALDH2 Mouse
Description
Product Specs
Product Science Overview
Aldehyde dehydrogenase 2 (ALDH2) is a crucial enzyme that belongs to the aldehyde dehydrogenase family. This family of enzymes is responsible for the detoxification of aldehydes, which are highly reactive and potentially toxic compounds. ALDH2, in particular, plays a significant role in the metabolism of acetaldehyde, a byproduct of alcohol metabolism, converting it into the less toxic acetic acid .
ALDH2 is a mitochondrial enzyme, meaning it is located within the mitochondria of cells. The enzyme functions as a homotetramer, consisting of four identical subunits. Each subunit contains an active site where the catalytic conversion of aldehydes takes place. The enzyme’s activity is crucial for preventing the accumulation of toxic aldehydes, which can cause cellular damage and contribute to various diseases .
There are several genetic variants of ALDH2 that can affect its enzymatic activity. One well-known variant is the ALDH2*2 allele, which is prevalent in East Asian populations. This variant results in a significantly reduced enzymatic activity, leading to the accumulation of acetaldehyde after alcohol consumption. This accumulation causes the characteristic “alcohol flush reaction,” where individuals experience facial flushing, nausea, and other symptoms .
ALDH2 has been implicated in various diseases, including alcohol-related liver disease, cardiovascular diseases, and certain types of cancer. The enzyme’s ability to detoxify reactive aldehydes makes it a potential target for therapeutic interventions. For example, enhancing ALDH2 activity could help mitigate the damage caused by oxidative stress and reduce the risk of developing aldehyde-related diseases .
Recombinant ALDH2, particularly from mouse models, is widely used in research to study the enzyme’s structure, function, and role in disease. Mouse recombinant ALDH2 is produced by expressing the mouse ALDH2 gene in a suitable host system, such as bacteria or yeast. This allows researchers to obtain large quantities of the enzyme for biochemical and structural studies .
