Aldehyde dehydrogenase (ALDH) is an enzyme that catalyzes the oxidation of various aldehydes to their corresponding carboxylic acid.{60733} There are 19 human ALDH isozymes, which have varying expression levels, subcellular localization, tissue distribution, cofactor preference, and substrate specificity.{60734} ALDH exists as a homodimer or homotetramer and is composed of a cofactor-binding domain, which binds NAD+ or NADP+, a catalytic domain, and an oligomerization domain. ALDH has protective roles in alcohol detoxification and oxidative stress, regulatory roles in the function of normal stem cells and tumor-initiating stem-like cells, and a biosynthetic role in the formation of retinoic acid.{60734,60733} It also catalyzes the catabolism of thromboxane B2 (TXB2; Item No. 19030) to 11-dehydro TXB2 (Item No. 19500).{20448} Mutations in the genes encoding ALDH isozymes are associated with a variety of human conditions, including alcohol intolerance, Parkinson's disease, and gout.{60733} Cayman's Aldehyde Dehydrogenase Polyclonal Antiserum can be used for Western blot (WB) applications. The antibody recognizes ALDH at 55 kDa from human and mouse samples.
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Aldehyde Dehydrogenase Polyclonal Antiserum
160720-1
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Aldehyde Dehydrogenase Polyclonal Antiserum
160720-1
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