Aldehyde Dehydrogenase Polyclonal Antiserum

Aldehyde dehydrogenase (ALDH) is an enzyme that catalyzes the oxidation of various aldehydes to their corresponding carboxylic acid.¹ There are 19 human ALDH isozymes, which have varying expression levels, subcellular localization, tissue distribution, cofactor preference, and substrate specificity.² 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.^2,1 It also catalyzes the catabolism of thromboxane B₂ (TXB₂; Item No. 19030) to 11-dehydro TXB₂ (Item No. 19500).³ Mutations in the genes encoding ALDH isozymes are associated with a variety of human conditions, including alcohol intolerance, Parkinson's disease, and gout.¹ 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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1. Shortall, K., Djeghader, A., Magner, E., et al. Insights into aldehyde dehydrogenase enzymes: A structural perspective. Front. Mol. Biosci. 8, 659550 (2021).

2. Vassalli, G. Aldehyde dehydrogenases: Not just markers, but functional regulators of stem cells. Stem Cells Int. 3904645 (2019).

3. Westlund, P., Fylling, A.C., Cederlund, E., et al. 11-Hydroxythromboxane B₂ dehydrogenase is identical to cytosolic aldehyde dehydrogenase. FEBS Lett. 345(2-3), 99-103 (1994).