Aldehyde dehydrogenase (ALDH) superfamily is a ubiquitous group of enzymes found in all taxonomic domains. ALDH detoxifies endogenous and exogenous aldehydes, protecting cellular homeostasis and organismal functions. These enzymes are necessary for the synthesis of retinoic acid, betaine, and folate. Recent studies have reported high levels of ALDH found in cancer cells, suggesting that ALDH can act as a marker for cancer cells found in a wide variety of tissues including skin, prostate, lung, and neural tissues. Additionally, certain diseases can be identified when ALDH activity is absent. ALDH1A1 is vital for retinol synthesis and alcohol metabolism. ALDH1A1 active sites include an active cysteine residue, which catalyses the transformation of aldehydes into their respective carboxylic groups. ALDH1A1 amino acid sequence and function is highly conserved in humans and rodents.
References
Western blot image of human A431 (lane 1), HepG2 (lane 2), PC3 (lane 3), Jurkat (lane 4), bovine tubulin (lane 5), and recombinant human ALDH1A1 (lane 6). The blot was probed with mouse monoclonal ALDH1A1 M558 (lanes 1-6) at a dilution of 1:1,000.
*For more information, see UniProt Accession P00352
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
This kit contains:
