The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity.
Anti-human ALDH5A1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ALDH5A1 protein 48-535 amino acids purified from E. coli.
ALDH5A1 is a mitochondrial NAD(+)-dependent succinic semialdehyde dehydrogenase, which is a member of the aldehyde dehydrogenase family of proteins. The ALDH5A1 protein functions as a mediator to the NADP+-dependent oxidation of aldehydes into acids and has an imperative role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH5A1 is expressed in various tissues, including the liver, heart, lung, brain, kidney and placenta. Deficiency in the ALDH5A1 enzyme, known as 4-hydroxybutyricaciduria, is a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA). In response to this defect, physiologic fluids from patients accumulate GHB, which is a compound with numerous neuromodulatory properties.
