ALDH5A1 (Aldehyde Dehydrogenase 5 Family Member A1), also known as succinate semialdehyde dehydrogenase (SSADH), is a mitochondrial enzyme critical in the catabolism of the neurotransmitter γ-aminobutyric acid (GABA). It catalyzes the oxidation of succinate semialdehyde to succinate, linking GABA metabolism to the tricarboxylic acid (TCA) cycle. ALDH5A1 deficiency, a rare autosomal recessive disorder, causes accumulation of toxic metabolites like γ-hydroxybutyrate (GHB), leading to neurodevelopmental impairments, epilepsy, and hypotonia.
Antibodies targeting ALDH5A1 are essential tools for studying its expression, localization, and function in biological systems. They are widely used in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to investigate ALDH5A1's role in neurological disorders, metabolic pathways, and mitochondrial dysfunction. These antibodies are typically raised against specific epitopes, such as recombinant protein fragments or synthetic peptides derived from the human ALDH5A1 sequence. Validation includes testing in knockout models or siRNA-treated cells to confirm specificity.
Research applications focus on understanding ALDH5A1's involvement in neurodegenerative diseases, metabolic syndromes, and its potential as a therapeutic target. Commercial antibodies vary in clonality (monoclonal/polyclonal), host species, and conjugates, enabling flexibility in experimental design. Reliable detection of ALDH5A1 aids in diagnosing genetic disorders and elucidating mechanisms underlying GABAergic neurotransmission defects.