MDH2 Recombinant Mouse mAb (S-5411)

MDH2 (malate dehydrogenase 2) is an NAD⁺-dependent dehydrogenase encoded by the nuclear gene MDH2 and localized to the mitochondrial matrix, where it plays a central role in eukaryotic energy metabolism. It catalyzes the reversible redox reaction between L-malate and oxaloacetate, serving as a key node connecting the tricarboxylic acid cycle with the malate-aspartate shuttle system—the former drives aerobic respiration for energy production, while the latter transports reducing equivalents from the cytosol into mitochondria for oxidation. Human MDH2 consists of approximately 337 amino acids and functions as a homodimer; its active site contains a critical proton-accepting residue (such as Arg102), and phosphate group binding can induce closure of the active loop, thereby stabilizing the substrate and cofactor to promote catalysis. Notably, MDH2 activity is positively regulated by acetylation, a mechanism involved in the dynamic regulation of metabolic networks. At the clinical level, the dual role of MDH2 has attracted increasing attention: on the one hand, its germline mutations can cause pediatric neurological disorders such as developmental and epileptic encephalopathy; on the other hand, MDH2 is upregulated in various tumors and is regarded as a promising anticancer target, while its mutations are also associated with the metabolic disturbances of recurrent focal segmental glomerulosclerosis.