Anti-LDHD / D-lactate dehydrogenase

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Two naturally occurring forms of lactate dehydrogenase with similar but unique substrate specificities have been isolated in lower organisms including invertebrates, fungi, and prokaryotes. These dehydrogenase enzymes are L-lactate dehydrogenase and D-lactate dehydrogenase (LDHD) that are specific to the L and D isomers of lactate, respectively (PMID: 12127981). In lactic acid bacteria, LDHD plays a key role in anaerobic energy metabolism (PMID: 497162). Despite the identification of D-lactate and other D-2-hydroxyacids in prokaryotes, and the obvious connections and similarities to vertebrate metabolic pathways, very few mammalian D-2-hydroxyacid dehydrogenases have been found. LDHD has 2 isoforms with the molecular weight of 52 and 54kDa, and can be detected as 45-54 kDa. Protein function: Involved in D-lactate, but not L-lactate catabolic process. [The UniProt Consortium]