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- Tel: 858.663.9055
- Email: info@nsjbio.com
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.
Optimal dilution of the LDHD antibody should be determined by the researcher.
An E.coli-derived human recombinant protein (amino acids R56-Q498) was used as the immunogen for the LDHD antibody.
After reconstitution, the LDHD antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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