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D-Lactate dehydrogenase (D-LDH), an oxidoreductase, catalyzes the oxidation of D-lactate to pyruvate leveraging NAD+ or NADP+ as acceptors and acting on the donor CH-OH group. Predominantly found in bacteria and fungi, it is frequently utilized in biochemical research [1].

Lactate Dehydrogenase (LDH), derived from Porcine Heart, also known as Lactic Dehydrogenase, serves as a biological material or organic compound utilized in life science research.

L-Lactate dehydrogenase (LAD) is an oxidoreductase enzyme in the anaerobic metabolic pathway and the gluconeogenic pathway, and is found in a wide range of tissues in the body.

L-Lactate Dehydrogenase, bovine muscle, is a redox enzyme that catalyzes the reversible conversion of lactate to pyruvate while simultaneously reducing NAD+ to NADH.

Lactate Dehydrogenase (LDH), sourced from Chicken Heart (LAD, LD, L-LDH, (S)-Lactate, LDH), serves as a biomaterial or organic compound useful for life science research.