A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.
L-LDH, Recombinant (Porcine)
High purity L-Lactate dehydrogenase (Porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
In 3.2 M ammonium sulphate.
Enzyme Commission Number
335 U/mg protein at pH 7.0 and 37°C.
One Unit of L-lactate dehydrogenase is defined as the amount of enzyme required to produce one µmole of NAD+ from NADH per minute.
up to 55°C
> 2 years at 4°C
For assay, this enzyme should be diluted in Tris. HCl buffer (10 mM), pH 7.5 containing 1 mg/mL BSA. Swirl to mix the enzyme immediately prior to use.
EC 220.127.116.11; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate