Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of lactate to pyruvic acid and back, as it converts NAD+ to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH exist in four distinct enzyme classes. This article is specifically about the NAD(P)-dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase (cytochrome)) and L-lactate (L-lactate dehydrogenase (cytochrome)). LDH is expressed extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure.

Human L-Lactate Dehydrogenase (L-LDH) ELISA Kit employs a two-site sandwich ELISA to quantitate L-LDH in samples. An antibody specific for L-LDH has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyL-LDH present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for L-LDH is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of L-LDH bound in the initial step. The color development is stopped and the intensity of the color is measured.

Human L-Lactate Dehydrogenase (L-LDH) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.

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