Dihydropyrimidine dehydrogenase (DPD) is an enzyme that is involved in pyrimidine degradation. It is the initial and rate-limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and Tegafur-uracil.The sequence of the gene suggested that DPD has at least 3 distinct domains: a possible NADPH binding site and FAD-binding site in the N terminus, 2 motifs of putative iron/sulfur-binding sites near the C terminus, and a peptide domain corresponding to the uracil-binding site.Expression of the pig enzyme in E. coli catalyzed the reduction of uracil, thymine, and 5-fluorouracil (5FU) with kinetics approximating those published for the enzyme purified from mammalian liver.

Rabbit Deoxypyridinoline (DPD) ELISA Kit employs a two-site sandwich ELISA to quantitate DPD in samples. An antibody specific for DPD has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyDPD present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for DPD 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 DPD bound in the initial step. The color development is stopped and the intensity of the color is measured.

Rabbit Deoxypyridinoline (DPD) 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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