Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate DPEP2 in samples. An antibody specific for DPEP2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyDPEP2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for DPEP2 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 DPEP2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:DPEP2 belongs to the membrane-bound dipeptidase (EC 3.4.13.19) family. These enzymes hydrolyze a variety of dipeptides, including leukotriene D4, the beta-lactam ring of some antibiotics, and cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation.The deduced 578-amino acid mouse protein contains several residues conserved among MBDs, including 6 cysteines, 3 histidines, and a glutamic acid that is important for catalytic activity. Mouse and human MBD2 share 80% amino acid identity. Spleen, liver, and skeletal muscle expressed low Mbd2 levels, and no expression was detected in kidney and brain. Phospholipase treatment released Mbd2 from transfected COS-7 cell membranes, indicating that Mbd2 is anchored to the membrane through glycosylphosphatidylinositol modification.
