Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate DPP8 in samples. An antibody specific for DPP8 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyDPP8 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for DPP8 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 DPP8 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Dipeptidyl peptidase 8 is member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond.
The encoded protein shares similarity with dipeptidyl peptidase IV in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described.The deduced 882-amino acid DPP8 protein shares about 27% sequence identity with DPP4 and FAP; unlike these proteins, however, DPP8 has no transmembrane domain and no N- or O-linked glycosylation sites.
