Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SCG2 in samples. An antibody specific for SCG2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySCG2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SCG2 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 SCG2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:SCG2 is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. Studies in rodents suggest that the full-length protein, secretogranin II, is involved in the packaging or sorting of peptide hormones and neuropeptides into secretory vesicles. The full-length protein is cleaved to produce the active peptide secretoneurin, which exerts chemotaxic effects on specific cell types, and EM66, whose function is unknown.SCG2 also has 9 potential dibasic cleavage sites, an N-glycosylation site not found in the bovine protein, and a putative sulfation site (tyr121). SCG2 was predicted to assume a secondary structure of alternating helix and turn structures over 45% and 40% of its length, respectively. The authors suggested that this structure may coordinate calcium.