Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate ZG16B in samples. An antibody specific for ZG16B has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyZG16B present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for ZG16B 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 ZG16B bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:ZG16b/PAUF has recently been found to play a role in gene regulation and cancer metastasis. However, the detailed functions of ZG16p and ZG16b remain to be clarified. ZG16p has a Jacalin-related β-prism fold, the first to be reported among mammalian lectins. The putative sugar-binding site of ZG16p is occupied by a glycerol molecule, mimicking the mannose bound to Jacalin-related mannose-binding-type plant lectins such as Banlec. ZG16b also has a β-prism fold, but some amino acid residues of the putative sugar-binding site differ from those of the mannose-type binding site suggesting altered preference. A positively charged patch, which may bind sulfated groups of the glycosaminoglycans, is located around the putative sugar-binding site of ZG16p and ZG16b. The sugar-binding site and the adjacent basic patch of ZG16p and ZG16b cooperatively form a functional glycosaminoglycan-binding site.
