Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate PRSS22 in samples. An antibody specific for PRSS22 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyPRSS22 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for PRSS22 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 PRSS22 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:The deduced 317-amino acid protein contains an N-terminal hydrophobic leader peptide, followed by a propeptide sequence and the serine protease domain, which has the catalytic triad of histidine, aspartic acid, and serine. PRSS22 also has 2 cysteines that form a disulfide bond linking the propeptide and the catalytic domain following proteolytic activation, and it has an N-glycosylation site. PRSS22 lacks a number of residues required by other tryptases to form tetramers. RNA dot blot analysis detected abundant PRSS22 expression in adult esophagus and trachea, with lower levels in adult placenta, pancreas, prostate, and thyroid, and in fetal kidney and lung. There was little to no expression in other tissues examined. Enzymatically active PRSS22 was secreted from a human epithelial cell line and from transfected COS-7 cells.
