Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate TMPRSS9 in samples. An antibody specific for TMPRSS9 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyTMPRSS9 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for TMPRSS9 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 TMPRSS9 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:TMPRSS9 contains a predicted type II transmembrane segment, an LDLR domain, and 3 protease domains, which they called serase-1, -2, and -3. The C-terminal serase-3 domain is predicted to be catalytically inactive. TMPRSS9 shares approximately 80% amino acid identity with both mouse and rat Tmprss9, and the protease domains share 40% to 48% amino acid identity with matriptase (ST14) and matriptase-2 (TMPRSS6). Northern blot analysis detected a 5.4-kb transcript in all adult tissues examined, fetal kidney, liver, lung, and brain, and in several tumor cell lines. Minor transcripts of 3.8 and 2.4 kb were detected in adult skeletal muscle, liver, placenta, and heart. Immunofluorescence microscopy localized TMPRSS9 to the plasma membrane in COS-7 cells.
