Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate TMEFF2 in samples. An antibody specific for TMEFF2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyTMEFF2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for TMEFF2 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 TMEFF2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:The deduced 368-amino acid TRa protein contains 2 follistatin-like domains and a conserved EGF-like domain. It also has a predicted N-terminal signal peptide, a transmembrane domain, a cytosolic tail G protein-activating motif, and potential sites for N-linked glycosylation and glycosaminoglycan attachment. Unlike other EGF/NRG family members, TRa has a histidine replacing a conserved arginine essential for EGF receptor recognition. The TRb and TRc proteins contain 418 and 379 amino acids, respectively, and differ from one another and TRa in the cytoplasmic domain. Northern blot analysis detected expression of approximately 2.2- and 3.1-kb TR transcripts predominantly in brain. The 374-amino acid TMEFF2 protein shares approximately 36% and 99% sequence identity with TMEFF1 and mouse Tmeff2, respectively.
