Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate TNFRSF10C in samples. An antibody specific for TNFRSF10C has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyTNFRSF10C present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for TNFRSF10C 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 TNFRSF10C bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:TRAILR3, a novel member of the TRAIL receptor family. Although the open reading frame potentially encoded a 299-amino acid protein, the authors suggested that translation begins at amino acid 41, yielding a protein of 259 amino acids. TRAILR3 contains a predicted signal sequence, 2 of the 4 cysteine-rich pseudorepeats characteristic of the extracellular domain of members of the TNF receptor family, an extracellular linker sequence, and a short, hydrophobic C-terminal sequence. Transient expression studies showed that TRAILR3 is a plasma membrane-bound protein capable of high affinity interaction with the TRAIL ligand. In contrast to TRAILR1 and TRAILR2, TRAILR3 appears to be glycosylphosphatidylinositol-linked and lacks a cytoplasmic region, including the death domain.
