Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate LRP10 in samples. An antibody specific for LRP10 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyLRP10 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for LRP10 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 LRP10 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Proteins with EGF-like domains often consist of more than 1,000 amino acids, have multiple copies of the EGF-like domain, and contain additional domains known to be involved in specific protein-protein interactions. The predicted partial LRP4 protein contains 2 EGF-like domains, a calcium binding-type EGF-like domain, 3 LDL receptor-type EGF-like domains, 4 YWTD spacer regions, a transmembrane domain, a cytoplasmic NPXY motif, which is required for clustering and internalization of LDL receptors, and a cytoplasmic tSXV motif, which anchors proteins with a PDZ domain. The sequence and domain organization of LRP4 shows significant similarities to those of members of the LDL receptor family. Northern blot analysis detected rat Megf7 expression in several regions of the brain.