Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SLC1A7 in samples. An antibody specific for SLC1A7 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySLC1A7 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SLC1A7 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 SLC1A7 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:EAAT5-mediated L-glutamate uptake was sodium- and voltage-dependent and chloride-independent. Transporter currents elicited by glutamate were also sodium- and voltage-dependent, but ion substitution experiments suggested that this current was largely carried by chloride ions.Although EAAT5 shares the structural homologies of the EAAT family, 1 novel feature of the EAAT5 sequence is a C-terminal motif previously identified in N-methyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering. EAAT5 has 46% amino acid sequence identity with EAAT1 (SLC1A3), 43% identity with EAAT4 (SLC1A6), 37% identity with EAAT3 (SLC1A1), and 36% identity with EAAT2 (SLC1A2).