Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SLC12A4 in samples. An antibody specific for SLC12A4 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySLC12A4 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SLC12A4 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 SLC12A4 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:The full-length sequence was obtained from EST clones and by RT-PCR of HEK293 cell RNA. The 1,085-amino acid KCC1 protein is 24 to 25% identical to NKCC1 and SLC12A3 and shares 97% identity with rabbit KCC1. The overall structure of KCC1 is similar to that of other cation-chloride cotransporters, with 12 predicted transmembrane regions, a large extracellular loop with potential N-linked glycosylation sites, and cytoplasmic N- and C-terminal domains. Northern blot analysis revealed that KCC1 is expressed ubiquitously. KCC1 exhibits the functional properties of the red cell K-Cl cotransporter, including stimulation by swelling and N-ethylmaleimide, and low affinities for rubidium, chloride, and bumetanide.
