Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SMAD7 in samples. An antibody specific for SMAD7 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySMAD7 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SMAD7 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 SMAD7 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:MAD proteins, originally defined in Drosophila, are essential components of the signaling pathways of the transforming growth factor-beta receptor family. Using a differential display approach in cultured endothelial cells subjected to multiple soluble and biomechanical stimuli, Topper et al. (1997) isolated a human endothelial cell cDNA encoding MADH7, which they called SMAD7.
The predicted 426-amino acid MADH7 protein lacks the C-terminal putative phosphorylation sites present in other MAD proteins, suggesting that it may be distinctly regulated. In situ hybridization and immunohistochemical analyses on human tissues showed that MADH7 is expressed predominantly in vascular endothelium.
