Description
Description: This assay employs a two-site sandwich ELISA to quantitate GALNT8 in samples. An antibody specific for GALNT8 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any GALNT8 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for GALNT8 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 GALNT8 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: GALNT8 encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression.The deduced 637-amino acid type II integral membrane protein has an N-terminal 6-residue cytoplasmic region, a single transmembrane domain, a 118-amino acid stem region, and a long luminal region with a ricin/lectin-like domain