epitope mapping near the N-terminus of β-1,3-Gal-T2 of human origin
recommended for detection of β-1,3-Gal-T2 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
β-1,3-Gal-T2 Background Information Several oligosaccharide structures and protein glycoconjugate types are found in nature (1,2). Homologous glycosyltransferase (GT) gene families catalyze the formation of glycosidic linkages (1,3). The beta-1,3 galactosyltransferase (∫-1,3-Gal-T) gene family encodes a set of type II transmembrane glycoproteins that are catalytically diverse and use different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine) to catalyze the addition of an activated monosaccharide to a terminal lactose (3–6). The protein coding sequences for ∫-1,3-Gal-T genes comprise a single exon and are distantly related to the Drosophila Brainiac gene (3,4). The ∫-1,4-galactosyltransferase (∫-1,4-Gal-T) gene family encodes type II membrane-bound glycoproteins that show exclusive specificity for the donor substrate, UDP-galactose (5). ∫-1,4-Gal-T genes transfer galactose in a ∫-1,4 linkage to similar acceptor sugars; each gene has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures (5). GTs on the surface of sperm in part mediate gamete adhesion by binding to appropriate carbohydrate substrates in the egg zona pellucida (6,7). In several tissues and cell lines, GTs localize to the Golgi complex (8).
