Anti-FUT3

Protein function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D- GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors and participates in the blood groups Lewis determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens (PubMed:12668675, PubMed:1977660, PubMed:11058871). Also catalyzes the transfer of L- fucose to subterminal GlcNAc of sialyl- and disialyl- lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sialyl Lewis a expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration (PubMed:12668675, PubMed:11058871, PubMed:27453266). Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin (PubMed:11058871). Prefers type 1 chain over type 2 acceptors (PubMed:7721776). Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred (PubMed:7721776). Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme (PubMed:1977660). [The UniProt Consortium] Buffer: 40% glycerol and PBS (pH 7.2). 0.02% sodium azide is added as preservative. Highest antigen sequence identity to mouse: 39% and to rat: 39%