FUT3 was first cloned among the members of the α1,3-fucosyltransferase (α1,3FUT) family by Kukowska-Latallo et al. in 1990 . It was named Fuc-TIII by J. Lowe et al. or FUT3 by Oriol et al. Later, it was demonstrated to be the Lewis enzyme responsible for the expression of Lewis histo-blood group antigens, such as Lewis a (Lea) and Lewis b (Leb) .
FUT3 catalyzes the transfer of fucose from GDP-fucose to the N-acetylglucosamine (GlcNAc) residue of type-2 chain (Galβ1-4GlcNAc) with an α1,3-linkage, or to the GlcNAc residue of type-1 chain (Galβ1-3GlcNAc) with an α1,4-linkage . This enzymatic activity is essential for the biosynthesis of various Lewis antigen epitopes, including Lea, Leb, Lex, Ley, sialyl Lea (sLea), and sLex .
The Lewis antigens synthesized by FUT3 are involved in several biological processes:
Recombinant Human Fucosyltransferase 3 (FUT3) is produced using advanced biotechnological methods. It is formulated to be used in cell surface glycoengineering of living cells without affecting cell viability or native phenotype . The recombinant protein is typically supplied as a carrier-free solution, ensuring high purity and stability .
Recombinant FUT3 has several applications in research and biotechnology: