Human 3-Galactosyl-N-Acetylglucosaminide 4-Alpha-L-Fucosyltransferase FUT3 (FUT3) Protein

Background

Fucosyltransferase 3 (FUT3) is an enzyme within the glycosyltransferase family that is essential for the biosynthesis of specific carbohydrate structures on glycoproteins and glycolipids. FUT3 is responsible for catalyzing the addition of fucose, a hexose sugar, to various glycan substrates through α(1,3)- and α(1,4)-linkages, which are critical for the synthesis of the Lewis antigen family, including Lewis a (Le^a) and Lewis b (Le^b) antigens. These carbohydrate structures are integral components of cell surface glycoconjugates and play essential roles in cell-cell adhesion, recognition, and signaling. Encoded by the FUT3 gene located on chromosome 19p13.3, FUT3 is primarily expressed in epithelial tissues and leukocytes, especially in the gastrointestinal tract and other mucosal tissues. It is one of several fucosyltransferases in the human genome, with FUT3 being the most involved in the generation of Lewis antigens. The genetic variations in FUT3 are known to result in different phenotypes of Lewis antigens, which are important in blood group determination and are relevant to various diseases, including cancers and inflammatory conditions.