Recombinant FUT5 protein (His tag)

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This product is a recombinant fragment of the human 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5 (Fucosyltransferase 5), encompassing amino acids 74-374. This 301-amino acid fragment has been computationally optimized for stability and solubility, making it an ideal tool for structural studies, enzymatic assays, and functional investigations into fucosylation mechanisms.

The full-length FUT5 enzyme is a Golgi apparatus-resident, type II membrane protein that catalyzes the transfer of L-fucose from GDP-beta-L-fucose to N-acetyllactosamine units via alpha (1,3) linkages, with a strong preference for type 2 chain oligosaccharides. It plays a crucial role in synthesizing important carbohydrate antigens including VIM-2, Lewis X/SSEA-1, and sialyl Lewis X, which are involved in cell recognition and adhesion processes. FUT5 demonstrates substrate flexibility, also catalyzing alpha (1,4) linkages on type 1 and H-type 1 chains to a lesser extent, and shows enhanced activity toward sialylated type 2 acceptors compared to neutral oligosaccharides. Its membrane-bound localization in trans Golgi cisternae positions it strategically for modifying glycoproteins and glycolipids during their trafficking through the secretory pathway.