FUT7 Human

FUT7 is a Golgi stack membrane protein that catalyzes the formation of alpha-1,3 glycosidic linkages. This enzyme is particularly important for the synthesis of sialyl-Lewis X antigens, which are involved in the E-selectin-binding process. The sialyl-Lewis X antigens are key elements in leukocyte homing and extravasation, processes essential for lymphocyte maturation and natural defense functions .

The fucose-containing glycans synthesized by FUT7 are critical for various cellular functions. These glycans are involved in cell-cell interactions, signaling pathways, and the immune response. The role of FUT7 in the creation of sialyl-Lewis X antigens highlights its importance in the immune system, particularly in the context of inflammation and infection .

Recombinant human FUT7 is produced using Chinese Hamster Ovary (CHO) cell lines. The recombinant protein is typically tagged with a C-terminal 6-His tag to facilitate purification. The production process ensures high purity and activity of the enzyme, making it suitable for various research and therapeutic applications .

Recombinant FUT7 is used in cell surface glycoengineering to modify the glycan structures on living cells. This modification does not affect cell viability or native phenotype apart from the intended impact on cell glycobiology. The enzyme’s ability to transfer fucose to specific substrates makes it valuable for studying glycosylation processes and developing glycan-based therapeutics .

Recombinant FUT7 is supplied as a 0.2 μm filtered solution in Tris and NaCl. It is shipped with polar packs and should be stored at -20 to -70 °C to maintain its stability. The enzyme remains stable for six months from the date of receipt when stored under the recommended conditions .