FUT7 (fucosyltransferase 7) is a Golgi-localized glycosyltransferase that catalyzes α1,3-fucosylation of N-acetylglucosamine residues on sialylated lactosamine units, generating sialyl Lewis X (sLeX), a critical ligand for selectin-mediated cell adhesion 1. This enzymatic activity is essential for leukocyte trafficking, as sLeX on leukocyte surfaces enables tethering and rolling along endothelial tissue expressing E-selectin and P-selectin, facilitating leukocyte accumulation at inflammatory sites 2. FUT7 also regulates 6-sulfo sLeX synthesis, which mediates L-selectin-dependent adhesion 1. Clinically, FUT7 dysregulation is implicated in multiple pathologies. In inflammatory bowel disease, reduced FUT7 expression in regulatory T cells impairs intestinal homing and immunosuppression; therapeutic FUT7 upregulation alleviates colitis 2. FUT7 promotes acute lymphoblastic leukemia cell adhesion and invasion via integrin/FAK/AKT signaling 3 and enhances bladder cancer progression through epithelial-mesenchymal transition and immune infiltration 4. In embryo implantation, FUT7-mediated sLeX expression facilitates trophoblast-endometrial adhesion 5. Additionally, FUT7 mutations associate with hereditary multiple exostoses through EXT1 pathway interactions 6. Recent therapeutic approaches harness FUT7-engineered extracellular vesicles expressing sLeX to promote angiogenesis and wound healing in diabetic wounds 7. Collectively, FUT7 functions as both a physiological adhesion regulator and a disease-relevant therapeutic target.