The B3GAT1 antibody targets the β-1.3-glucuronyltransferase 1 (B3GAT1) enzyme, also known as GlcAT-I, which plays a critical role in glycosaminoglycan (GAG) biosynthesis. This enzyme catalyzes the transfer of glucuronic acid to the terminal galactose residue in the linker region of proteoglycans, a step essential for forming the carbohydrate-protein linkage required for heparan sulfate and chondroitin sulfate chains. These glycosylated structures are vital for cellular processes, including cell adhesion, neural development, and extracellular matrix organization. B3GAT1 is particularly notable for its involvement in the biosynthesis of HNK-1 (human natural killer-1) carbohydrate epitopes, which are implicated in synaptic plasticity, memory formation, and immune cell interactions. Dysregulation of B3GAT1 has been associated with neurodevelopmental disorders, connective tissue abnormalities, and tumor progression. Antibodies against B3GAT1 are widely used in research to investigate its expression patterns, enzymatic activity, and functional roles in both normal physiology and disease models. They enable applications such as Western blotting, immunohistochemistry, and flow cytometry, aiding in the study of glycosylation defects and potential therapeutic targets. Recent studies also explore its interaction with integrins and growth factor receptors, highlighting its broader impact on cellular signaling pathways.