The B3GALNT2 antibody targets the β-1.3-N-acetylgalactosaminyltransferase 2 enzyme, encoded by the *B3GALNT2* gene. This enzyme catalyzes the transfer of N-acetylgalactosamine (GalNAc) to glycoproteins and glycolipids, playing a critical role in glycosylation pathways, particularly in synthesizing the core 3 and core 4 O-glycan structures. These structures are essential for cellular adhesion, signaling, and tissue integrity. Dysregulation of B3GALNT2 has been linked to congenital disorders of glycosylation (CDGs), including muscular dystrophy-dystroglycanopathy and intellectual disability. Antibodies against B3GALNT2 are primarily used in research to study its expression, localization, and functional roles in normal physiology and disease. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding in the characterization of glycosylation defects. Commercially available B3GALNT2 antibodies are typically monoclonal or polyclonal, validated for specificity across human, mouse, or rat samples. Recent studies also explore its potential as a biomarker in cancer, where altered glycosylation patterns influence tumor progression. Understanding B3GALNT2's mechanisms through antibody-based assays contributes to therapeutic strategies targeting glycosylation-related pathologies.