The ST6GAL1 antibody targets the ST6 beta-galactoside alpha-2.6-sialyltransferase 1. an enzyme critical in protein glycosylation. ST6GAL1 catalyzes the addition of α2.6-linked sialic acids to N-glycans, particularly on immunoglobulins, integrins, and other glycoproteins, influencing cell-cell interactions, immune responses, and cancer progression. This enzyme is implicated in various diseases, including cancers (e.g., colon, ovarian, pancreatic), where its overexpression correlates with metastasis, drug resistance, and poor prognosis. It also plays roles in inflammatory conditions and neurological disorders. Antibodies against ST6GAL1 are widely used in research to study its expression patterns, subcellular localization, and functional roles via techniques like Western blot, immunohistochemistry, and flow cytometry. Such tools help elucidate its contribution to disease mechanisms or therapeutic targeting. Commercial ST6GAL1 antibodies vary in specificity, often validated for reactivity across human, mouse, or rat samples. Researchers must verify antibody performance in specific experimental contexts, as glycosylation heterogeneity can affect detection. Ongoing studies focus on ST6GAL1’s potential as a biomarker or target for glycoengineering-based therapies, underscoring the antibody’s importance in both basic and translational research.