Date published: 2026-5-18

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β-1,4-Gal-T1 Inhibitors

Santa Cruz Biotechnology now offers a broad range of beta-1,4-Gal-T1 Inhibitors for use in various applications. Beta-1,4-galactosyltransferase 1 (beta-1,4-Gal-T1) is a key enzyme involved in the biosynthesis of glycoproteins and glycolipids, specifically catalyzing the transfer of galactose to N-acetylglucosamine residues on these molecules. This enzyme plays a crucial role in the formation of glycan structures, which are essential for numerous biological processes, including cell-cell communication, protein folding, and immune responses. Inhibitors of beta-1,4-Gal-T1 are important tools in scientific research, as they allow researchers to study the functional implications of altered glycosylation patterns. By inhibiting this enzyme, scientists can investigate the role of glycosylation in various cellular processes, including cell signaling, adhesion, and the development of diseases linked to glycan abnormalities. Beta-1,4-Gal-T1 inhibitors are particularly valuable in research focused on understanding how changes in glycosylation affect protein function and stability, as well as how these changes contribute to pathologies such as cancer, inflammation, and autoimmune disorders. Additionally, these inhibitors are used in studies aiming to study the mechanisms of enzyme regulation and to explore potential scientific strategies for modulating glycosylation pathways. The availability of a diverse range of beta-1,4-Gal-T1 inhibitors enables researchers to design experiments that target specific aspects of glycan biosynthesis, advancing our understanding of the complex roles that glycosylation plays in health and disease. View detailed information on our available beta-1,4-Gal-T1 Inhibitors by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

4-Deoxy-D-glucose

28434-38-0sc-220937
25 mg
$323.00
(0)

4-Deoxy-D-glucose acts as a selective beta-1,4-Gal-T1 inhibitor, interfering with glycosylation processes by mimicking the natural substrate. Its structural conformation allows for specific hydrogen bonding and steric hindrance, effectively blocking enzyme activity. This inhibition alters carbohydrate metabolism pathways, impacting cell signaling and adhesion. The compound's unique interactions with the enzyme's active site provide insights into the regulation of glycan structures and their biological implications.