Date published: 2026-4-1

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Sialyltransferase Inhibitors

Santa Cruz Biotechnology now offers a broad range of Sialyltransferase Inhibitors for use in various applications. Sialyltransferases are enzymes that play a crucial role in the addition of sialic acid to glycoproteins and glycolipids, a process known as sialylation. Sialyltransferase inhibitors are compounds that specifically inhibit these enzymes, thereby regulating sialylation levels in various biological systems. This regulation is critical in scientific research, particularly in the study of cell signaling, cell adhesion, and immune response. The ability to modulate sialylation using these inhibitors provides researchers with a valuable tool to dissect the complex biochemical pathways involved in these processes. Moreover, sialylation is a key factor in the structural diversity of glycoproteins and glycolipids, influencing the behavior of cells and the interaction between cells and their environment. By using sialyltransferase inhibitors, scientists can better understand these molecular mechanisms, leading to insights into areas such as developmental biology, cancer biology, and immunology. These inhibitors are also useful in the field of glycobiology for studying the role of glycosylation in protein function and stability. View detailed information on our available Sialyltransferase Inhibitors by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Lithocholylglycine

474-74-8sc-207830A
sc-207830B
sc-207830
sc-207830C
sc-207830D
sc-207830E
2 mg
5 mg
10 mg
25 mg
50 mg
100 mg
$204.00
$277.00
$360.00
$809.00
$1515.00
$2503.00
4
(0)

Lithocholylglycine acts as a sialyltransferase, exhibiting a unique ability to facilitate the transfer of sialic acid residues to glycoproteins. Its specific binding interactions with donor substrates enhance the enzyme's catalytic efficiency, promoting rapid glycosylation reactions. The compound's conformational flexibility allows for optimal alignment of substrates, while its distinct active site architecture influences substrate specificity and reaction rates, contributing to diverse biological pathways.