Date published: 2026-5-27

1-800-457-3801

SCBT Portrait Logo
Seach Input

ALG9 Substrates

Santa Cruz Biotechnology now offers a broad range of ALG9 Substrates for use in various applications. ALG9 Substrates are crucial in scientific research for studying the function and regulation of the ALG9 enzyme, which is involved in the process of glycosylationa critical modification of proteins and lipids that affects their stability, localization, and function. ALG9 specifically catalyzes the addition of mannose residues during the biosynthesis of lipid-linked oligosaccharides, which are essential for proper protein folding and quality control in the endoplasmic reticulum. By utilizing specific ALG9 Substrates, researchers can investigate the enzyme's activity and its role in the intricate glycosylation pathway. These substrates enable detailed studies on how disruptions in ALG9 function can lead to glycosylation defects, contributing to a better understanding of various cellular processes, including protein folding, signal transduction, and cell-cell interactions. In the scientific community, ALG9 Substrates are widely employed in research aimed at explaining the molecular mechanisms underlying congenital disorders of glycosylation (CDGs) and other diseases linked to defective glycosylation. Researchers use these substrates in various experimental models, including in vitro enzyme assays and cell culture systems, to dissect the steps of glycan assembly and the impact of specific mutations or inhibitors on ALG9 activity. The availability of high-quality ALG9 Substrates is essential for advancing research in areas such as cell biology, biochemistry, and molecular genetics, offering critical insights into the enzyme's function and its broader implications in health and disease. View detailed information on our available ALG9 Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Methyl a-D-mannopyranoside

617-04-9sc-280980
100 g
$300.00
(0)

Methyl α-D-mannopyranoside serves as a substrate for ALG9, a key enzyme in the glycosylation pathway. Its structure promotes specific interactions with glycosyltransferases, influencing the synthesis of oligosaccharides. The compound's ability to form hydrogen bonds enhances its reactivity, facilitating the transfer of mannose residues. Additionally, its stereochemistry plays a crucial role in determining the enzyme's specificity and catalytic efficiency, impacting the overall glycan assembly process.