Date published: 2026-4-3

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MAN1 Substrates

Santa Cruz Biotechnology now offers a broad range of MAN1 Substrates for use in various applications. MAN1, or mannosidase 1, is an important enzyme involved in the processing and maturation of glycoproteins within the Golgi apparatus. MAN1 substrates are vital in scientific research for studying glycoprotein biosynthesis and the role of N-glycan trimming in cellular processes. These substrates are used in assays to measure the activity of MAN1, helping researchers understand the enzyme's function in the removal of mannose residues during glycoprotein modification. By utilizing MAN1 substrates, scientists can explore the mechanisms governing protein folding, trafficking, and degradation. This research is essential for comprehending how glycoproteins contribute to cellular communication, adhesion, and immune response. Additionally, MAN1 substrates are employed in studies examining the impact of glycosylation on protein stability and function, offering insights into disorders related to glycoprotein processing. These substrates also facilitate the identification of inhibitors or modulators of MAN1 activity, which can be used to investigate the regulation of glycosylation pathways. Overall, MAN1 substrates are critical tools for advancing our understanding of glycoprotein biology and cellular metabolism. View detailed information on our available MAN1 Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Methyl 2-O-(α-D-Mannopyranosyl)-α-D-mannopyranoside

59571-75-4sc-221895
5 mg
$326.00
(0)

Methyl 2-O-(α-D-Mannopyranosyl)-α-D-mannopyranoside exhibits unique molecular interactions due to its dual mannopyranosyl structure, which enhances its solubility and reactivity in glycosylation reactions. The presence of the methyl group contributes to its stability while influencing the steric hindrance during enzymatic processes. This compound's specific configuration allows for selective binding with glycosidases, impacting reaction kinetics and product specificity in carbohydrate transformations.