Date published: 2026-4-1

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alpha-mannosidase Inhibitors

Santa Cruz Biotechnology now offers a broad range of alpha-mannosidase Inhibitors for use in various applications. Alpha-mannosidase Inhibitors are critical tools in scientific research, particularly for studying the role of alpha-mannosidase enzymes in the catabolism of glycoproteins within lysosomes. These enzymes are responsible for cleaving mannose residues from glycoproteins, a key step in the degradation process that allows cells to recycle and properly process these molecules. By inhibiting alpha-mannosidase, researchers can investigate the enzyme's role in glycoprotein metabolism and explore the broader implications of its activity on cellular function. These inhibitors are particularly important in studies focused on understanding the molecular mechanisms underlying lysosomal storage disorders, such as alpha-mannosidosis, where a deficiency in alpha-mannosidase leads to the accumulation of undigested oligosaccharides within cells, resulting in cellular dysfunction. In the scientific community, alpha-mannosidase Inhibitors are widely used to dissect the pathways of glycoprotein turnover and to explore the consequences of enzyme inhibition in both normal and disease states. Researchers utilize these inhibitors in a variety of experimental setups, including in vitro enzyme assays, cell culture studies, and in vivo models, to gain insights into the regulation of lysosomal function, the impact of metabolic disruptions, and new fundemental targets. The availability of high-quality alpha-mannosidase Inhibitors is essential for advancing research in fields such as biochemistry, cell biology, and molecular genetics, providing the necessary tools to study and manipulate enzyme activity with precision. View detailed information on our available alpha-mannosidase Inhibitors by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

1-Deoxymannojirimycin hydrochloride

73465-43-7sc-255823
sc-255823A
1 mg
5 mg
$87.00
$143.00
4
(1)

1-Deoxymannojirimycin hydrochloride serves as a potent alpha-mannosidase inhibitor, characterized by its ability to form stable interactions with the enzyme's active site. This compound's unique structure allows for competitive inhibition, effectively altering the enzyme's kinetics. Its presence can significantly impact glycoprotein processing pathways, leading to altered glycan structures. The compound's solubility properties enhance its accessibility in biochemical assays, facilitating detailed studies of mannosidase activity.

Phenyl 2,3,4,6-Tetra-O-acetyl-1-thio-α-D-mannopyranoside

108032-93-5sc-222158
1 g
$260.00
(0)

Phenyl 2,3,4,6-Tetra-O-acetyl-1-thio-α-D-mannopyranoside acts as a selective alpha-mannosidase inhibitor through its unique thioacetyl group, which enhances binding affinity to the enzyme's active site. This compound exhibits a distinct mechanism of action, promoting non-competitive inhibition that influences substrate turnover rates. Its structural features allow for specific molecular interactions, potentially modulating glycan biosynthesis and affecting cellular glycoprotein dynamics.

D-Manno-γ-lactam

62362-63-4sc-218030
5 mg
$300.00
(0)

D-Manno-γ-lactam serves as a potent alpha-mannosidase inhibitor, characterized by its unique cyclic structure that facilitates strong interactions with the enzyme's active site. This compound exhibits competitive inhibition, effectively altering the enzyme's kinetics and substrate affinity. Its distinctive lactam ring enhances stability and solubility, allowing for precise modulation of glycosylation pathways. The compound's stereochemistry plays a crucial role in its selectivity, influencing glycan processing in cellular environments.

D-Mannojirimycin Bisulfite

sc-218031
5 mg
$299.00
(0)

D-Mannojirimycin Bisulfite acts as a selective alpha-mannosidase inhibitor, distinguished by its ability to form stable complexes with the enzyme through specific hydrogen bonding and hydrophobic interactions. This compound exhibits non-competitive inhibition, impacting the enzyme's catalytic efficiency without directly competing with the substrate. Its unique bisulfite modification enhances solubility and reactivity, allowing for targeted modulation of glycan biosynthesis and cellular glycoprotein maturation.