PNGase inhibitors, short for Peptide-N-Glycosidase inhibitors, belong to a class of chemical compounds that play a crucial role in biochemical research and biotechnology. These inhibitors are specifically designed to target and modulate the activity of the enzyme Peptide-N-Glycosidase (PNGase), which is involved in the process of deglycosylation. Deglycosylation is the enzymatic removal of N-linked glycans from glycoproteins, a pivotal step in understanding protein structure, function, and quality control in various biological contexts. PNGase itself is a hydrolase enzyme responsible for cleaving the glycosidic bond between the asparagine (Asn) residue and the N-linked glycan, thus releasing the glycan moiety from the protein backbone.
PNGase inhibitors are synthesized to influence the catalytic activity of PNGase, either by enhancing or inhibiting its function. These compounds are invaluable tools in glycobiology research, as they allow scientists to manipulate and study the glycosylation patterns of proteins. Inhibitors can block PNGase activity, leading to the preservation of glycoproteins in their glycosylated form, providing insights into the functional consequences of glycosylation. Researchers use PNGase inhibitors to gain a deeper understanding of glycoprotein function, protein folding, and the implications of glycosylation in various cellular processes, which is fundamental in advancing our knowledge of biology and biochemistry.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Z-VAD-FMK | 187389-52-2 | sc-3067 | 500 µg | $75.00 | 256 | |
A pan-caspase inhibitor that can also inhibit de-glycosylation activity indirectly, as it can influence the pathways involving caspases which may interact with NGLY1. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $60.00 $265.00 $1000.00 | 163 | |
A proteasome inhibitor that can elevate ER stress, potentially affecting NGLY1-related deglycosylation processes due to the unfolded protein response. | ||||||
Kifunensine | 109944-15-2 | sc-201364 sc-201364A sc-201364B sc-201364C | 1 mg 5 mg 10 mg 100 mg | $135.00 $540.00 $1025.00 $6248.00 | 25 | |
A mannosidase inhibitor that can lead to the accumulation of misfolded glycoproteins, potentially impacting NGLY1 activity indirectly. | ||||||
Swainsonine | 72741-87-8 | sc-201362 sc-201362C sc-201362A sc-201362D sc-201362B | 1 mg 2 mg 5 mg 10 mg 25 mg | $138.00 $251.00 $631.00 $815.00 $1832.00 | 6 | |
Inhibits mannosidase II, which could potentially lead to altered glycosylation patterns, indirectly affecting NGLY1's substrate availability. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
An N-linked glycosylation inhibitor that can indirectly affect NGLY1 by reducing its glycoprotein substrate pool. | ||||||
Deoxynojirimycin | 19130-96-2 | sc-201369 sc-201369A | 1 mg 5 mg | $73.00 $145.00 | ||
An inhibitor of glucosidases, which may indirectly affect the function of NGLY1 by altering glycan processing. | ||||||
Castanospermine | 79831-76-8 | sc-201358 sc-201358A | 100 mg 500 mg | $184.00 $632.00 | 10 | |
A glucosidase inhibitor that can indirectly influence NGLY1 activity through the modulation of glycan structures on glycoproteins. | ||||||
Deoxymannojirimycin hydrochloride | 84444-90-6 | sc-201360 sc-201360A | 1 mg 5 mg | $93.00 $239.00 | 2 | |
Inhibits mannosidase I, possibly leading to altered glycoprotein processing and indirectly influencing NGLY1. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $158.00 | 6 | |
A triterpene that induces heat shock response and could indirectly modulate the function of NGLY1 by affecting protein folding. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $110.00 $250.00 $936.00 $50.00 | 33 | |
A flavonoid that has various cellular effects and could alter NGLY1 activity indirectly through modulation of cellular signaling pathways. | ||||||