Items 31 to 40 of 51 total
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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N-(2-Hydroxyethyl)-1-deoxy-L-idonojirimycin Hydrochloride | sc-218913 | 5 mg | $360.00 | |||
N-(2-Hydroxyethyl)-1-deoxy-L-idonojirimycin Hydrochloride functions as a glycosidase inhibitor, showcasing remarkable specificity in its interactions with enzyme active sites. Its structural features facilitate the formation of stable enzyme-inhibitor complexes, effectively modulating glycosidase activity. The compound's unique hydroxyl group enhances solubility and reactivity, influencing kinetic parameters and providing a nuanced understanding of carbohydrate metabolism and enzymatic regulation. | ||||||
Phenyl β-D-glucopyranoside | 1464-44-4 | sc-222154B sc-222154 sc-222154A | 1 g 5 g 10 g | $38.00 $91.00 $115.00 | ||
Phenyl β-D-glucopyranoside acts as a glycosidase substrate, exhibiting unique interactions with enzyme active sites that promote hydrolysis. Its phenyl group enhances hydrophobic interactions, influencing binding affinity and reaction rates. The compound's glycosidic bond configuration allows for selective cleavage by specific glycosidases, providing insights into enzymatic mechanisms. Additionally, its solubility characteristics facilitate diverse experimental conditions, impacting kinetic studies of carbohydrate processing. | ||||||
5-Bromo-4-chloro-3-indolyl N-acetyl-β-D-glucosaminide | 4264-82-8 | sc-221011 sc-221011A | 250 mg 1 g | $200.00 $280.00 | ||
5-Bromo-4-chloro-3-indolyl N-acetyl-β-D-glucosaminide serves as a glycosidase substrate, characterized by its distinctive indole structure that enhances π-π stacking interactions with enzyme active sites. This compound's unique halogen substituents can modulate electronic properties, influencing enzyme specificity and catalytic efficiency. Its N-acetyl group contributes to steric hindrance, affecting the accessibility of the glycosidic bond, thus providing a nuanced understanding of glycosidase activity and substrate recognition. | ||||||
Naphthol AS-BI β-D-galactopyranoside | 51349-63-4 | sc-222039 sc-222039A | 250 mg 2 g | $228.00 $587.00 | ||
Naphthol AS-BI β-D-galactopyranoside acts as a glycosidase substrate, distinguished by its naphthol moiety that facilitates hydrogen bonding with enzyme active sites. The β-D-galactopyranoside configuration enhances solubility and reactivity, promoting efficient hydrolysis. Its structural features allow for specific interactions with glycosidases, influencing reaction kinetics and substrate turnover rates, thereby providing insights into enzyme mechanisms and substrate selectivity. | ||||||
N-Methyl-1-deoxynojirimycin | 69567-10-8 | sc-219184 | 5 mg | $465.00 | ||
N-Methyl-1-deoxynojirimycin serves as a potent glycosidase inhibitor, characterized by its unique ability to mimic the transition state of glycosidic bonds. This structural mimicry leads to strong binding interactions with the enzyme's active site, effectively blocking substrate access. Its stereochemistry and nitrogen substitution enhance selectivity, influencing enzyme kinetics and providing a deeper understanding of glycosidase mechanisms and substrate specificity. | ||||||
N-(2-Hydroxyethyl)-1-deoxy-L-altronojirimycin | 72432-03-2 (non-salt) | sc-218912 | 1 mg | $490.00 | ||
N-(2-Hydroxyethyl)-1-deoxy-L-altronojirimycin acts as a glycosidase inhibitor, distinguished by its ability to form hydrogen bonds with key residues in the enzyme's active site. This interaction stabilizes the enzyme-substrate complex, altering reaction kinetics and enhancing selectivity. Its unique hydroxyl and amine functionalities contribute to its binding affinity, providing insights into the catalytic mechanisms of glycosidases and their substrate interactions. | ||||||
α-Amylase | 9000-90-2 | sc-487951 sc-487951A | 25 g 500 g | $86.00 $340.00 | 3 | |
α-Amylase is a glycosidase that catalyzes the hydrolysis of α-1,4-glycosidic bonds in starch and glycogen, facilitating carbohydrate metabolism. Its active site features a catalytic triad that enhances substrate binding through van der Waals interactions and electrostatic stabilization. The enzyme exhibits a unique substrate specificity, with varying kinetic parameters influenced by pH and temperature, allowing for efficient starch degradation in diverse environments. | ||||||
4-Hydroxy diclofenac acyl glucuronide | sc-491289 sc-491289A | 1 mg 10 mg | $454.00 $3121.00 | |||
4-Hydroxy diclofenac acyl glucuronide acts as a glycosidase by facilitating the hydrolysis of glycosidic bonds through its unique structural conformation. Its active site is characterized by specific hydrogen bonding and hydrophobic interactions that enhance substrate affinity. The enzyme demonstrates distinct kinetic behavior, with reaction rates sensitive to ionic strength and temperature variations, allowing it to efficiently process diverse glycosidic substrates in various biochemical contexts. | ||||||
N-Ethyldeoxynojirimycin HCl | 72458-42-5 | sc-286403 sc-286403A | 5 mg 10 mg | $220.00 $400.00 | ||
N-Ethyldeoxynojirimycin HCl functions as a glycosidase by selectively inhibiting glycosidic bond hydrolysis through its unique stereochemistry. Its molecular structure allows for specific interactions with enzyme active sites, leading to competitive inhibition. The compound exhibits notable reaction kinetics, with a pronounced effect on substrate specificity and affinity, influenced by pH and ionic conditions, thereby modulating glycosidase activity in biochemical pathways. | ||||||
N-Dodecyldeoxynojirimycin | 79206-22-7 | sc-222003 | 10 mg | $388.00 | ||
N-Dodecyldeoxynojirimycin functions as a glycosidase inhibitor by selectively interacting with the active sites of glycosidases, disrupting their catalytic activity. Its long hydrophobic dodecyl chain enhances membrane permeability, allowing for effective enzyme targeting. The compound exhibits unique binding dynamics, with a preference for specific glycosidic linkages, which influences the rate of enzymatic reactions and alters substrate turnover. This specificity can lead to distinct modulation of glycan metabolism. |