beta-Galactosidase Substrates
Items 11 to 16 of 16 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Chlorophenol Red-β-D-galactopyranoside | 99792-79-7 | sc-257242 sc-257242A sc-257242B sc-257242C | 25 mg 100 mg 500 mg 1 g | $58.00 $180.00 $655.00 $1220.00 | 2 | |
Chlorophenol Red-β-D-galactopyranoside acts as a substrate for beta-galactosidase, characterized by its chromogenic properties that enable visual detection of enzymatic activity. The compound's aromatic structure enhances its interaction with the enzyme, leading to a distinct colorimetric change upon hydrolysis. This substrate exhibits unique reaction kinetics, with pH and substrate concentration significantly influencing the rate of reaction, making it a valuable tool for studying enzyme dynamics in various biochemical assays. | ||||||
4-Chloro-3-indolyl β-D-galactopyranoside | 135313-63-2 | sc-220933 | 50 mg | $43.00 | ||
4-Chloro-3-indolyl β-D-galactopyranoside serves as a substrate for beta-galactosidase, featuring a unique indole moiety that facilitates specific enzyme binding. Its hydrolysis results in a fluorescent product, allowing for sensitive detection of enzymatic activity. The compound's structural characteristics influence its reactivity, with distinct kinetic profiles observed under varying ionic strengths and temperatures, providing insights into enzyme-substrate interactions and catalytic mechanisms. | ||||||
6-Bromo-2-naphthyl β-D-galactopyranoside | 15572-30-2 | sc-221085 sc-221085A | 1 g 2 g | $284.00 $555.00 | ||
6-Bromo-2-naphthyl β-D-galactopyranoside acts as a substrate for beta-galactosidase, characterized by its naphthyl group that enhances hydrophobic interactions with the enzyme's active site. This compound undergoes hydrolysis, yielding a chromogenic product that can be monitored spectrophotometrically. Its unique structural features contribute to varied reaction kinetics, revealing insights into enzyme specificity and the influence of steric factors on catalytic efficiency. | ||||||
2-Methoxy-4-(2-nitrovinyl)phenyl β-D-galactopyranoside | 70622-78-5 | sc-216229 sc-216229A | 250 mg 1 g | $131.00 $419.00 | ||
2-Methoxy-4-(2-nitrovinyl)phenyl β-D-galactopyranoside serves as a substrate for beta-galactosidase, distinguished by its nitrovinyl moiety, which introduces electron-withdrawing effects that modulate reactivity. The methoxy group enhances solubility and facilitates enzyme binding through hydrogen bonding. This compound exhibits unique hydrolytic behavior, allowing for the exploration of enzyme kinetics and the impact of substituent positioning on catalytic pathways, providing insights into enzyme-substrate interactions. | ||||||
5-Iodo-3-indoxyl-β-D-galactopyranoside | 36473-36-6 | sc-281464 sc-281464A | 50 mg 100 mg | $126.00 $200.00 | ||
5-Iodo-3-indoxyl-β-D-galactopyranoside acts as a substrate for beta-galactosidase, characterized by its indoxyl structure that promotes specific interactions with the enzyme's active site. The presence of the iodine atom enhances the compound's electrophilicity, influencing reaction rates and product formation. This substrate undergoes hydrolysis, yielding a colored product that allows for real-time monitoring of enzymatic activity, thus providing valuable insights into kinetic parameters and enzyme specificity. | ||||||
5-Dodecanoylaminoflorescein di-b-D-galactopyranoside | 138777-25-0 | sc-284621 sc-284621A sc-284621B sc-284621C sc-284621D | 1 mg 2 mg 5 mg 10 mg 25 mg | $204.00 $369.00 $826.00 $1543.00 $3478.00 | 1 | |
5-Dodecanoylaminoflorescein di-b-D-galactopyranoside serves as a substrate for beta-Galactosidase, showcasing unique molecular interactions that enhance enzymatic activity. The compound's long hydrophobic dodecanoyl chain promotes membrane affinity, influencing enzyme localization and stability. Its distinct fluorescence properties enable real-time monitoring of enzymatic reactions, providing insights into reaction kinetics and substrate specificity. This compound's behavior in glycosidic bond hydrolysis reveals intricate pathways in carbohydrate metabolism. | ||||||