4-Nitrophenyl Alpha-D-Glucopyranoside: A Chromogenic Enzyme Substrate
Enhance your biochemical assays with a reliable chromogenic substrate for enzyme detection and pharmaceutical intermediate needs.
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4-Nitrophenyl Alpha-D-Glucopyranoside
This compound is a critical chromogenic substrate, specifically designed for the detection of alpha-D-glucosidase activity. Its enzymatic cleavage releases a p-nitrophenolate ion, which exhibits a distinct yellow color, making it ideal for quantitative enzyme activity measurement in various biological and chemical contexts.
- Leverage this reliable 4-nitrophenyl alpha-d-glucopyranoside enzyme substrate for accurate enzymatic reactions.
- Utilize its chromogenic substrate for alpha-d-glucosidase properties in biochemical analysis.
- Source high-quality pharmaceutical intermediates like 3767-28-0 for your synthesis needs.
- Explore the detection of glucansucrases and yeast alpha-d-glucosidase with this versatile reagent.
Key Advantages
Enzyme Activity Monitoring
Precisely track enzyme activity using this effective chromogenic substrate for alpha-d-glucosidase, ensuring reliable results in your research.
Diagnostic Applications
This compound is invaluable for the detection of glucansucrases and yeast alpha-d-glucosidase, supporting advancements in diagnostic methodologies.
Pharmaceutical Intermediate
As a key pharmaceutical intermediate 3767-28-0, it plays a crucial role in the synthesis of various therapeutic compounds.
Key Applications
Enzyme Assays
Employ 4-nitrophenyl alpha-d-glucopyranoside enzyme substrate for precise enzyme characterization and kinetic studies.
Diagnostic Development
Facilitate the development of diagnostic kits and assays through the reliable detection of glucansucrases and yeast alpha-d-glucosidase.
Drug Synthesis
This compound serves as a vital pharmaceutical intermediate, aiding in the creation of complex medicinal molecules.
Biochemical Research
Utilize this chromogenic substrate for alpha-d-glucosidase in fundamental biochemical research, exploring enzyme mechanisms and structures.