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2-nitrophenyl β-D-galactopyranoside-[2-13C]

General Information
Catalog: BLP-013257
Molecular Formula: C11[13C]H15NO8
Molecular Weight: 302.24
Chemical Structure
2-nitrophenyl β-D-galactopyranoside-[2-13C]
Description Labelled 2-Nitrophenyl-beta-D-galactopyranoside. It is used for the determination of β-galactosidase activity, and it is used as the substrate of β-galactosidase in biochemical studies.
Synonyms 2-nitrophenyl beta-D-[2-13C]galactopyranoside
Related CAS 369-07-3 (unlabelled)

2-Nitrophenyl β-D-galactopyranoside-[2-13C] is a synthetic substrate used predominantly in biochemical assays and research. Here are some key applications of 2-nitrophenyl β-D-galactopyranoside-[2-13C]:

Enzyme Kinetics: 2-Nitrophenyl β-D-galactopyranoside-[2-13C] is employed to study the kinetic properties of β-galactosidase enzymes. By monitoring the release of the chromogenic nitrophenyl group, researchers can measure enzyme activity and determine kinetic parameters such as Km and Vmax. This detailed kinetic analysis is crucial for understanding enzyme mechanisms and designing effective inhibitors.

Metabolic Flux Analysis: This compound is valuable for tracking metabolic pathways involving β-galactosidase activity through stable isotope labeling. The incorporation of the [2-13C] label allows precise measurement of carbon flow through metabolic networks. This technique helps elucidate cellular metabolism and assess the impact of genetic or environmental changes on metabolic activities.

Diagnostic Assays: In diagnostic applications, 2-nitrophenyl β-D-galactopyranoside-[2-13C] serves as a substrate in assays to identify bacterial contamination and certain genetic diseases. When bacteria with β-galactosidase activity are present, the substrate is hydrolyzed, leading to a colorimetric change that can be easily detected. This is particularly useful in clinical and environmental microbiology for rapid and accurate diagnostics.

Protein Engineering: Researchers utilize this compound in protein engineering experiments to screen for optimized or mutated β-galactosidase enzymes with improved properties. By assessing the hydrolysis of the substrate, scientists can evaluate enzyme performance under different conditions. This aids in the development of more efficient biocatalysts for industrial and therapeutic applications.

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