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MAK129 Sigma-Aldrich

β-Glucosidase Activity Assay Kit

sufficient for 100 colorimetric tests

  •  NACRES NA.84

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Properties

Related Categories Assay Kits by Specialty Area, Carbohydrate Metabolism Assay Kits, Cell Biology, Enzymatic Activity Assay Kits, Enzymatic Kits for the Quantitation of Nutrients and Metabolites,
usage   sufficient for 100 colorimetric tests
storage temp.   −20°C
Gene Information   human ... GBA(2629), GBA2(57704), GBA3(57733)
mouse ... GBA(14466), GBA2(230101)
rat ... GBA(684536), GBA2(298399), GBA3(289687)

Description

General description

β-Glucosidase hydrolyzes carbohydrates by acting on terminal, non-reducing b(1→4)-linked D-glucose residues with the release of D-glucose. β-Glucosidases are required by organisms for the consumption of cellulose. Lysozyme, a β-glucosidase present in tears, acts on the β(1→4) glucose bonds present in the peptidoglycan cell wall of Gram-negative bacteria and helps to prevent bacterial infections in the eye. Defects in β-glucosidase activity have been implicated in Gaucher′s disease and Parkinson′s disease.

Application

β-Glucosidase Activity Assay Kit has been used to measure the β-glucosidase activity of the sample.

Features and Benefits

Compatible with high-throughput handling systems.

Suitability

The β-Glucosidase Activity Assay kit provides a simple and direct procedure for measuring β-glucosidase activity in biological samples, for characterizing β-glucosidase production, and for the screening of β-glucosidase modulators.

Principle

In this assay, β-glucosidase activity is determined by a reaction in which β-glucosidase hydrolyzes p-nitrophenyl-β-D-glucopyranoside resulting in the formation of a colorimetric (405 nm) product, proportional to the β-glucosidase activity present. One unit of β-Glucosidse is the amount of enzyme that catalyzes the hydrolysis of 1.0 μmole substrate per minute at pH 7.0.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Protocols & Articles
Peer-Reviewed Papers
15

References

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