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Beta-Lactamase Activity Colorimetric Assay Kit

based on 1 citations in multiple journalsBeta-Lactamase Activity Colorimetric Assay Kit14.1 4
Catalog #: K803

In stock

$625.00

Product Details

Cat # +Size K803-100
Size 100 assays
Detection Method Absorbance (490 nm)
Applications • Measurement of β-Lactamase activity in various biological samples
• Analysis of β-Lactamase activity in pathological conditions
Features & Benefits • Rapid, simple & sensitive
• The assay can detect enzymatic activity as low as 0.06 mU in a variety of biological samples.
Kit Components • βL Assay Buffer
• Nitrocefin (in DMSO)
• Positive Control (Lyophilized)
• βL Hydrolysis Buffer
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not For Use in Humans.

Details

Beta-Lactamases (βLs), are a large family of hydrolases comprising more than 850 identified members expressed in Gram-positive and Gram-negative bacteria. βLs can be classified according to their substrate or inhibitor specificity. These enzymes are capable of hydrolyzing four atom rings known as β-lactams. Antibiotics containing β-lactam rings (i.e. penicillin, cephalosporin, monobactam, carbapenem) are highly susceptible to be hydrolyzed via enzymatic activity, which deactivates their antibiotic potency. βLs have become a significant clinical threat due to the alarming number of cases of bacterial strains showing β-lactam antibiotic resistance. BioVision’s Beta-Lactamase Activity Assay Kit offers a simple and sensitive assay that can detect and quantify the enzymatic activity of these hydrolases. The assay is based on the hydrolysis of Nitrocefin, a chromogenic cephalosporin, that results in the generation of a colored product (OD 490 nm), which is directly proportional to the amount of βL activity. The assay can detect enzymatic activity as low as 0.06 mU in a variety of biological samples.


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Penwell et al., Molecular Mechanisms of Sulbactam Antibacterial Activity and Resistance Determinants in Acinetobacter baumannii. Antimicrob. Agents Chemother., Mar 2015; 59: 1680 - 1689.
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