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Sigma-Aldrich

Beta-Lactamase Inhibitor Screening Kit

Sufficient for 100 Colorimetric tests

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Synonym(s):
β-Lactamase Inhibitor Screening Kit

detection method

colorimetric

storage temp.

−20°C

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This Item
L6170P4524426205
Sigma-Aldrich

L6170

β-Lactamase

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

General description

β-Lactamase (β-lactamase, βL, EC 3.5.2.6) is an enzyme first identified in Escherichia coli and has been described as penicillinase. A number of βLs have since been identified from various bacteria. β-Lactamases specifically hydrolyze β-lactam rings present in antibiotics such as penicillin, cephalosporins, monobactam, and carbapenem, and confer resistance against these antibiotics.

Application

Beta-Lactamase Inhibitor Screening Kit has been used in enzymatic assays.

Features and Benefits

Compatible with high-throughput handling systems.

Suitability

Suitable for the screening of inhibitors of β-Lactamase

Principle

The β-Lactamase Inhibitor Screening Kit is a rapid, simple and sensitive assay that is suitable for high throughput screening of β-Lactamase inhibitors. βL activity is measured by hydrolyzing a chromogenic cephalosporin called nitrocefin, producing a colorimetric product (A490), proportional to the enzymatic activity present.

Kit Components Only

Product No.
Description

  • β-Lactamase Assay Buffer

  • Nitrocefin, in DMSO

  • β-Lactamase

  • Inhibitor Control, Clavulanic acid

pictograms

Health hazard

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3


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Customers Also Viewed

Evaluation of 1, 4, 7-Triazacyclononane (TACN) as a potential Metallo-B-Lactamase inhibitor in Enterobacteriaceae: Restoring the Activity of B-lactams
Somboro A M, et al.
bioRxiv, 366146-366146 (2018)
Anou M Somboro et al.
Applied and environmental microbiology, 85(3) (2018-11-28)
Metallo-β-lactamase (MBL)-producing Enterobacteriaceae are of grave clinical concern, particularly as there are no metallo-β-lactamase inhibitors approved for clinical use. The discovery and development of MBL inhibitors to restore the efficacy of available β-lactams are thus imperative. We investigated a zinc-chelating

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