MAK222
Beta-Lactamase Inhibitor Screening Kit
Sufficient for 100 Colorimetric tests
Synonym(s):
β-Lactamase Inhibitor Screening Kit
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About This Item
UNSPSC Code:
12161503
NACRES:
NA.84
Recommended Products
detection method
colorimetric
storage temp.
−20°C
Related Categories
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Sens. 1
Storage Class
10 - Combustible liquids
Certificates of Analysis (COA)
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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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