SAE0013
Oxyrase ® for Broth
Sinónimos:
OB
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
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General description
Oxyrase for Broth is a sterile enzyme formulation that uses the Oxyrase Enzyme System to produce anaerobic conditions in different bacteriological broth media. Oxyrase for Broth facilitates growth of anaerobes, such as for reviving lyophiles. Oxyrase for Broth is a ready-to-use product that renders broth anaerobic in 10-15 minutes, and continues to remove oxygen from the container headspace beyond that time.
Application
Oxyrase® for broth has been used in reinforced clostridial media to provide an anaerobic environment for culturing Bifidobacterium adolescentis. It has also been used as a component in PMM/imaging media for oxygen-free microscopy experiments to remove oxygen.
Biochem/physiol Actions
Oxyrase® for broth is useful to cultivate species like Shigella sonnei and Shewanella oneidensis.It also provides anaerobic conditions for cultivating species like Escherichia coli, Staphylococcus aureus, and Pseudomonas aeruginosa.
Storage and Stability
Store at -20 °C. (Long Term Storage)
Analysis Note
Oxyrase contains a penicillin binding protein that may interfere with penicillin and some related antibiotics.
Legal Information
Oxyrase is a registered trademark of Oxyrase, Inc.
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Referencia del producto
Descripción
Precios
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Andrew P Jacobson et al.
Journal of AOAC International, 87(5), 1115-1122 (2004-10-21)
Alternative methods of reducing oxygen during anaerobic enrichment in the Bacteriological Analytical Manual (BAM) Shigella culture method were evaluated and compared to the current and less practical GasPak method. The alternative anaerobic methods included the use of reducing agents in
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Aminoglycosides are broad-spectrum antibiotics whose mechanism of action is under debate. It is widely accepted that membrane voltage potentiates aminoglycoside activity, which is ascribed to voltage-dependent drug uptake. In this paper, we measured the response of Escherichia coli treated with
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