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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥1500.00 units/mg protein (using benzylpenicillin)
Biological source:
Bacillus sp. (Bacillus cereus)
biological source
Bacillus sp. (Bacillus cereus)
form
lyophilized powder
specific activity
≥1500.00 units/mg protein (using benzylpenicillin)
composition
Protein, ~10%
technique(s)
activity assay: suitable
application(s)
diagnostic assay manufacturing
shipped in
wet ice
storage temp.
2-8°C
Quality Level
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General description
Penicillinase from Bacillus cereus has been shown to contain three distinct species when purified and examined for homogeneity by sedimentation analysis, amino-terminal analysis, and vertical acrylamide gel electrophoresis.
Application
Penicillinase can be used to reduce levels of penicillin in patients with severe penicillin reactions.
Used in the production of penicillin.
Used in the production of penicillin. Penicillinase from Bacillus cereus has been used in a comparison study with penicillinase from Bacillus subtillis where the Michaelis constant, shape of the Ph/activity curve and immunological properties were shown to be significantly different.
Biochem/physiol Actions
Penicillinase specifically catalyzes the hydrolysis of β-lactam ring of penicillin.
Physical form
Lyophilized powder containing phosphate and citrate buffer salts
Analysis Note
Protein determined by biuret.
Other Notes
One unit will hydrolyze 1.0 μmole of indicated substrate per min at pH 7.0 at 25 °C. Sold as benzylpenicillin units. This International Unit (using benzylpenicillin as substrate) is approximately equal to 600 Levy or 75 Pollock units.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Regulatory Information
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Cristian Piras et al.
Chemical science, 13(6), 1746-1758 (2022-03-15)
Large-scale population screening for early and accurate detection of disease is a key objective for future diagnostics. Ideally, diagnostic tests that achieve this goal are also cost-effective, fast and easily adaptable to new diseases with the potential of multiplexing. Mass
Anaphylactic shock after therapy with penicillinase.
A L HYMAN
Journal of the American Medical Association, 169(6), 593-594 (1959-02-07)
Junichiro Marui et al.
Journal of bioscience and bioengineering, 110(1), 8-11 (2010-06-15)
Aspergillus oryzae penicillin biosynthetic genes were clustered. The penicillin production was positively regulated by VeA, a global gene regulator required for transcriptional expression of the penicillin biosynthetic genes. Overexpression of the biosynthetic genes by a strong promoter yielded a greater
A Comparison of the Properties of Penicillinase produced by Bacillus subtilis and Bacillus cereus with and without Addition of Penicillin
Manson, E., et al.
Microbiology, 11, 493-505 (1954)
M A van Opstal et al.
Journal of pharmaceutical and biomedical analysis, 8(1), 49-60 (1990-01-01)
An automated assay for the determination of penicillin in formulations suitable for use in pharmaceutical quality control is presented. The method is based on the classical iodometric penicillin assay which is incorporated in a flow injection analysis (FIA) system. The
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