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P4524 Sigma-Aldrich

β-Lactamase from Enterobacter cloacae

Type IV, lyophilized powder, 0.2-0.6 units/mg protein (using benzylpenicillin)

Synonym: β-Lactamase I, β-Lactamase II, Cephalosporinase, Penicillin amido-β-lactam hydrolase, Penicillinase from Enterobacter cloacae

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Description

General description

β-Lactamase is a monomeric enzyme of 29 kDa. This product is produced from Enterobacter cloacae and is provided as a lyophilized powder. It acts as a target protein for β-lactam antibiotics. This enzyme is present in Gram-negative bacteria.

Application

β--lactamase is used to inactivate β-lactam antibiotics by breaking open the β-lactam ring. β--lactamase is used to study antibiotic resistance and resistance suppression. Product P4524 is produced from Enterobacter cloacae and is provided as a lyophilized powder.

β-Lactamase from Enterobacter cloacae has been used in the maternal and fetal quantitative blood cultures to avoid any carryover phenomenon. It has also been used as a component in Mueller Hinton (MH) broth for placental cultures.

Packaging

100, 250 units in glass bottle

Biochem/physiol Actions

β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring.

Unit Definition

One unit will hydrolyze 1.0 μmole of benzylpenicillin per min at pH 7.0 at 25 °C. This International Unit (using benzylpenicillin as substrate) is approximately equal to 600 Levy or 75 Pollock units.

Physical form

Lyophilized powder containing sodium phosphate buffer salts

Analysis Note

Protein determined by biuret.

Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis (COA)

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Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Metabolomics, Molecular biology

Peer-Reviewed Papers
15

References

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