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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)

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Synonym(s):
β-Lactamase I, β-Lactamase II, Cephalosporinase, Penicillin amido-β-lactam hydrolase, Penicillinase from Enterobacter cloacae
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

biological source

bacterial (Enterobacter cloacae)

Quality Level

type

Type IV

form

lyophilized powder

specific activity

0.2-0.6 units/mg protein (using benzylpenicillin)

mol wt

29 kDa

composition

Protein, ~60%

technique(s)

enzyme immunoassay: suitable

suitability

suitable for enzyme test

application(s)

pharmaceutical

storage temp.

2-8°C

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1 of 4

This Item
L6170P0389G5635
Sigma-Aldrich

L6170

β-Lactamase

Penicillinase from Bacillus cereus lyophilized powder, 1,500-3,000 units/mg protein (using benzylpenicillin)

P0389

Penicillinase from Bacillus cereus

biological source

bacterial (Enterobacter cloacae)

biological source

-

biological source

Bacillus sp. (Bacillus cereus)

biological source

-

technique(s)

enzyme immunoassay: suitable

technique(s)

-

technique(s)

activity assay: suitable

technique(s)

-

application(s)

pharmaceutical

application(s)

-

application(s)

diagnostic assay manufacturing

application(s)

-

suitability

suitable for enzyme test

suitability

-

suitability

-

suitability

-

form

lyophilized powder

form

powder

form

lyophilized powder

form

lyophilized powder

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.

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.

inhibitor

Product No.
Description
Pricing

pictograms

Health hazard

signalword

Danger

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Persistent bacteremia in rabbit fetuses despite maternal antibiotic therapy in a novel intrauterine-infection model
Gras-Le Guen C, et al.
Antimicrobial Agents and Chemotherapy, 47(7), 2125-2130 (2003)
Protein-protein interactions monitored in mammalian cells via complementation of beta-lactamase enzyme fragments
Wehrman T, et al.
Proceedings of the National Academy of Sciences of the USA, 99(6), 3469-3474 (2002)
Past and present perspectives on beta$-lactamases
Bush K
Antimicrobial Agents and Chemotherapy, 62(10) (2018)
P J Johnsen et al.
Genetics, 181(4), 1521-1533 (2009-02-05)
We present a new hypothesis for the selective pressures responsible for maintaining natural competence and transformation. Our hypothesis is based in part on the observation that in Bacillus subtilis, where transformation is widespread, competence is associated with periods of nongrowth
Jung-Ho Shin et al.
EMBO reports, 22(2), e51790-e51790 (2021-01-20)
Bactericidal antibiotics are powerful agents due to their ability to convert essential bacterial functions into lethal processes. However, many important bacterial pathogens are remarkably tolerant against bactericidal antibiotics due to inducible damage repair responses. The cell wall damage response two-component

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