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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
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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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.
Physical form
Lyophilized powder containing sodium phosphate buffer salts
Analysis Note
Protein determined by biuret.
Other Notes
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
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Past and present perspectives on beta$-lactamases
Bush K
Antimicrobial Agents and Chemotherapy, 62(10) (2018)
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)
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)
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
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
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