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AB12251

Anti-Beta Lactamase antibody [8A5.A10]

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(33 Publications)

Mouse Monoclonal Beta-lactamase antibody. Carrier free. Suitable for ELISA, WB and reacts with Escherichia coli samples. Cited in 33 publications.

View Alternative Names

ampA, b4150, JW4111, ampC, Beta-lactamase, Cephalosporinase, CSase

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

8A5.A10

Isotype

IgG1

Carrier free

Yes

Reacts with

Escherichia coli

Applications

WB, ELISA

applications

Specificity

This antibody specifically recognizes TEM type beta lactamases.

Reactivity data

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Product details

Dilute in PBS or medium which is identical to that used in the assay system.

This product was changed from ascites to tissue culture supernatant on 19/12/2018. Please note that the dilutions may need to be adjusted accordingly. If you have any questions please do not hesitate to contact our scientific support team.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purified from TCS
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Beta-lactamase is an enzyme responsible for breaking down beta-lactam antibiotics such as penicillins and cephalosporins. This enzyme is also known by several names: beta lactamase beta-lactamase and b-lactamase. It has a molecular weight of approximately 29 kDa. Mainly beta-lactamase is expressed in various bacterial species including Escherichia coli and Staphylococcus aureus where it provides them with resistance against beta-lactam antibiotics. The presence of beta-lactamase significantly impacts the efficacy of these antibiotics in clinical settings.
Biological function summary

Beta-lactamase enzymes interact with beta-lactam antibiotics by hydrolyzing the beta-lactam ring within the antibiotic molecule. This action prohibits the antibiotics from binding to their bacterial targets rendering them ineffective. Beta-lactamase does not function alone; it can associate with other proteins in bacteria such as the outer membrane proteins which facilitate its secretion and activity. This enzyme is not part of a larger complex but works independently to confer antibiotic resistance to the host organism.

Pathways

Beta-lactamase plays a critical role in the antibiotic resistance pathway. This enzyme links to the cell wall biosynthesis pathway by inhibiting antibiotics that target bacterial cell wall synthesis. Because of this inhibition the production of cell wall components continues unhindered. Beta-lactamase activity is associated with penicillin-binding proteins (PBPs) which are the intended targets of beta-lactam antibiotics. By preventing the binding of antibiotics to these PBPs beta-lactamase ensures the survival of resistant bacterial strains.

Beta-lactamase contributes significantly to antibiotic resistance leading to infections that are difficult to treat such as methicillin-resistant Staphylococcus aureus (MRSA) and multidrug-resistant Escherichia coli infections. These bacteria produce beta-lactamase neutralizing the therapeutic effects of many commonly used antibiotics. The enzyme's action connects it to other proteins involved in resistance mechanisms like efflux pumps and proteases which also play parts in shielding bacteria from antibacterial agents. This correlation underlines the necessity for developing inhibitors that target beta-lactamase without hindering beneficial bacterial functions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Class C beta-lactamase which confers resistance to penicillins and cephalosporins (PubMed : 12323371, PubMed : 17956081, PubMed : 23043117, PubMed : 33199391, PubMed : 6998377). Has benzylpenicillin- and cephaloridine-hydrolyzing activity (PubMed : 3264154, PubMed : 3264155, PubMed : 6998377). Has weak cefuroxime, cefotaxime, cefoxitin and oxacillin-hydrolyzing activities (PubMed : 19913034, PubMed : 3264154, PubMed : 3264155).
See full target information ampC

Publications (33)

Recent publications for all applications. Explore the full list and refine your search

Communications biology 7:1549 PubMed39572728

2024

Infection with novel duck reovirus induces stress granule and methylation-mediated host translational shutoff in Muscovy ducklings.

Applications

Unspecified application

Species

Unspecified reactive species

Tao Yun,Jionggang Hua,Liu Chen,Weicheng Ye,Zheng Ni,Yinchu Zhu,Cun Zhang

Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] 54:645-653 PubMed36808308

2023

Influence of class 2 integron integrase concentration on gene cassette insertion and excision in vivo.

Applications

Unspecified application

Species

Unspecified reactive species

Yu Zhu,Tong Wang,Wenwen Zhu,Quhao Wei

Microbiology spectrum :e0417922 PubMed36790208

2023

Legionella longbeachae Regulates the Association of Polyubiquitinated Proteins on Bacterial Phagosome with Multiple Deubiquitinases.

Applications

Unspecified application

Species

Unspecified reactive species

Yunjia Shi,Hongtao Liu,Kelong Ma,Zhao-Qing Luo,Jiazhang Qiu

PloS one 18:e0281587 PubMed36758031

2023

Legionella longbeachae effector protein RavZ inhibits autophagy and regulates phagosome ubiquitination during infection.

Applications

Unspecified application

Species

Unspecified reactive species

Yunjia Shi,Hongtao Liu,Kelong Ma,Zhao-Qing Luo,Jiazhang Qiu

Membranes 11: PubMed34832035

2021

In Vivo Secretion of β-Lactamase-Carrying Outer Membrane Vesicles as a Mechanism of β-Lactam Therapy Failure.

Applications

Unspecified application

Species

Unspecified reactive species

Martina Bielaszewska,Ondřej Daniel,Otakar Nyč,Alexander Mellmann

The EMBO journal 40:e105202 PubMed33410511

2021

Crystal structure of bacterial cytotoxic necrotizing factor CNF reveals molecular building blocks for intoxication.

Applications

Unspecified application

Species

Unspecified reactive species

Paweena Chaoprasid,Peer Lukat,Sabrina Mühlen,Thomas Heidler,Emerich-Mihai Gazdag,Shuangshuang Dong,Wenjie Bi,Christian Rüter,Marco Kirchenwitz,Anika Steffen,Lothar Jänsch,Theresia E B Stradal,Petra Dersch,Wulf Blankenfeldt

Developmental cell 55:784-801.e9 PubMed33296682

2020

Programmable Extracellular Vesicles for Macromolecule Delivery and Genome Modifications.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaojuan Zhang,Quanbin Xu,Zhike Zi,Zeyu Liu,Chun Wan,Lauren Crisman,Jingshi Shen,Xuedong Liu

Frontiers in microbiology 11:1374 PubMed32714302

2020

CexE Is a Coat Protein and Virulence Factor of Diarrheagenic Pathogens.

Applications

Unspecified application

Species

Unspecified reactive species

Zachary P Rivas,Kacey M Talbot,Leidy C Merselis,Ryan M McCormack,Becky Adkins,George P Munson

PLoS neglected tropical diseases 14:e0008128 PubMed32236098

2020

Deciphering the possible role of ctxB7 allele on higher production of cholera toxin by Haitian variant Vibrio cholerae O1.

Applications

Unspecified application

Species

Unspecified reactive species

Arindam Naha,Rahul Shubhra Mandal,Prosenjit Samanta,Rudra Narayan Saha,Sreeja Shaw,Amit Ghosh,Nabendu Sekhar Chatterjee,Pujarini Dutta,Keinosuke Okamoto,Shanta Dutta,Asish Kumar Mukhopadhyay

The Journal of antimicrobial chemotherapy 74:2904-2912 PubMed31335939

2019

A β-lactamase-producing plasmid from Neisseria gonorrhoeae carrying a unique 6 bp deletion in blaTEM-1 encoding a truncated 24 kDa TEM-1 penicillinase that hydrolyses ampicillin slowly.

Applications

Unspecified application

Species

Unspecified reactive species

Reema Singh,Sumudu R Perera,George S Katselis,Paulos Chumala,Irene Martin,Anthony Kusalik,Kristen M Mitzel,Jo-Anne R Dillon
View all publications

Product promise

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