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Inhibition of Beta-Lactamase Enzymes from US Patent US10800778: "Beta-lactamase inhibitor compounds"
Assay data:39 Active, 1 Activity ≤ 1 nM, 38 Activity ≤ 1 µM, 40 Tested
SummaryCompounds, ActiveCompounds, activity ≤ 1 µMRelated BioAssays by Target
Test for beta-lactamase Inhibitory Activity from US Patent US10544146: "Bicyclic compounds and their use as antibacterial agents and β-lactamase inhibitors"
Assay data:1 Active, 1 Activity ≤ 1 µM, 1 Tested
Cell Free Inhibition Assay from US Patent US9120808: "Substituted clavulanic acid"
Assay data:38 Active, 3 Activity ≤ 1 nM, 30 Activity ≤ 1 µM, 42 Tested
Steady-State Kinetics Assay from Article 10.1021/bi501197t: "Detecting a quasi-stable imine species on the reaction pathway of SHV-1 -lactamase and 6 -(hydroxymethyl)penicillanic acid sulfone."
Assay data:4 Active, 2 Activity ≤ 1 µM, 4 Tested
SummaryCompounds, ActiveCompounds, activity ≤ 1 µMPubMed CitationRelated BioAssays by Target
Inhibition Assay from Article 10.1016/S1074-5521(01)00034-5: "Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase."
Assay data:33 Active, 17 Activity ≤ 1 µM, 41 Tested
Inhibition of bacterial Beta-lactamase TEM-1 (24 - 286) (unknown origin) expressed in Escherichia coli Transetta (DE3)
Assay data:10 Active, 2 Activity ≤ 1 µM, 22 Tested
Inhibition of bacterial wild type Beta-lactamase TEM-1 pre-incubated for 5 mins before addition of chromogenic beta-lactamase substrate CENTA by spectrophotometry
Assay data:1 Active, 3 Tested
SummaryCompounds, ActivePubMed CitationRelated BioAssays by Target
Binding affinity to bacterial wild type Beta-lactamase TEM-1 assessed as change in melting temperature at 100-fold molar excess compound concentration relative to apo-enzymes by SYPRO Orange dye based differential scanning fluorimetry
Assay data:1 Tested
SummaryPubMed CitationRelated BioAssays by Target
Inhibition of Escherichia coli TEM-1 beta-lactamase
Inhibition of beta-lactamase TEM-1 in Escherichia coli GN5482 assessed as potentiation of ceftazidime-induced antibacterial activity by measuring ceftazidime MIC (Rvb = 4 ug/ml)
Inhibition of bacterial N-terminal His-tagged TEV protease site linked TEM-1 (24 to 286 amino acids) expressed in Escherichia coli Transetta (DE3) preincubated for 10 mins followed by FC5 fluorescent substrate addition by fluorescence assay
Assay data:7 Active, 1 Activity ≤ 1 µM, 35 Tested
Inhibition of bacterial beta lactamase TEM-1 after 5 mins
Assay data:1 Activity ≤ 1 µM, 1 Tested
SummaryCompounds, activity ≤ 1 µMPubMed CitationRelated BioAssays by Target
Inhibition of bacterial beta lactamase TEM-1
Inhibition of TEM-1 in penicillin-resistant Escherichia coli TG1 transfected with pBGS18 plasmid encoding replication origin and kanamycin resistance assessed as potentiation of ampicillin-induced antibacterial activity by measuring ampicillin MIC at 16 ug/mL in Mueller-Hinton broth by CLSI protocol based method (Rvb > 1024 ug/mL)
Assay data:8 Tested
Inhibition of bacterial beta-lactamase TEM-1
Assay data:1 Active, 1 Tested
Inhibition of recombinant bacterial class A serine beta-lactamase TEM-1 expressed in Escherichia coli assessed as reduction in breakdown of cephalosporin FC-5 preincubated for 10 mins followed by cephalosporin FC-5 addition by fluorescence method
Inhibition of recombinant N-terminal His-tagged Escherichia coli TEM1 (24 to 286 residues) expressed in Escherichia coli BL21(DE3) at 200 uM using FC5 as substrate
Assay data:57 Tested
Inhibition of recombinant N-terminal His-tagged Escherichia coli TEM1 (24 to 286 residues) expressed in Escherichia coli BL21(DE3) using FC5 as substrate assessed as residual activity at 200 uM
Assay data:2 Tested
Inhibition of recombinant N-terminal His-tagged bacterial Escherichia coli TEM-1 (24 to 286 residues) expressed in Escherichia coli BL21 (DE3) cells using FC5 as substrate preincubated up to 360 mins prior to substrate addition by fluorescence-based assay
Assay data:1 Active, 2 Tested
Inhibition of Klebsiella pneumoniae KP1004 TEM-1 assessed as imipenem MIC at 4 ug/ml by broth microdilution method
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