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94
ATCC escherichia coli bl21 de3
Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.
Escherichia Coli Bl21 De3, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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New England Biolabs bl21 de3 competent e coli cells
Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.
Bl21 De3 Competent E Coli Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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New England Biolabs escherichia coli bl21 de3 competent cells
Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.
Escherichia Coli Bl21 De3 Competent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC virus strains escherichia coli bl21 de3 atcc n a
Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.
Virus Strains Escherichia Coli Bl21 De3 Atcc N A, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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97
New England Biolabs bl21 de3
Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.
Bl21 De3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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New England Biolabs e coli bl21
Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.
E Coli Bl21, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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New England Biolabs e coli bl21 de3
Functional modification of MtrC with a SpyTag bioconjugation domain in S. oneidensis and <t>E.</t> <t>coli</t> (A) Fusion of a SpyTag domain to the C-terminus of MtrC enables the bioconjugation of a SpyCatcher-fused fluorescent protein, facilitating selective surface labeling of modified cells. (B) The fluorescence of S. oneidensis cells was quantified by spectrofluorometry (arbitrary units) and shown as the mean of 3 separate experiments performed in triplicate with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). Expression of MtrC or MtrC-SpyTag in S. oneidensis cells was regulated using either a weak or strong RBS. (C) The fluorescence of E. coli cells expressing CymA-MtrCAB or CymA-MtrCAB-SpyTag shown as the mean of 3 separate experiments performed in triplicate, with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). (D) Fluorescence microscopy revealed observable mCerulean3 fluorescence for E. coli cells expressing CymA-MtrCAB-SpyTag compared with cells expressing CymA-MtrCAB following incubation with mCerulean3-SpyCatcher. Scale bars, 100 μm.
E Coli Bl21 De3, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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New England Biolabs e coli bl21 derivative strain
Functional modification of MtrC with a SpyTag bioconjugation domain in S. oneidensis and <t>E.</t> <t>coli</t> (A) Fusion of a SpyTag domain to the C-terminus of MtrC enables the bioconjugation of a SpyCatcher-fused fluorescent protein, facilitating selective surface labeling of modified cells. (B) The fluorescence of S. oneidensis cells was quantified by spectrofluorometry (arbitrary units) and shown as the mean of 3 separate experiments performed in triplicate with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). Expression of MtrC or MtrC-SpyTag in S. oneidensis cells was regulated using either a weak or strong RBS. (C) The fluorescence of E. coli cells expressing CymA-MtrCAB or CymA-MtrCAB-SpyTag shown as the mean of 3 separate experiments performed in triplicate, with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). (D) Fluorescence microscopy revealed observable mCerulean3 fluorescence for E. coli cells expressing CymA-MtrCAB-SpyTag compared with cells expressing CymA-MtrCAB following incubation with mCerulean3-SpyCatcher. Scale bars, 100 μm.
E Coli Bl21 Derivative Strain, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
ATCC e coli bl21 de3
Functional modification of MtrC with a SpyTag bioconjugation domain in S. oneidensis and <t>E.</t> <t>coli</t> (A) Fusion of a SpyTag domain to the C-terminus of MtrC enables the bioconjugation of a SpyCatcher-fused fluorescent protein, facilitating selective surface labeling of modified cells. (B) The fluorescence of S. oneidensis cells was quantified by spectrofluorometry (arbitrary units) and shown as the mean of 3 separate experiments performed in triplicate with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). Expression of MtrC or MtrC-SpyTag in S. oneidensis cells was regulated using either a weak or strong RBS. (C) The fluorescence of E. coli cells expressing CymA-MtrCAB or CymA-MtrCAB-SpyTag shown as the mean of 3 separate experiments performed in triplicate, with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). (D) Fluorescence microscopy revealed observable mCerulean3 fluorescence for E. coli cells expressing CymA-MtrCAB-SpyTag compared with cells expressing CymA-MtrCAB following incubation with mCerulean3-SpyCatcher. Scale bars, 100 μm.
E Coli Bl21 De3, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.

Journal: Poultry Science

Article Title: Research note: Antimicrobial properties of commercial black soldier fly ( Hermetia illucens ) meal against gram-positive and gram-negative bacteria

doi: 10.1016/j.psj.2026.106424

Figure Lengend Snippet: Part A: Representative images of disk diffusion assay in which the clear zone showed bacterial growth inhibition. BSFM, BSFL extract and BSF oil were applied to the disk for testing growth inhibition against the bacteria mentioned above. BSF oil was obtained from the mechanical compression of dried BSFL for producing BSFM. Part B: Antibacterial activities of BSFL extract (top) and BSFM extract (bottom) for 24 h (monitored by OD 600 ). BSFL and BSFM extracts were separately treated with (left) E. coli , (middle) S. aureus and (right) S. enteritidis , ranging from 0.39 to 100 mg/mL with half dilution. Each data point is represented by mean ± std (n=3). Part C: MICs of BSFM and BSFL extracts against the tested bacteria.

Article Snippet: Bacteria species used in this study included Staphylococcus aureus (ATCC 31290), Escherichia coli (BL21(DE3)), Salmonella enterica (ATCC 14028), Salmonella enteritidis (ATCC 13076) and Salmonella typhimurium (NCTC 8391).

Techniques: Diffusion-based Assay, Inhibition, Bacteria

Functional modification of MtrC with a SpyTag bioconjugation domain in S. oneidensis and E. coli (A) Fusion of a SpyTag domain to the C-terminus of MtrC enables the bioconjugation of a SpyCatcher-fused fluorescent protein, facilitating selective surface labeling of modified cells. (B) The fluorescence of S. oneidensis cells was quantified by spectrofluorometry (arbitrary units) and shown as the mean of 3 separate experiments performed in triplicate with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). Expression of MtrC or MtrC-SpyTag in S. oneidensis cells was regulated using either a weak or strong RBS. (C) The fluorescence of E. coli cells expressing CymA-MtrCAB or CymA-MtrCAB-SpyTag shown as the mean of 3 separate experiments performed in triplicate, with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). (D) Fluorescence microscopy revealed observable mCerulean3 fluorescence for E. coli cells expressing CymA-MtrCAB-SpyTag compared with cells expressing CymA-MtrCAB following incubation with mCerulean3-SpyCatcher. Scale bars, 100 μm.

Journal: iScience

Article Title: Engineering electron conduits in bacteria for selective biointerfacing and enhanced energy transfer

doi: 10.1016/j.isci.2026.114805

Figure Lengend Snippet: Functional modification of MtrC with a SpyTag bioconjugation domain in S. oneidensis and E. coli (A) Fusion of a SpyTag domain to the C-terminus of MtrC enables the bioconjugation of a SpyCatcher-fused fluorescent protein, facilitating selective surface labeling of modified cells. (B) The fluorescence of S. oneidensis cells was quantified by spectrofluorometry (arbitrary units) and shown as the mean of 3 separate experiments performed in triplicate with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). Expression of MtrC or MtrC-SpyTag in S. oneidensis cells was regulated using either a weak or strong RBS. (C) The fluorescence of E. coli cells expressing CymA-MtrCAB or CymA-MtrCAB-SpyTag shown as the mean of 3 separate experiments performed in triplicate, with subtracted background fluorescence of unreacted control cells. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test). (D) Fluorescence microscopy revealed observable mCerulean3 fluorescence for E. coli cells expressing CymA-MtrCAB-SpyTag compared with cells expressing CymA-MtrCAB following incubation with mCerulean3-SpyCatcher. Scale bars, 100 μm.

Article Snippet: E. coli BL21 (DE3) , NEB , Cat#C2527.

Techniques: Functional Assay, Modification, Labeling, Fluorescence, Control, Standard Deviation, One-tailed Test, Expressing, Microscopy, Incubation

Extracellular substrate reduction by S. oneidensis and E. coli cells that express engineered MtrC proteins (A) Reduction of iron(III) to iron(II) by wild-type S. oneidensis , compared to a Δ mtrC /Δ mtrF /Δ omcA knockout strain. The Δ mtrC /Δ mtrF /Δ omcA knockout strain was subsequently engineered to express MtrC or MtrC-SpyTag. The formation of iron(II) after 16 h of anaerobic culture was quantified using a ferrozine assay and shown as a mean of three experiments with three biological repeats. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, two-tailed t test). (B) Reduction of methyl orange with electrons from E. coli BL21(DE3) cells containing only the pEC86 plasmid, or cells co-expressing either the CymA-MtrCAB complex, CymA-MtrCAB with SpyTag, or CymA-MtrCAB with GrBP5. The change in methyl orange absorbance at 465 nm upon the reduction of the azo group was measured after 24 h of anaerobic culture, and is shown as a mean of three experiments with three biological repeats ( n = 3, significance calculated using a parametric, unpaired, two-tailed t test). Error bars represent the standard deviation between experiments.

Journal: iScience

Article Title: Engineering electron conduits in bacteria for selective biointerfacing and enhanced energy transfer

doi: 10.1016/j.isci.2026.114805

Figure Lengend Snippet: Extracellular substrate reduction by S. oneidensis and E. coli cells that express engineered MtrC proteins (A) Reduction of iron(III) to iron(II) by wild-type S. oneidensis , compared to a Δ mtrC /Δ mtrF /Δ omcA knockout strain. The Δ mtrC /Δ mtrF /Δ omcA knockout strain was subsequently engineered to express MtrC or MtrC-SpyTag. The formation of iron(II) after 16 h of anaerobic culture was quantified using a ferrozine assay and shown as a mean of three experiments with three biological repeats. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, two-tailed t test). (B) Reduction of methyl orange with electrons from E. coli BL21(DE3) cells containing only the pEC86 plasmid, or cells co-expressing either the CymA-MtrCAB complex, CymA-MtrCAB with SpyTag, or CymA-MtrCAB with GrBP5. The change in methyl orange absorbance at 465 nm upon the reduction of the azo group was measured after 24 h of anaerobic culture, and is shown as a mean of three experiments with three biological repeats ( n = 3, significance calculated using a parametric, unpaired, two-tailed t test). Error bars represent the standard deviation between experiments.

Article Snippet: E. coli BL21 (DE3) , NEB , Cat#C2527.

Techniques: Knock-Out, Ferrozine Assay, Standard Deviation, Two Tailed Test, Plasmid Preparation, Expressing

Improved graphite binding by S. oneidensis and E. coli cells expressing MtrC-GrBP5 (A) Illustration shows the C-terminal modification of MtrC with a graphite binding domain to improve the affinity of S. oneidensis cells to a graphite electrode. (B) SEM images of graphite felt fibers with no cells, as well as with bound S. oneidensis Δ mtrC /Δ mtrF /Δ omcA cells expressing either MtrC or MtrC-GrBP5 (scale bars, 5 μm). (C) SEM images of graphite felt fibers with no cells, as well as with bound E. coli BL21(DE3) expressing either CymA-MtrCAB or CymA-MtrCAB-GrBP5 (scale bars, 5 μm). (D) Lysed protein content from a graphite felt electrode aerobically incubated with S. oneidensis or E. coli cells expressing MtrC with or without the GrBP5 binding domain. The data represent the mean protein per cm 2 of geometric surface area of graphite felt electrode (mg/cm 2 ) in cell lysate from three biological replicates from three separate experiments of S. oneidensis Δ mtrC /Δ mtrF /Δ omcA cells expressing recombinant MtrC or MtrC-GrBP5, or of E. coli BL21(DE3) cells expressing CymA-MtrCAB-GrBP5 compared to CymA-MtrCAB. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test).

Journal: iScience

Article Title: Engineering electron conduits in bacteria for selective biointerfacing and enhanced energy transfer

doi: 10.1016/j.isci.2026.114805

Figure Lengend Snippet: Improved graphite binding by S. oneidensis and E. coli cells expressing MtrC-GrBP5 (A) Illustration shows the C-terminal modification of MtrC with a graphite binding domain to improve the affinity of S. oneidensis cells to a graphite electrode. (B) SEM images of graphite felt fibers with no cells, as well as with bound S. oneidensis Δ mtrC /Δ mtrF /Δ omcA cells expressing either MtrC or MtrC-GrBP5 (scale bars, 5 μm). (C) SEM images of graphite felt fibers with no cells, as well as with bound E. coli BL21(DE3) expressing either CymA-MtrCAB or CymA-MtrCAB-GrBP5 (scale bars, 5 μm). (D) Lysed protein content from a graphite felt electrode aerobically incubated with S. oneidensis or E. coli cells expressing MtrC with or without the GrBP5 binding domain. The data represent the mean protein per cm 2 of geometric surface area of graphite felt electrode (mg/cm 2 ) in cell lysate from three biological replicates from three separate experiments of S. oneidensis Δ mtrC /Δ mtrF /Δ omcA cells expressing recombinant MtrC or MtrC-GrBP5, or of E. coli BL21(DE3) cells expressing CymA-MtrCAB-GrBP5 compared to CymA-MtrCAB. Error bars represent standard deviation between experiments ( n = 3, significance calculated using a parametric, unpaired, one-tailed t test).

Article Snippet: E. coli BL21 (DE3) , NEB , Cat#C2527.

Techniques: Binding Assay, Expressing, Modification, Incubation, Recombinant, Standard Deviation, One-tailed Test