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e coli atcc 8739 genome database  (ATCC)


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    ATCC e coli atcc 8739 genome database
    Membrane integrity or damage and morphology of <t>E.</t> <t>coli</t> following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.
    E Coli Atcc 8739 Genome Database, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 6583 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli atcc 8739 genome database/product/ATCC
    Average 99 stars, based on 6583 article reviews
    e coli atcc 8739 genome database - by Bioz Stars, 2026-06
    99/100 stars

    Images

    1) Product Images from "A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B"

    Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

    Journal: Current Research in Microbial Sciences

    doi: 10.1016/j.crmicr.2025.100535

    Membrane integrity or damage and morphology of E. coli following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.
    Figure Legend Snippet: Membrane integrity or damage and morphology of E. coli following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.

    Techniques Used: Membrane, Staining, Microscopy, Fluorescence, Control

    In vitro interaction of NCR169C 17–38 , NCR169, NCR169 16–27 and NCR169 17–27 with nucleic acids. (A) Gel retardation assay of 100 ng E. coli genomic DNA incubated with 0, 10, or 100 µM peptide. (B) Same setup as in (A), but using 100 ng E. coli total RNA. (C) Interaction of NCR169C 17–38 with 250 ng circular plasmid DNA at varying concentrations. (D) Real-time monitoring of DNA binding by fluorescence of SYBR Gold–DNA complexes (excitation 490 nm, emission 535 nm). Peptides (10 µM) were added to 100 ng DNA at 0 or 14 min (red arrows); Proteinase K (1 mg/mL) was added at 27 min (black arrow).
    Figure Legend Snippet: In vitro interaction of NCR169C 17–38 , NCR169, NCR169 16–27 and NCR169 17–27 with nucleic acids. (A) Gel retardation assay of 100 ng E. coli genomic DNA incubated with 0, 10, or 100 µM peptide. (B) Same setup as in (A), but using 100 ng E. coli total RNA. (C) Interaction of NCR169C 17–38 with 250 ng circular plasmid DNA at varying concentrations. (D) Real-time monitoring of DNA binding by fluorescence of SYBR Gold–DNA complexes (excitation 490 nm, emission 535 nm). Peptides (10 µM) were added to 100 ng DNA at 0 or 14 min (red arrows); Proteinase K (1 mg/mL) was added at 27 min (black arrow).

    Techniques Used: In Vitro, Electrophoretic Mobility Shift Assay, Incubation, Plasmid Preparation, Binding Assay, Fluorescence

    GO enrichment analysis of DEGs in E coli treated with NCR169C 17–38 annotated in three main categories: (A) biological process, (B) molecular function, and (C) cellular component.
    Figure Legend Snippet: GO enrichment analysis of DEGs in E coli treated with NCR169C 17–38 annotated in three main categories: (A) biological process, (B) molecular function, and (C) cellular component.

    Techniques Used:



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    e coli atcc 8739 genome database  (ATCC)
    99
    ATCC e coli atcc 8739 genome database
    Membrane integrity or damage and morphology of <t>E.</t> <t>coli</t> following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.
    E Coli Atcc 8739 Genome Database, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli atcc 8739 genome database/product/ATCC
    Average 99 stars, based on 1 article reviews
    e coli atcc 8739 genome database - by Bioz Stars, 2026-06
    99/100 stars
    		  Buy from Supplier

    Image Search Results


    Membrane integrity or damage and morphology of E. coli following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.

    Journal: Current Research in Microbial Sciences

    Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

    doi: 10.1016/j.crmicr.2025.100535

    Figure Lengend Snippet: Membrane integrity or damage and morphology of E. coli following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.

    Article Snippet: The trimmed samples were aligned to the E. coli ATCC_8739 genome database using STAR ( ) as described by ( ; supplementary Table 37).

    Techniques: Membrane, Staining, Microscopy, Fluorescence, Control

    In vitro interaction of NCR169C 17–38 , NCR169, NCR169 16–27 and NCR169 17–27 with nucleic acids. (A) Gel retardation assay of 100 ng E. coli genomic DNA incubated with 0, 10, or 100 µM peptide. (B) Same setup as in (A), but using 100 ng E. coli total RNA. (C) Interaction of NCR169C 17–38 with 250 ng circular plasmid DNA at varying concentrations. (D) Real-time monitoring of DNA binding by fluorescence of SYBR Gold–DNA complexes (excitation 490 nm, emission 535 nm). Peptides (10 µM) were added to 100 ng DNA at 0 or 14 min (red arrows); Proteinase K (1 mg/mL) was added at 27 min (black arrow).

    Journal: Current Research in Microbial Sciences

    Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

    doi: 10.1016/j.crmicr.2025.100535

    Figure Lengend Snippet: In vitro interaction of NCR169C 17–38 , NCR169, NCR169 16–27 and NCR169 17–27 with nucleic acids. (A) Gel retardation assay of 100 ng E. coli genomic DNA incubated with 0, 10, or 100 µM peptide. (B) Same setup as in (A), but using 100 ng E. coli total RNA. (C) Interaction of NCR169C 17–38 with 250 ng circular plasmid DNA at varying concentrations. (D) Real-time monitoring of DNA binding by fluorescence of SYBR Gold–DNA complexes (excitation 490 nm, emission 535 nm). Peptides (10 µM) were added to 100 ng DNA at 0 or 14 min (red arrows); Proteinase K (1 mg/mL) was added at 27 min (black arrow).

    Article Snippet: The trimmed samples were aligned to the E. coli ATCC_8739 genome database using STAR ( ) as described by ( ; supplementary Table 37).

    Techniques: In Vitro, Electrophoretic Mobility Shift Assay, Incubation, Plasmid Preparation, Binding Assay, Fluorescence

    GO enrichment analysis of DEGs in E coli treated with NCR169C 17–38 annotated in three main categories: (A) biological process, (B) molecular function, and (C) cellular component.

    Journal: Current Research in Microbial Sciences

    Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

    doi: 10.1016/j.crmicr.2025.100535

    Figure Lengend Snippet: GO enrichment analysis of DEGs in E coli treated with NCR169C 17–38 annotated in three main categories: (A) biological process, (B) molecular function, and (C) cellular component.

    Article Snippet: The trimmed samples were aligned to the E. coli ATCC_8739 genome database using STAR ( ) as described by ( ; supplementary Table 37).

    Techniques: