ciprofloxacin  (ATCC)


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    ATCC ciprofloxacin
    (A) Correlation between transcriptomics and proteomics data after they were filtered based on an adjusted P value of 0.05. The Pearson correlation coefficient between both data sets is 0.84. (B) Venn diagram depicting the relationship between genes and proteins that had a log 2 fold change of greater or less than 1.5 (adjusted P value of <0.05). The proteomics data set is represented by the blue oval, and the transcriptomics data set is represented by red. The expression of 16 intersecting genes and proteins was greater than 1.5 (log 2 fold change), and the expression of 8 was less than 1.5 (log 2 fold change). (C) Intersecting genes and proteins from the Venn diagram were identified and plotted in a heat map. (D) Functional class analysis of genes/proteins based on COG categories. Bars represent the number of genes (blue) or proteins (red) in each COG category that had either increased or decreased expression by a log 2 fold change of greater than 1.5 or less than 1.5 (adjusted P value of <0.05), respectively. (E) The transcriptional (blue) and proteomic (red) response of A. baumannii AB5075-UW to <t>ciprofloxacin</t> shock treatment. Each point in the graph represents a single ORF within the genome, arranged according to their location in the genome on the x axis and their fold change (log 2 ) in expression on the y axis, following treatment with 31.25 μg/ml ciprofloxacin for 1 h. (F) Distribution of DNA reads along AB5075-UW chromosome of ciprofloxacin-treated (31.25 μg/ml, 1 h) and control (no treatment). The height of the graph shows the coverage of reads represented as minimum (red), average (purple), and maximum (blue).
    Ciprofloxacin, 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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    Images

    1) Product Images from "Identification of a Novel Ciprofloxacin Tolerance Gene, aciT , Which Contributes to Filamentation in Acinetobacter baumannii"

    Article Title: Identification of a Novel Ciprofloxacin Tolerance Gene, aciT , Which Contributes to Filamentation in Acinetobacter baumannii

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01400-20

    (A) Correlation between transcriptomics and proteomics data after they were filtered based on an adjusted P value of 0.05. The Pearson correlation coefficient between both data sets is 0.84. (B) Venn diagram depicting the relationship between genes and proteins that had a log 2 fold change of greater or less than 1.5 (adjusted P value of <0.05). The proteomics data set is represented by the blue oval, and the transcriptomics data set is represented by red. The expression of 16 intersecting genes and proteins was greater than 1.5 (log 2 fold change), and the expression of 8 was less than 1.5 (log 2 fold change). (C) Intersecting genes and proteins from the Venn diagram were identified and plotted in a heat map. (D) Functional class analysis of genes/proteins based on COG categories. Bars represent the number of genes (blue) or proteins (red) in each COG category that had either increased or decreased expression by a log 2 fold change of greater than 1.5 or less than 1.5 (adjusted P value of <0.05), respectively. (E) The transcriptional (blue) and proteomic (red) response of A. baumannii AB5075-UW to ciprofloxacin shock treatment. Each point in the graph represents a single ORF within the genome, arranged according to their location in the genome on the x axis and their fold change (log 2 ) in expression on the y axis, following treatment with 31.25 μg/ml ciprofloxacin for 1 h. (F) Distribution of DNA reads along AB5075-UW chromosome of ciprofloxacin-treated (31.25 μg/ml, 1 h) and control (no treatment). The height of the graph shows the coverage of reads represented as minimum (red), average (purple), and maximum (blue).
    Figure Legend Snippet: (A) Correlation between transcriptomics and proteomics data after they were filtered based on an adjusted P value of 0.05. The Pearson correlation coefficient between both data sets is 0.84. (B) Venn diagram depicting the relationship between genes and proteins that had a log 2 fold change of greater or less than 1.5 (adjusted P value of <0.05). The proteomics data set is represented by the blue oval, and the transcriptomics data set is represented by red. The expression of 16 intersecting genes and proteins was greater than 1.5 (log 2 fold change), and the expression of 8 was less than 1.5 (log 2 fold change). (C) Intersecting genes and proteins from the Venn diagram were identified and plotted in a heat map. (D) Functional class analysis of genes/proteins based on COG categories. Bars represent the number of genes (blue) or proteins (red) in each COG category that had either increased or decreased expression by a log 2 fold change of greater than 1.5 or less than 1.5 (adjusted P value of <0.05), respectively. (E) The transcriptional (blue) and proteomic (red) response of A. baumannii AB5075-UW to ciprofloxacin shock treatment. Each point in the graph represents a single ORF within the genome, arranged according to their location in the genome on the x axis and their fold change (log 2 ) in expression on the y axis, following treatment with 31.25 μg/ml ciprofloxacin for 1 h. (F) Distribution of DNA reads along AB5075-UW chromosome of ciprofloxacin-treated (31.25 μg/ml, 1 h) and control (no treatment). The height of the graph shows the coverage of reads represented as minimum (red), average (purple), and maximum (blue).

    Techniques Used: Expressing, Functional Assay

    (A) Graph shows 6.25-h growth rate in Mueller-Hinton broth of AB5075-UW (parental strain, blue line), AB5075-UW expressing empty pVRL1Z plasmid (light blue), the AB00272 mutant strain (ABUW_0098 gene insertionally inactivated) (red), AB00272 mutant strain expressing empty pVRL1Z plasmid (light red), and AB00272 mutant strain complemented with pVRL1Z ABUW_0098 (black). (B) All AB5075-UW constructs shocked with 31.25 μg/ml of ciprofloxacin after 2 h 6 min of growth. (C) All AB5075-UW constructs shocked with 46.87 μg/ml of ciprofloxacin after 2 h 6 min of growth. (D) All AB5075-UW constructs shocked with 62.5 μg/ml of ciprofloxacin after 2 h 6 min of growth (OD 600 of ∼0.5). Growth of the ΔABUW_0098 mutant strain, AB00272, was significantly inhibited in the presence of ciprofloxacin. Error bars show the standard errors from three independent experiments. (E) Cell morphology of AB5075-UW expressing empty pVRL1Z plasmid, the AB00272 mutant strain expressing empty pVRL1Z plasmid, and the AB00272 mutant strain complemented with pVRL1Z ABUW_0098 grown without antibiotics to mid-log phase (no treatment) followed by exposure to a sub-MIC of ciprofloxacin (31.25 μg/ml) at 1, 2, and 4 h. Scale bar, 2 μm.
    Figure Legend Snippet: (A) Graph shows 6.25-h growth rate in Mueller-Hinton broth of AB5075-UW (parental strain, blue line), AB5075-UW expressing empty pVRL1Z plasmid (light blue), the AB00272 mutant strain (ABUW_0098 gene insertionally inactivated) (red), AB00272 mutant strain expressing empty pVRL1Z plasmid (light red), and AB00272 mutant strain complemented with pVRL1Z ABUW_0098 (black). (B) All AB5075-UW constructs shocked with 31.25 μg/ml of ciprofloxacin after 2 h 6 min of growth. (C) All AB5075-UW constructs shocked with 46.87 μg/ml of ciprofloxacin after 2 h 6 min of growth. (D) All AB5075-UW constructs shocked with 62.5 μg/ml of ciprofloxacin after 2 h 6 min of growth (OD 600 of ∼0.5). Growth of the ΔABUW_0098 mutant strain, AB00272, was significantly inhibited in the presence of ciprofloxacin. Error bars show the standard errors from three independent experiments. (E) Cell morphology of AB5075-UW expressing empty pVRL1Z plasmid, the AB00272 mutant strain expressing empty pVRL1Z plasmid, and the AB00272 mutant strain complemented with pVRL1Z ABUW_0098 grown without antibiotics to mid-log phase (no treatment) followed by exposure to a sub-MIC of ciprofloxacin (31.25 μg/ml) at 1, 2, and 4 h. Scale bar, 2 μm.

    Techniques Used: Expressing, Plasmid Preparation, Mutagenesis, Construct

    (A) Tree showing the phylogenetic relationship of ABUW_0098 protein. The tree was generated using iTOL from a Clustal Omega alignment of protein sequence obtained from the National Center for Biotechnology Information database. (B) Predicted transmembrane topology of the ABUW_0098 protein (AciT) based on predictions made using TMHMM . This protein is predicted to have three transmembrane α-helices. (C) Induction of ABUW_0098 ( aciT ) homologs by ciprofloxacin in A. baumannii strains ACICU, AYE, ATCC 17978, ATCC 19606, and D1279779. A subinhibitory concentration of ciprofloxacin was added to the medium when cells were in the exponential growth phase. The bars represent a change in aciT gene expression compared with an untreated control after 1 h of growth in the presence of ciprofloxacin. Error bars show the standard errors from at least 2 biological and 4 technical replicates.
    Figure Legend Snippet: (A) Tree showing the phylogenetic relationship of ABUW_0098 protein. The tree was generated using iTOL from a Clustal Omega alignment of protein sequence obtained from the National Center for Biotechnology Information database. (B) Predicted transmembrane topology of the ABUW_0098 protein (AciT) based on predictions made using TMHMM . This protein is predicted to have three transmembrane α-helices. (C) Induction of ABUW_0098 ( aciT ) homologs by ciprofloxacin in A. baumannii strains ACICU, AYE, ATCC 17978, ATCC 19606, and D1279779. A subinhibitory concentration of ciprofloxacin was added to the medium when cells were in the exponential growth phase. The bars represent a change in aciT gene expression compared with an untreated control after 1 h of growth in the presence of ciprofloxacin. Error bars show the standard errors from at least 2 biological and 4 technical replicates.

    Techniques Used: Generated, Sequencing, Concentration Assay, Expressing

    ciprofloxacin  (ATCC)


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    ATCC ciprofloxacin
    (A) Correlation between transcriptomics and proteomics data after they were filtered based on an adjusted P value of 0.05. The Pearson correlation coefficient between both data sets is 0.84. (B) Venn diagram depicting the relationship between genes and proteins that had a log 2 fold change of greater or less than 1.5 (adjusted P value of <0.05). The proteomics data set is represented by the blue oval, and the transcriptomics data set is represented by red. The expression of 16 intersecting genes and proteins was greater than 1.5 (log 2 fold change), and the expression of 8 was less than 1.5 (log 2 fold change). (C) Intersecting genes and proteins from the Venn diagram were identified and plotted in a heat map. (D) Functional class analysis of genes/proteins based on COG categories. Bars represent the number of genes (blue) or proteins (red) in each COG category that had either increased or decreased expression by a log 2 fold change of greater than 1.5 or less than 1.5 (adjusted P value of <0.05), respectively. (E) The transcriptional (blue) and proteomic (red) response of A. baumannii AB5075-UW to <t>ciprofloxacin</t> shock treatment. Each point in the graph represents a single ORF within the genome, arranged according to their location in the genome on the x axis and their fold change (log 2 ) in expression on the y axis, following treatment with 31.25 μg/ml ciprofloxacin for 1 h. (F) Distribution of DNA reads along AB5075-UW chromosome of ciprofloxacin-treated (31.25 μg/ml, 1 h) and control (no treatment). The height of the graph shows the coverage of reads represented as minimum (red), average (purple), and maximum (blue).
    Ciprofloxacin, 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
    https://www.bioz.com/result/ciprofloxacin/product/ATCC
    Average 94 stars, based on 1 article reviews
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    ciprofloxacin - by Bioz Stars, 2023-06
    94/100 stars

    Images

    1) Product Images from "Identification of a Novel Ciprofloxacin Tolerance Gene, aciT , Which Contributes to Filamentation in Acinetobacter baumannii"

    Article Title: Identification of a Novel Ciprofloxacin Tolerance Gene, aciT , Which Contributes to Filamentation in Acinetobacter baumannii

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01400-20

    (A) Correlation between transcriptomics and proteomics data after they were filtered based on an adjusted P value of 0.05. The Pearson correlation coefficient between both data sets is 0.84. (B) Venn diagram depicting the relationship between genes and proteins that had a log 2 fold change of greater or less than 1.5 (adjusted P value of <0.05). The proteomics data set is represented by the blue oval, and the transcriptomics data set is represented by red. The expression of 16 intersecting genes and proteins was greater than 1.5 (log 2 fold change), and the expression of 8 was less than 1.5 (log 2 fold change). (C) Intersecting genes and proteins from the Venn diagram were identified and plotted in a heat map. (D) Functional class analysis of genes/proteins based on COG categories. Bars represent the number of genes (blue) or proteins (red) in each COG category that had either increased or decreased expression by a log 2 fold change of greater than 1.5 or less than 1.5 (adjusted P value of <0.05), respectively. (E) The transcriptional (blue) and proteomic (red) response of A. baumannii AB5075-UW to ciprofloxacin shock treatment. Each point in the graph represents a single ORF within the genome, arranged according to their location in the genome on the x axis and their fold change (log 2 ) in expression on the y axis, following treatment with 31.25 μg/ml ciprofloxacin for 1 h. (F) Distribution of DNA reads along AB5075-UW chromosome of ciprofloxacin-treated (31.25 μg/ml, 1 h) and control (no treatment). The height of the graph shows the coverage of reads represented as minimum (red), average (purple), and maximum (blue).
    Figure Legend Snippet: (A) Correlation between transcriptomics and proteomics data after they were filtered based on an adjusted P value of 0.05. The Pearson correlation coefficient between both data sets is 0.84. (B) Venn diagram depicting the relationship between genes and proteins that had a log 2 fold change of greater or less than 1.5 (adjusted P value of <0.05). The proteomics data set is represented by the blue oval, and the transcriptomics data set is represented by red. The expression of 16 intersecting genes and proteins was greater than 1.5 (log 2 fold change), and the expression of 8 was less than 1.5 (log 2 fold change). (C) Intersecting genes and proteins from the Venn diagram were identified and plotted in a heat map. (D) Functional class analysis of genes/proteins based on COG categories. Bars represent the number of genes (blue) or proteins (red) in each COG category that had either increased or decreased expression by a log 2 fold change of greater than 1.5 or less than 1.5 (adjusted P value of <0.05), respectively. (E) The transcriptional (blue) and proteomic (red) response of A. baumannii AB5075-UW to ciprofloxacin shock treatment. Each point in the graph represents a single ORF within the genome, arranged according to their location in the genome on the x axis and their fold change (log 2 ) in expression on the y axis, following treatment with 31.25 μg/ml ciprofloxacin for 1 h. (F) Distribution of DNA reads along AB5075-UW chromosome of ciprofloxacin-treated (31.25 μg/ml, 1 h) and control (no treatment). The height of the graph shows the coverage of reads represented as minimum (red), average (purple), and maximum (blue).

    Techniques Used: Expressing, Functional Assay

    (A) Graph shows 6.25-h growth rate in Mueller-Hinton broth of AB5075-UW (parental strain, blue line), AB5075-UW expressing empty pVRL1Z plasmid (light blue), the AB00272 mutant strain (ABUW_0098 gene insertionally inactivated) (red), AB00272 mutant strain expressing empty pVRL1Z plasmid (light red), and AB00272 mutant strain complemented with pVRL1Z ABUW_0098 (black). (B) All AB5075-UW constructs shocked with 31.25 μg/ml of ciprofloxacin after 2 h 6 min of growth. (C) All AB5075-UW constructs shocked with 46.87 μg/ml of ciprofloxacin after 2 h 6 min of growth. (D) All AB5075-UW constructs shocked with 62.5 μg/ml of ciprofloxacin after 2 h 6 min of growth (OD 600 of ∼0.5). Growth of the ΔABUW_0098 mutant strain, AB00272, was significantly inhibited in the presence of ciprofloxacin. Error bars show the standard errors from three independent experiments. (E) Cell morphology of AB5075-UW expressing empty pVRL1Z plasmid, the AB00272 mutant strain expressing empty pVRL1Z plasmid, and the AB00272 mutant strain complemented with pVRL1Z ABUW_0098 grown without antibiotics to mid-log phase (no treatment) followed by exposure to a sub-MIC of ciprofloxacin (31.25 μg/ml) at 1, 2, and 4 h. Scale bar, 2 μm.
    Figure Legend Snippet: (A) Graph shows 6.25-h growth rate in Mueller-Hinton broth of AB5075-UW (parental strain, blue line), AB5075-UW expressing empty pVRL1Z plasmid (light blue), the AB00272 mutant strain (ABUW_0098 gene insertionally inactivated) (red), AB00272 mutant strain expressing empty pVRL1Z plasmid (light red), and AB00272 mutant strain complemented with pVRL1Z ABUW_0098 (black). (B) All AB5075-UW constructs shocked with 31.25 μg/ml of ciprofloxacin after 2 h 6 min of growth. (C) All AB5075-UW constructs shocked with 46.87 μg/ml of ciprofloxacin after 2 h 6 min of growth. (D) All AB5075-UW constructs shocked with 62.5 μg/ml of ciprofloxacin after 2 h 6 min of growth (OD 600 of ∼0.5). Growth of the ΔABUW_0098 mutant strain, AB00272, was significantly inhibited in the presence of ciprofloxacin. Error bars show the standard errors from three independent experiments. (E) Cell morphology of AB5075-UW expressing empty pVRL1Z plasmid, the AB00272 mutant strain expressing empty pVRL1Z plasmid, and the AB00272 mutant strain complemented with pVRL1Z ABUW_0098 grown without antibiotics to mid-log phase (no treatment) followed by exposure to a sub-MIC of ciprofloxacin (31.25 μg/ml) at 1, 2, and 4 h. Scale bar, 2 μm.

    Techniques Used: Expressing, Plasmid Preparation, Mutagenesis, Construct

    (A) Tree showing the phylogenetic relationship of ABUW_0098 protein. The tree was generated using iTOL from a Clustal Omega alignment of protein sequence obtained from the National Center for Biotechnology Information database. (B) Predicted transmembrane topology of the ABUW_0098 protein (AciT) based on predictions made using TMHMM . This protein is predicted to have three transmembrane α-helices. (C) Induction of ABUW_0098 ( aciT ) homologs by ciprofloxacin in A. baumannii strains ACICU, AYE, ATCC 17978, ATCC 19606, and D1279779. A subinhibitory concentration of ciprofloxacin was added to the medium when cells were in the exponential growth phase. The bars represent a change in aciT gene expression compared with an untreated control after 1 h of growth in the presence of ciprofloxacin. Error bars show the standard errors from at least 2 biological and 4 technical replicates.
    Figure Legend Snippet: (A) Tree showing the phylogenetic relationship of ABUW_0098 protein. The tree was generated using iTOL from a Clustal Omega alignment of protein sequence obtained from the National Center for Biotechnology Information database. (B) Predicted transmembrane topology of the ABUW_0098 protein (AciT) based on predictions made using TMHMM . This protein is predicted to have three transmembrane α-helices. (C) Induction of ABUW_0098 ( aciT ) homologs by ciprofloxacin in A. baumannii strains ACICU, AYE, ATCC 17978, ATCC 19606, and D1279779. A subinhibitory concentration of ciprofloxacin was added to the medium when cells were in the exponential growth phase. The bars represent a change in aciT gene expression compared with an untreated control after 1 h of growth in the presence of ciprofloxacin. Error bars show the standard errors from at least 2 biological and 4 technical replicates.

    Techniques Used: Generated, Sequencing, Concentration Assay, Expressing

    hbdl  (ATCC)


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    ATCC hbdl
    Hbdl, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    hbdl - by Bioz Stars, 2023-06
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    mic  (ATCC)


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    ATCC mic
    Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and <t>C.</t> <t>albicans</t> (c, f), respectively at 1/2×, 1× and 2× <t>MIC</t> (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments
    Mic, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mic/product/ATCC
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mic - by Bioz Stars, 2023-06
    86/100 stars

    Images

    1) Product Images from "Biological characterization of omw1 and omw2: antimicrobial peptides derived from omwaprin"

    Article Title: Biological characterization of omw1 and omw2: antimicrobial peptides derived from omwaprin

    Journal: 3 Biotech

    doi: 10.1007/s13205-019-1801-x

    Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments
    Figure Legend Snippet: Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments

    Techniques Used:

    Antibiofilm activity of omw1 and omw2. a Biofilm formation. Omw1 and omw2 exerted a significant effect on the formation of biofilm by clinical isolate, Candida albicans. Concentrations represent the log of 1/16×, 1/8×, 1/4× and 1/2× of MIC (50 µg/ml). b Dissolution of matured biofilms. The peptides were also equally potent to dissolute the established biofilm mass of Candida albicans. Values are mean ± SD of three independent experiments
    Figure Legend Snippet: Antibiofilm activity of omw1 and omw2. a Biofilm formation. Omw1 and omw2 exerted a significant effect on the formation of biofilm by clinical isolate, Candida albicans. Concentrations represent the log of 1/16×, 1/8×, 1/4× and 1/2× of MIC (50 µg/ml). b Dissolution of matured biofilms. The peptides were also equally potent to dissolute the established biofilm mass of Candida albicans. Values are mean ± SD of three independent experiments

    Techniques Used: Activity Assay

    MIC and MBC of omwaprin-derived peptides omw1 and omw2 against reference and clinical microbial strains
    Figure Legend Snippet: MIC and MBC of omwaprin-derived peptides omw1 and omw2 against reference and clinical microbial strains

    Techniques Used:

    Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2
    Figure Legend Snippet: Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2

    Techniques Used: Fluorescence, Microscopy, Staining, Activity Assay, Concentration Assay

    Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments
    Figure Legend Snippet: Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments

    Techniques Used:

    Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2
    Figure Legend Snippet: Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2

    Techniques Used: Fluorescence, Microscopy, Staining, Activity Assay, Concentration Assay

    mic  (ATCC)


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    ATCC mic
    Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and <t>C.</t> <t>albicans</t> (c, f), respectively at 1/2×, 1× and 2× <t>MIC</t> (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments
    Mic, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mic/product/ATCC
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mic - by Bioz Stars, 2023-06
    86/100 stars

    Images

    1) Product Images from "Biological characterization of omw1 and omw2: antimicrobial peptides derived from omwaprin"

    Article Title: Biological characterization of omw1 and omw2: antimicrobial peptides derived from omwaprin

    Journal: 3 Biotech

    doi: 10.1007/s13205-019-1801-x

    Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments
    Figure Legend Snippet: Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments

    Techniques Used:

    Antibiofilm activity of omw1 and omw2. a Biofilm formation. Omw1 and omw2 exerted a significant effect on the formation of biofilm by clinical isolate, Candida albicans. Concentrations represent the log of 1/16×, 1/8×, 1/4× and 1/2× of MIC (50 µg/ml). b Dissolution of matured biofilms. The peptides were also equally potent to dissolute the established biofilm mass of Candida albicans. Values are mean ± SD of three independent experiments
    Figure Legend Snippet: Antibiofilm activity of omw1 and omw2. a Biofilm formation. Omw1 and omw2 exerted a significant effect on the formation of biofilm by clinical isolate, Candida albicans. Concentrations represent the log of 1/16×, 1/8×, 1/4× and 1/2× of MIC (50 µg/ml). b Dissolution of matured biofilms. The peptides were also equally potent to dissolute the established biofilm mass of Candida albicans. Values are mean ± SD of three independent experiments

    Techniques Used: Activity Assay

    MIC and MBC of omwaprin-derived peptides omw1 and omw2 against reference and clinical microbial strains
    Figure Legend Snippet: MIC and MBC of omwaprin-derived peptides omw1 and omw2 against reference and clinical microbial strains

    Techniques Used:

    Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2
    Figure Legend Snippet: Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2

    Techniques Used: Fluorescence, Microscopy, Staining, Activity Assay, Concentration Assay

    Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments
    Figure Legend Snippet: Time-kill kinetics of omw1 and omw2. Time-kill kinetics of omw1 and omw2 against E. coli ATCC 25922 (a, d), S. aureus ATCC 25923 (b, e) and C. albicans (c, f), respectively at 1/2×, 1× and 2× MIC (15.625, 125 and 250 µg/ml for E. coli ATCC 25922, S. aureus ATCC 25923, respectively) and 1×, 2× and 4× MIC for C. albicans. Control is the individual bacterial culture without any peptide. Data represented are the mean ± SD of three independent experiments

    Techniques Used:

    Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2
    Figure Legend Snippet: Phase contrast and fluorescence microscopy images treated with Omw1 and Omw2 against a E. coli ATCC 25922, b S. aureus ATCC 25923 and c C. albicans. Propidium iodide (PI) stain is used for this experiment. PI stains the cells with damaged membrane while leaving the intact cells unstained or lightly stained. Red signal indicating membrane-lytic activity was observed in the cells treated with 2× MIC concentration of peptides for bacteria and 4× MIC for Candida cells. Columns 1 and 2 depict phase contrast and fluorescence images of the control and treated microbial cells. Column 3 is the merged image of 1 and 2

    Techniques Used: Fluorescence, Microscopy, Staining, Activity Assay, Concentration Assay

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