macconkey agar base Search Results


remel macconkey agar base  (Thermo Fisher)
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Remel MacConkey Agar Base is used for the cultivation of gram-negative bacilli.
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macconkey agar base  (Becton Dickinson)
90
Becton Dickinson macconkey agar base
KfrA dimerization in vivo and in vitro . (A) Graphic presentation of the analyzed kfrA deletion mutants. The N-terminal fragment of 53 amino acids is labeled green, with the HTH motif indicated by light green, the middle alpha-helical fragment is purple, and the repetitive motifs in the C terminus are in various shades of gray. Numbers indicate amino acid residues. (B and C) Analysis of KfrA dimerization ability in the BACTH system. Double transformants of E. coli BTH101 cyaA with compatible plasmids encoding CyaA fragment T18 or T25 fused to either intact KfrA (B) or various KfrA deletion variants (C) were analyzed on indicator <t>MacConkey</t> plates (pictured here) with maltose as a carbon source and by β-galactosidase assays in liquid cultures. Dark (purple) streaks are indicative of interactions between the two hybrid proteins. Numbers below the images represent β-galactosidase units with SD from at least three experiments. Two shades of gray symbolize strong and weak interactions. Absence of shading indicates no interactions. Double transformants with empty BACTH vectors were used as controls. (D) Cross-linking of purified KfrA variants. His 6 -tagged KfrA and its truncated derivatives (0.1 mg ml −1 ) were incubated with increasing concentrations of glutaraldehyde (0 to 0.05%). The products were separated by SDS-PAGE on polyacrylamide gels of appropriate concentration (18%, 15%, or 12%) and stained with Coomassie brilliant blue. Arrows indicate monomers and putative dimers; brackets encompass higher order complexes. M, protein markers (Spectra multicolor protein ladders [Thermo Fisher Scientific]; low range for KfrA 1–53 and broad range for the other KfrA variants).
Macconkey Agar Base, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/macconkey+agar+base/macconkey+agar+base/pmc07783346-431-0-3
Average 90 stars, based on 1 article reviews
macconkey agar base - by Bioz Stars, 2026-10
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macconkey base agar medium  (ICN Biomedicals)
90
ICN Biomedicals macconkey base agar medium
KfrA dimerization in vivo and in vitro . (A) Graphic presentation of the analyzed kfrA deletion mutants. The N-terminal fragment of 53 amino acids is labeled green, with the HTH motif indicated by light green, the middle alpha-helical fragment is purple, and the repetitive motifs in the C terminus are in various shades of gray. Numbers indicate amino acid residues. (B and C) Analysis of KfrA dimerization ability in the BACTH system. Double transformants of E. coli BTH101 cyaA with compatible plasmids encoding CyaA fragment T18 or T25 fused to either intact KfrA (B) or various KfrA deletion variants (C) were analyzed on indicator <t>MacConkey</t> plates (pictured here) with maltose as a carbon source and by β-galactosidase assays in liquid cultures. Dark (purple) streaks are indicative of interactions between the two hybrid proteins. Numbers below the images represent β-galactosidase units with SD from at least three experiments. Two shades of gray symbolize strong and weak interactions. Absence of shading indicates no interactions. Double transformants with empty BACTH vectors were used as controls. (D) Cross-linking of purified KfrA variants. His 6 -tagged KfrA and its truncated derivatives (0.1 mg ml −1 ) were incubated with increasing concentrations of glutaraldehyde (0 to 0.05%). The products were separated by SDS-PAGE on polyacrylamide gels of appropriate concentration (18%, 15%, or 12%) and stained with Coomassie brilliant blue. Arrows indicate monomers and putative dimers; brackets encompass higher order complexes. M, protein markers (Spectra multicolor protein ladders [Thermo Fisher Scientific]; low range for KfrA 1–53 and broad range for the other KfrA variants).
Macconkey Base Agar Medium, supplied by ICN Biomedicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/macconkey+agar+base/macconkey+base+agar+medium/pm15383715-240-5-9
Average 90 stars, based on 1 article reviews
macconkey base agar medium - by Bioz Stars, 2026-10
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macconkey agar base  (Eiken Chemical)
90
Eiken Chemical macconkey agar base
KfrA dimerization in vivo and in vitro . (A) Graphic presentation of the analyzed kfrA deletion mutants. The N-terminal fragment of 53 amino acids is labeled green, with the HTH motif indicated by light green, the middle alpha-helical fragment is purple, and the repetitive motifs in the C terminus are in various shades of gray. Numbers indicate amino acid residues. (B and C) Analysis of KfrA dimerization ability in the BACTH system. Double transformants of E. coli BTH101 cyaA with compatible plasmids encoding CyaA fragment T18 or T25 fused to either intact KfrA (B) or various KfrA deletion variants (C) were analyzed on indicator <t>MacConkey</t> plates (pictured here) with maltose as a carbon source and by β-galactosidase assays in liquid cultures. Dark (purple) streaks are indicative of interactions between the two hybrid proteins. Numbers below the images represent β-galactosidase units with SD from at least three experiments. Two shades of gray symbolize strong and weak interactions. Absence of shading indicates no interactions. Double transformants with empty BACTH vectors were used as controls. (D) Cross-linking of purified KfrA variants. His 6 -tagged KfrA and its truncated derivatives (0.1 mg ml −1 ) were incubated with increasing concentrations of glutaraldehyde (0 to 0.05%). The products were separated by SDS-PAGE on polyacrylamide gels of appropriate concentration (18%, 15%, or 12%) and stained with Coomassie brilliant blue. Arrows indicate monomers and putative dimers; brackets encompass higher order complexes. M, protein markers (Spectra multicolor protein ladders [Thermo Fisher Scientific]; low range for KfrA 1–53 and broad range for the other KfrA variants).
Macconkey Agar Base, supplied by Eiken Chemical, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/macconkey+agar+base/macconkey+agar+base/pm12190853-20-24-28
Average 90 stars, based on 1 article reviews
macconkey agar base - by Bioz Stars, 2026-10
90/100 stars
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macconkey agar base powder  (Becton Dickinson)
90
Becton Dickinson macconkey agar base powder
KfrA dimerization in vivo and in vitro . (A) Graphic presentation of the analyzed kfrA deletion mutants. The N-terminal fragment of 53 amino acids is labeled green, with the HTH motif indicated by light green, the middle alpha-helical fragment is purple, and the repetitive motifs in the C terminus are in various shades of gray. Numbers indicate amino acid residues. (B and C) Analysis of KfrA dimerization ability in the BACTH system. Double transformants of E. coli BTH101 cyaA with compatible plasmids encoding CyaA fragment T18 or T25 fused to either intact KfrA (B) or various KfrA deletion variants (C) were analyzed on indicator <t>MacConkey</t> plates (pictured here) with maltose as a carbon source and by β-galactosidase assays in liquid cultures. Dark (purple) streaks are indicative of interactions between the two hybrid proteins. Numbers below the images represent β-galactosidase units with SD from at least three experiments. Two shades of gray symbolize strong and weak interactions. Absence of shading indicates no interactions. Double transformants with empty BACTH vectors were used as controls. (D) Cross-linking of purified KfrA variants. His 6 -tagged KfrA and its truncated derivatives (0.1 mg ml −1 ) were incubated with increasing concentrations of glutaraldehyde (0 to 0.05%). The products were separated by SDS-PAGE on polyacrylamide gels of appropriate concentration (18%, 15%, or 12%) and stained with Coomassie brilliant blue. Arrows indicate monomers and putative dimers; brackets encompass higher order complexes. M, protein markers (Spectra multicolor protein ladders [Thermo Fisher Scientific]; low range for KfrA 1–53 and broad range for the other KfrA variants).
Macconkey Agar Base Powder, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/macconkey+agar+base/macconkey+agar+base+powder/pm32094012-33-15-19
Average 90 stars, based on 1 article reviews
macconkey agar base powder - by Bioz Stars, 2026-10
90/100 stars
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oxoid cefixime rhamnose sorbitol macconkey agar base  (Thermo Fisher)
N/A
Oxoid Cefixime Rhamnose Sorbitol MacConkey Agar Base (CR-SMAC) is a selective and differential medium containing rhamnose and cefixime for the isolation of E. coli O157.
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Image Search Results


KfrA dimerization in vivo and in vitro . (A) Graphic presentation of the analyzed kfrA deletion mutants. The N-terminal fragment of 53 amino acids is labeled green, with the HTH motif indicated by light green, the middle alpha-helical fragment is purple, and the repetitive motifs in the C terminus are in various shades of gray. Numbers indicate amino acid residues. (B and C) Analysis of KfrA dimerization ability in the BACTH system. Double transformants of E. coli BTH101 cyaA with compatible plasmids encoding CyaA fragment T18 or T25 fused to either intact KfrA (B) or various KfrA deletion variants (C) were analyzed on indicator MacConkey plates (pictured here) with maltose as a carbon source and by β-galactosidase assays in liquid cultures. Dark (purple) streaks are indicative of interactions between the two hybrid proteins. Numbers below the images represent β-galactosidase units with SD from at least three experiments. Two shades of gray symbolize strong and weak interactions. Absence of shading indicates no interactions. Double transformants with empty BACTH vectors were used as controls. (D) Cross-linking of purified KfrA variants. His 6 -tagged KfrA and its truncated derivatives (0.1 mg ml −1 ) were incubated with increasing concentrations of glutaraldehyde (0 to 0.05%). The products were separated by SDS-PAGE on polyacrylamide gels of appropriate concentration (18%, 15%, or 12%) and stained with Coomassie brilliant blue. Arrows indicate monomers and putative dimers; brackets encompass higher order complexes. M, protein markers (Spectra multicolor protein ladders [Thermo Fisher Scientific]; low range for KfrA 1–53 and broad range for the other KfrA variants).

Journal: Applied and Environmental Microbiology

Article Title: Unique Properties of the Alpha-Helical DNA-Binding Protein KfrA Encoded by the IncU Incompatibility Group Plasmid RA3 and Its Host-Dependent Role in Plasmid Maintenance

doi: 10.1128/AEM.01771-20

Figure Lengend Snippet: KfrA dimerization in vivo and in vitro . (A) Graphic presentation of the analyzed kfrA deletion mutants. The N-terminal fragment of 53 amino acids is labeled green, with the HTH motif indicated by light green, the middle alpha-helical fragment is purple, and the repetitive motifs in the C terminus are in various shades of gray. Numbers indicate amino acid residues. (B and C) Analysis of KfrA dimerization ability in the BACTH system. Double transformants of E. coli BTH101 cyaA with compatible plasmids encoding CyaA fragment T18 or T25 fused to either intact KfrA (B) or various KfrA deletion variants (C) were analyzed on indicator MacConkey plates (pictured here) with maltose as a carbon source and by β-galactosidase assays in liquid cultures. Dark (purple) streaks are indicative of interactions between the two hybrid proteins. Numbers below the images represent β-galactosidase units with SD from at least three experiments. Two shades of gray symbolize strong and weak interactions. Absence of shading indicates no interactions. Double transformants with empty BACTH vectors were used as controls. (D) Cross-linking of purified KfrA variants. His 6 -tagged KfrA and its truncated derivatives (0.1 mg ml −1 ) were incubated with increasing concentrations of glutaraldehyde (0 to 0.05%). The products were separated by SDS-PAGE on polyacrylamide gels of appropriate concentration (18%, 15%, or 12%) and stained with Coomassie brilliant blue. Arrows indicate monomers and putative dimers; brackets encompass higher order complexes. M, protein markers (Spectra multicolor protein ladders [Thermo Fisher Scientific]; low range for KfrA 1–53 and broad range for the other KfrA variants).

Article Snippet: MacConkey agar base (BD Difco) supplemented with 1% maltose was used in the bacterial adenylate cyclase-based two-hybrid system (BACTH).

Techniques: In Vivo, In Vitro, Labeling, Purification, Incubation, SDS Page, Concentration Assay, Staining