congo red agar plates Search Results


heart infusion broth congo red agar plates  (Difco)
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Difco heart infusion broth congo red agar plates
Heart Infusion Broth Congo Red Agar Plates, supplied by Difco, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red agar plates  (Fluka Chemie)
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Fluka Chemie congo red agar plates
Congo Red Agar Plates, supplied by Fluka Chemie, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red agar plates  (Beijing Solarbio Science)
90
Beijing Solarbio Science congo red agar plates
Congo Red Agar Plates, supplied by Beijing Solarbio Science, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red agar plate  (Bacto Laboratories)
90
Bacto Laboratories congo red agar plate
Congo Red Agar Plate, supplied by Bacto Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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lb agar plate containing 0.1‰ congo red  (Applichem inc)
90
Applichem inc lb agar plate containing 0.1‰ congo red
Lb Agar Plate Containing 0.1‰ Congo Red, supplied by Applichem inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red agar plates  (Fisher Scientific)
90
Fisher Scientific congo red agar plates
(a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on <t>Congo</t> <t>red</t> <t>agar</t> <t>plates</t> and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24
Congo Red Agar Plates, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red agar plates - by Bioz Stars, 2026-03
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congo red cr agar plates  (Merck KGaA)
90
Merck KGaA congo red cr agar plates
(a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on <t>Congo</t> <t>red</t> <t>agar</t> <t>plates</t> and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24
Congo Red Cr Agar Plates, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red cr agar plates - by Bioz Stars, 2026-03
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tryptic soy broth agar plates containing 0.5% congo red  (Difco)
90
Difco tryptic soy broth agar plates containing 0.5% congo red
(a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on <t>Congo</t> <t>red</t> <t>agar</t> <t>plates</t> and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24
Tryptic Soy Broth Agar Plates Containing 0.5% Congo Red, supplied by Difco, 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/result/tryptic soy broth agar plates containing 0.5% congo red/product/Difco
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mueller-hinton agar plates congo red  (Difco)
90
Difco mueller-hinton agar plates congo red
(a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on <t>Congo</t> <t>red</t> <t>agar</t> <t>plates</t> and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24
Mueller Hinton Agar Plates Congo Red, supplied by Difco, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mueller-hinton agar plates congo red - by Bioz Stars, 2026-03
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congo red yeast extract mannitol (yem) agar plates  (HiMedia Laboratories)
90
HiMedia Laboratories congo red yeast extract mannitol (yem) agar plates
(a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on <t>Congo</t> <t>red</t> <t>agar</t> <t>plates</t> and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24
Congo Red Yeast Extract Mannitol (Yem) Agar Plates, supplied by HiMedia Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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congo red yeast extract mannitol (yem) agar plates - by Bioz Stars, 2026-03
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Image Search Results


(a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on Congo red agar plates and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24

Journal: Nature structural & molecular biology

Article Title: Molecular Organization of the E. coli Cellulose Synthase Macrocomplex

doi: 10.1038/s41594-021-00569-7

Figure Lengend Snippet: (a) Clumping cells upon expression of the recombinant Bcs genes with AdrA in liquid cultures. Cells without BcsC remain planktonic. (b) Cultures in (a) were grown on Congo red agar plates and photographed on a Fisher Scientific UV lightbox. (c) Overlay of the ssNMR spectrum shown in Fig. 1 with the pEtN standard. (d) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively. Inset: SDS-PAGE of the peak fractions. (e) Catalytic activity determined by UDP-Glc[13H] incorporation as described.24 The synthesized polymer is sensitive to cellulase (BcsZ) degradation. DPM: Disintegrations per minute. Error bars represent standard deviations from the means of three independent replicas. (f) Western blot analysis of the purified Ec IMC. Right panel: Coomassie-stained SDS-PAGE of the purified complex. Percentages indicate peptide covered in MS-sequencing based on the identified unique peptides (also shown). R/NR: Reducing and non-reducing conditions; * denotes a BcsG proteolytic fragment. (g) Identification of Myc-tagged BcsF by Western blotting in the purified complex (left Coomassie-stained SDS-PAGE; right: anti-Myc Western blot). (h, i) Kinetic analysis of the purified detergent-solubilized samples. UDP generation was quantified in real time using an enzyme-coupled assay that monitors the oxidation of NADH, as described.24

Article Snippet: Cells without BcsC remain planktonic. ( b ) Cultures in (a) were grown on Congo red agar plates and photographed on a Fisher Scientific UV lightbox. ( c ) Overlay of the ssNMR spectrum shown in with the pEtN standard. ( d ) Gel filtration purification of Ec Bcs, 256 and 280nm absorbances are shown in red and blue, respectively.

Techniques: Expressing, Recombinant, Filtration, Purification, SDS Page, Activity Assay, Synthesized, Western Blot, Staining, Sequencing