gradient bis tris gel for electrophoresis Search Results


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Thermo Fisher novex sds page system
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Boston BioProducts tris tricine
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Thermo Fisher gradient tris boric acid edta buffer tbe polyacrylamide mini electrophoresis gels
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Bio-Rad bis tris polyacrylamide gel electrophoresis gels
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
Bis Tris Polyacrylamide Gel Electrophoresis Gels, supplied by Bio-Rad, 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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Thermo Fisher bis–tris sds–page gel
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Thermo Fisher bca assay kit
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
Bca Assay Kit, supplied by Thermo Fisher, 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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SERVA Electrophoresis 33 tricine-sds loading buffer
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Thermo Fisher acrylamide bis gradient mes page
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
Acrylamide Bis Gradient Mes Page, supplied by Thermo Fisher, 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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GenScript corporation 4%–12% bis-tris sure page gels
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Bio-Rad tristricine gel electrophoresis
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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New England Biolabs ne buffer 1
Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% <t>Tricine</t> gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.
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Image Search Results


Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% Tricine gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Therapeutic CMP-nonulosonates against multidrug-resistant Neisseria gonorrhoeae

doi: 10.4049/jimmunol.1901398

Figure Lengend Snippet: Incorporation of NulO into N. gonorrhoeae LOS. A. mAb 3F11 binding. mAb 3F11 binds to terminal lactosamine of LNnT; extensions beyond LNnT abrogates 3F11 binding (55). N. gonorrhoeae F62 ΔlgtD was grown in media alone or media containing 25 µg/ml of the indicated CMP-NulO. mAb 3F11 binding was detected by flow cytometry and median fluorescence was recorded. Binding is shown as percentage relative to 3F11 binding to unsialylated bacteria (three independent observations). Comparisons across groups, made by one-way ANOVA, showed significant differences were observed (F=43.76; P<0.0001). Pairwise comparisons, made by Tukey’s multiple comparisons test, are indicated. B. Incorporation of NulO as visualized by silver-stained SDS-PAGE gels. Protease K lysates of F62 ΔlgtD grown in media alone or media containing each of the indicated CMP-NulOs (100 µg/ml) were separated on 16% Tricine gels (Bio-Rad) and LOS was visualized by silver staining. Slower mobility relative to bacteria grown in media alone (No CMP-NulO) indicates addition of NulO.

Article Snippet: Gonococcal lysates were treated with protease K (100 µg/ml) and suspended in Tris-tricine sample buffer (Boston Bioproducts).

Techniques: Binding Assay, Flow Cytometry, Fluorescence, Staining, SDS Page, Silver Staining