1× cathode buffer Search Results


tris tricine cathode buffer  (Boston BioProducts)
91
Boston BioProducts tris tricine cathode 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.
Tris Tricine Cathode Buffer, supplied by Boston BioProducts, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 91 stars, based on 1 article reviews
tris tricine cathode buffer - by Bioz Stars, 2026-03
91/100 stars
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labelling with neurobiotin  (Vector Laboratories)
95
Vector Laboratories labelling with neurobiotin
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.
Labelling With Neurobiotin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
labelling with neurobiotin - by Bioz Stars, 2026-03
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tricine sds cathode buffer system  (Bio-Rad)
98
Bio-Rad tricine sds cathode buffer system
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.
Tricine Sds Cathode Buffer System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 98 stars, based on 1 article reviews
tricine sds cathode buffer system - by Bioz Stars, 2026-03
98/100 stars
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cathode buffer additive invitrogen  (Thermo Fisher)
86
Thermo Fisher cathode buffer additive invitrogen
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.
Cathode Buffer Additive Invitrogen, 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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Average 86 stars, based on 1 article reviews
cathode buffer additive invitrogen - by Bioz Stars, 2026-03
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tris–glycine electrode buffer (ph 8.3)  (Hoefer)
90
Hoefer tris–glycine electrode buffer (ph 8.3)
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.
Tris–Glycine Electrode Buffer (Ph 8.3), supplied by Hoefer, 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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Average 90 stars, based on 1 article reviews
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90/100 stars
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tris glycine electrode buffer  (Valiant Co Ltd)
93
Valiant Co Ltd tris glycine electrode 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.
Tris Glycine Electrode Buffer, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
tris glycine electrode buffer - by Bioz Stars, 2026-03
93/100 stars
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1× cathode buffer  (Thermo Fisher)
90
Thermo Fisher 1× cathode 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.
1× Cathode Buffer, 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
https://www.bioz.com/result/1× cathode buffer/product/Thermo Fisher
Average 90 stars, based on 1 article reviews
1× cathode buffer - by Bioz Stars, 2026-03
90/100 stars
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25x tris glycine transfer buffer  (Boston BioProducts)
94
Boston BioProducts 25x tris glycine transfer 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.
25x Tris Glycine Transfer Buffer, supplied by Boston BioProducts, 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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Average 94 stars, based on 1 article reviews
25x tris glycine transfer buffer - by Bioz Stars, 2026-03
94/100 stars
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agcl electrodes bathed in 0.1 m kcl solution contained in borosilicate glass capillaries  (Hilgenberg gmbh)
90
Hilgenberg gmbh agcl electrodes bathed in 0.1 m kcl solution contained in borosilicate glass capillaries
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.
Agcl Electrodes Bathed In 0.1 M Kcl Solution Contained In Borosilicate Glass Capillaries, supplied by Hilgenberg gmbh, 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/agcl electrodes bathed in 0.1 m kcl solution contained in borosilicate glass capillaries/product/Hilgenberg gmbh
Average 90 stars, based on 1 article reviews
agcl electrodes bathed in 0.1 m kcl solution contained in borosilicate glass capillaries - by Bioz Stars, 2026-03
90/100 stars
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1x cathode buffer  (Bio-Rad)
96
Bio-Rad 1x cathode 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.
1x Cathode Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 1 article reviews
1x cathode buffer - by Bioz Stars, 2026-03
96/100 stars
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1 nativepage anode running buffer  (Thermo Fisher)
90
Thermo Fisher 1 nativepage anode running 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.
1 Nativepage Anode Running Buffer, 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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Average 90 stars, based on 1 article reviews
1 nativepage anode running buffer - by Bioz Stars, 2026-03
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pbs buffer  (Fisher Scientific)
90
Fisher Scientific pbs 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.
Pbs Buffer, 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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Average 90 stars, based on 1 article reviews
pbs buffer - by Bioz Stars, 2026-03
90/100 stars
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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: Cell lysates were separated on 16.5% Criterion Tris-Tricine gels (Bio-Rad) using Tris-Tricine Cathode buffer (Boston Bioproducts) and LOS was stained using the Bio-Rad Silver Stain kit.

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