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86
GE Healthcare unmodified gold sensor chips
Unmodified Gold Sensor Chips, supplied by GE Healthcare, 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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90
Biacore cm5 research grade sensor chips
Cm5 Research Grade Sensor Chips, supplied by Biacore, 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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90
Biolin Scientific silica-coated sensor chips qsx 303
Silica Coated Sensor Chips Qsx 303, supplied by Biolin 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
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90
Biacore gold sensor chips
Gold Sensor Chips, supplied by Biacore, 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
Biosensing Instrument Inc gold sensor chips
Gold Sensor Chips, supplied by Biosensing Instrument 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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Average 90 stars, based on 1 article reviews
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90
Biacore biacore sensor chips
Biacore Sensor Chips, supplied by Biacore, 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
XanTec bioanalytics 1000m polycarboxylate hydrogel sensor chips
Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a <t>1000M</t> polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.
1000m Polycarboxylate Hydrogel Sensor Chips, supplied by XanTec bioanalytics, 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/1000m polycarboxylate hydrogel sensor chips/product/XanTec bioanalytics
Average 90 stars, based on 1 article reviews
1000m polycarboxylate hydrogel sensor chips - by Bioz Stars, 2026-03
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92
GE Healthcare cm5 sensor chips
Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a <t>1000M</t> polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.
Cm5 Sensor Chips, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 1 article reviews
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93
GE Healthcare cm5 chips
Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a <t>1000M</t> polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.
Cm5 Chips, supplied by GE Healthcare, 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
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90
SouthernBiotech cm5 sensor chips
Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a <t>1000M</t> polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.
Cm5 Sensor Chips, supplied by SouthernBiotech, 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
cm5 sensor chips - by Bioz Stars, 2026-03
90/100 stars
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86
Danaher Inc cm5 sensor chips
Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a <t>1000M</t> polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.
Cm5 Sensor Chips, supplied by Danaher Inc, 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
cm5 sensor chips - by Bioz Stars, 2026-03
86/100 stars
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90
Biacore sensor chips
Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a <t>1000M</t> polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.
Sensor Chips, supplied by Biacore, 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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sensor chips - by Bioz Stars, 2026-03
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Image Search Results


Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a 1000M polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.

Journal: The Journal of Biological Chemistry

Article Title: Affinity Map of Bromodomain Protein 4 (BRD4) Interactions with the Histone H4 Tail and the Small Molecule Inhibitor JQ1 *

doi: 10.1074/jbc.M113.523019

Figure Lengend Snippet: Binding of BRD4 BD1 and BD2 to acetylated peptides. A , TR-FRET quantification of BRD4 BD1 and BD2 (100 n m ) binding to acetylated peptides derived from H3, H4 or RelA (200 n m each). B , determination of BRD4 BD1 and BD2 affinities to H4 K5(ac)K8(ac)K12(ac)K16(ac) using a TR-FRET homogeneous competition assay. 200 n m biotinylated H4 peptide and 50 n m BRD4 BD1 or 500 n m BRD4 BD2 were titrated with unlabeled H4 peptide at the concentrations indicated. Delta F values were plotted against the concentrations of unlabeled peptide (competitor). The fitting of data to the four-parameter equation described under “Experimental Procedures” (line) served to calculate the K D values indicated in . C , SPR sensorgrams of the interaction between BRD4 BD1 (immobilized on a 1000 m polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). D , SPR sensorgrams of the interaction between BRD4 BD2 (immobilized on a 1000M polycarboxylate chip) and histone H4 K5(ac)K8(ac)K12(ac)K16(ac). The insets in C and D show SPR equilibrium resonance values Req versus [BRD4 BD1] and Req versus [BRD4 BD2] plots from which the K D values indicated in the text were calculated. Red lines represent the fit of the data to the Langmuir 1:1 and single-site equilibrium binding equations. All data are the mean values of at least two experiments with multiple replicates each.

Article Snippet: For peptide binding assays, BRD4 BD1 and BD2 (50 μg/ml in 25 m m HEPES, pH 7) were immobilized on 1000M polycarboxylate hydrogel sensor chips (Xantec) at densities varying between 2000 and 3000 RU using standard amine coupling methods based on ethyl(dimethylaminopropyl)carbodiimide/ N -hydroxysuccinimide chemistry at densities varying between 2000 and 3000 RU.

Techniques: Binding Assay, Derivative Assay, Competitive Binding Assay