Review





Similar Products

spr sensorgrams  (Biacore)
86
Biacore spr sensorgrams
<t>SPR</t> analysis of Kre binding to full-length and truncated epeX RNA transcripts. a) Schematic overview of truncated epeX RNA fragments. I ) The full-length RNA construct ( epeX 1–11) spans from the +1 transcriptional start site of epeX to the start codon of epeE (232 nt). II ) To identify specific binding regions, three mid-sized fragments (∼80 nt each) were generated: epeX 1–3, epeX 5–7, and epeX 9–11. III ) For higher-resolution mapping, a tiling strategy was applied using eleven 40 bp fragments ( epeX 1 through epe X 11), each overlapping its neighbouring fragment by 20 bp. b-e) <t>Sensorgrams</t> (left panels) depict response units of Kre to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA b) epeX 1-11, as well as truncated versions of the epeX RNA c) epeX 1-3, d) epeX 5-7, and e) epeX 9-11, were applied for SPR as well as IM analysis.
Spr Sensorgrams, supplied by Biacore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/spr sensorgrams/product/Biacore
Average 86 stars, based on 1 article reviews
spr sensorgrams - by Bioz Stars, 2026-05
86/100 stars
  Buy from Supplier
experimental spr sensorgrams overlay plot  (Biacore)
86
Biacore experimental spr sensorgrams overlay plot
<t>SPR</t> analysis of Kre binding to full-length and truncated epeX RNA transcripts. a) Schematic overview of truncated epeX RNA fragments. I ) The full-length RNA construct ( epeX 1–11) spans from the +1 transcriptional start site of epeX to the start codon of epeE (232 nt). II ) To identify specific binding regions, three mid-sized fragments (∼80 nt each) were generated: epeX 1–3, epeX 5–7, and epeX 9–11. III ) For higher-resolution mapping, a tiling strategy was applied using eleven 40 bp fragments ( epeX 1 through epe X 11), each overlapping its neighbouring fragment by 20 bp. b-e) <t>Sensorgrams</t> (left panels) depict response units of Kre to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA b) epeX 1-11, as well as truncated versions of the epeX RNA c) epeX 1-3, d) epeX 5-7, and e) epeX 9-11, were applied for SPR as well as IM analysis.
Experimental Spr Sensorgrams Overlay Plot, supplied by Biacore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/experimental spr sensorgrams overlay plot/product/Biacore
Average 86 stars, based on 1 article reviews
experimental spr sensorgrams overlay plot - by Bioz Stars, 2026-05
86/100 stars
  Buy from Supplier
spr sensorgrams overlay plot  (Biacore)
86
Biacore spr sensorgrams overlay plot
<t>SPR</t> analysis of Kre binding to full-length and truncated epeX RNA transcripts. a) Schematic overview of truncated epeX RNA fragments. I ) The full-length RNA construct ( epeX 1–11) spans from the +1 transcriptional start site of epeX to the start codon of epeE (232 nt). II ) To identify specific binding regions, three mid-sized fragments (∼80 nt each) were generated: epeX 1–3, epeX 5–7, and epeX 9–11. III ) For higher-resolution mapping, a tiling strategy was applied using eleven 40 bp fragments ( epeX 1 through epe X 11), each overlapping its neighbouring fragment by 20 bp. b-e) <t>Sensorgrams</t> (left panels) depict response units of Kre to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA b) epeX 1-11, as well as truncated versions of the epeX RNA c) epeX 1-3, d) epeX 5-7, and e) epeX 9-11, were applied for SPR as well as IM analysis.
Spr Sensorgrams Overlay Plot, supplied by Biacore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/spr sensorgrams overlay plot/product/Biacore
Average 86 stars, based on 1 article reviews
spr sensorgrams overlay plot - by Bioz Stars, 2026-05
86/100 stars
  Buy from Supplier
surface plasmon resonance spr sensorgrams  (Biacore)
86
Biacore surface plasmon resonance spr sensorgrams
Biolayer interferometry screening data for point mutations. (A) Representative biolayer interferometry <t>sensorgrams</t> show the binding of veligrotug and teprotumumab to wild-type human IGF-1R protein, as well as I285A or L286A point mutations. I285A and L286A had minimal effects on binding of veligrotug to IGF-1R. (B) In contrast, I285A reduced binding of teprotumumab to IGF-1R, while L286A completely abrogated binding of teprotumumab to IGF-1R. These results demonstrate that veligrotug and teprotumumab have distinct epitopes.
Surface Plasmon Resonance Spr Sensorgrams, supplied by Biacore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/surface plasmon resonance spr sensorgrams/product/Biacore
Average 86 stars, based on 1 article reviews
surface plasmon resonance spr sensorgrams - by Bioz Stars, 2026-05
86/100 stars
  Buy from Supplier

Image Search Results


SPR analysis of Kre binding to full-length and truncated epeX RNA transcripts. a) Schematic overview of truncated epeX RNA fragments. I ) The full-length RNA construct ( epeX 1–11) spans from the +1 transcriptional start site of epeX to the start codon of epeE (232 nt). II ) To identify specific binding regions, three mid-sized fragments (∼80 nt each) were generated: epeX 1–3, epeX 5–7, and epeX 9–11. III ) For higher-resolution mapping, a tiling strategy was applied using eleven 40 bp fragments ( epeX 1 through epe X 11), each overlapping its neighbouring fragment by 20 bp. b-e) Sensorgrams (left panels) depict response units of Kre to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA b) epeX 1-11, as well as truncated versions of the epeX RNA c) epeX 1-3, d) epeX 5-7, and e) epeX 9-11, were applied for SPR as well as IM analysis.

Journal: bioRxiv

Article Title: SpoVG and the Kre-ComK Regulatory Module Orchestrate Production of the EPE Toxin in Bacillus subtilis

doi: 10.64898/2026.04.02.716078

Figure Lengend Snippet: SPR analysis of Kre binding to full-length and truncated epeX RNA transcripts. a) Schematic overview of truncated epeX RNA fragments. I ) The full-length RNA construct ( epeX 1–11) spans from the +1 transcriptional start site of epeX to the start codon of epeE (232 nt). II ) To identify specific binding regions, three mid-sized fragments (∼80 nt each) were generated: epeX 1–3, epeX 5–7, and epeX 9–11. III ) For higher-resolution mapping, a tiling strategy was applied using eleven 40 bp fragments ( epeX 1 through epe X 11), each overlapping its neighbouring fragment by 20 bp. b-e) Sensorgrams (left panels) depict response units of Kre to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA b) epeX 1-11, as well as truncated versions of the epeX RNA c) epeX 1-3, d) epeX 5-7, and e) epeX 9-11, were applied for SPR as well as IM analysis.

Article Snippet: For this purpose, the SPR sensorgrams were exported from the Biacore T200 Evaluation Software 3.2.1 as *.txt files and imported into TraceDrawer Software 1.10.1 (Ridgeview Instruments, Uppsala, Sweden).

Techniques: Binding Assay, Construct, Generated

SPR analysis of SpoVG binding to full-length and truncated epeX RNA transcripts. Sensorgrams (left panels) depict response units of SpoVG to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA a) epeX 1-11, as well as truncated versions of the epeX RNA b) epeX 1-3, c) epeX 5-7, and d) epeX 9-11, were applied for SPR analysis.

Journal: bioRxiv

Article Title: SpoVG and the Kre-ComK Regulatory Module Orchestrate Production of the EPE Toxin in Bacillus subtilis

doi: 10.64898/2026.04.02.716078

Figure Lengend Snippet: SPR analysis of SpoVG binding to full-length and truncated epeX RNA transcripts. Sensorgrams (left panels) depict response units of SpoVG to increasing concentrations of epeX RNA fragments (black: 10 nM; red: 25 nM; light green: 50 nM; yellow: 100 nM; blue: 250 nM; turquoise: 500 nM; light blue: 1000 nM; grey: 2500 nM; brown: 5000 nM). Interaction Maps (central panels) show the distribution of association and dissociation rate constants as stability (dissociation rate; log k d ) and recognition (association rate, log k a ). The corresponding calculated sensorgrams from the IM peaks (right panels) are presented on the right, the colours of the curved correspond to the respective peaks from the IM analyses. The data were quantified and the respective overall affinities (K D ) calculated from the respective association ( k a ) and dissociation rates ( k d ) are shown, as well as the peak weights (PW) showing the overall contribution of the respective interaction towards the total sensorgrams given in (%). (see for details). Since bulk binding are not included in the calculations, 100% were not reached in total. The full-length epeX RNA a) epeX 1-11, as well as truncated versions of the epeX RNA b) epeX 1-3, c) epeX 5-7, and d) epeX 9-11, were applied for SPR analysis.

Article Snippet: For this purpose, the SPR sensorgrams were exported from the Biacore T200 Evaluation Software 3.2.1 as *.txt files and imported into TraceDrawer Software 1.10.1 (Ridgeview Instruments, Uppsala, Sweden).

Techniques: Binding Assay

Biolayer interferometry screening data for point mutations. (A) Representative biolayer interferometry sensorgrams show the binding of veligrotug and teprotumumab to wild-type human IGF-1R protein, as well as I285A or L286A point mutations. I285A and L286A had minimal effects on binding of veligrotug to IGF-1R. (B) In contrast, I285A reduced binding of teprotumumab to IGF-1R, while L286A completely abrogated binding of teprotumumab to IGF-1R. These results demonstrate that veligrotug and teprotumumab have distinct epitopes.

Journal: mAbs

Article Title: Preclinical pharmacology, pharmacokinetics, and pharmacodynamics of veligrotug, a full antagonist antibody to the IGF-1 receptor in development for thyroid eye disease

doi: 10.1080/19420862.2025.2585616

Figure Lengend Snippet: Biolayer interferometry screening data for point mutations. (A) Representative biolayer interferometry sensorgrams show the binding of veligrotug and teprotumumab to wild-type human IGF-1R protein, as well as I285A or L286A point mutations. I285A and L286A had minimal effects on binding of veligrotug to IGF-1R. (B) In contrast, I285A reduced binding of teprotumumab to IGF-1R, while L286A completely abrogated binding of teprotumumab to IGF-1R. These results demonstrate that veligrotug and teprotumumab have distinct epitopes.

Article Snippet: The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface.

Techniques: Binding Assay

SPR single-cycle kinetics of veligrotug and human IGF-1R interaction. The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface. The black curves overlaid on the experimental data were obtained by fitting the sensorgram with the 1:1 interaction model. The results demonstrated that veligrotug binds with high affinity to human IGF-1R, with a mean K D value of 0.55 nM, averaged from three independent experiments (range from 0.38–0.69 nM).

Journal: mAbs

Article Title: Preclinical pharmacology, pharmacokinetics, and pharmacodynamics of veligrotug, a full antagonist antibody to the IGF-1 receptor in development for thyroid eye disease

doi: 10.1080/19420862.2025.2585616

Figure Lengend Snippet: SPR single-cycle kinetics of veligrotug and human IGF-1R interaction. The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface. The black curves overlaid on the experimental data were obtained by fitting the sensorgram with the 1:1 interaction model. The results demonstrated that veligrotug binds with high affinity to human IGF-1R, with a mean K D value of 0.55 nM, averaged from three independent experiments (range from 0.38–0.69 nM).

Article Snippet: The surface plasmon resonance (SPR) sensorgrams from three independent experiments (blue lines) of the response (resonance units) versus time (seconds) of the single cycle kinetics were performed by injecting five increasing concentrations (6.3, 12.5, 25, 50, and 100 nM) of human His-tagged IGF-1R extracellular domain protein over the veligrotug captured on the Biacore chip surface.

Techniques: SPR Assay