spr binding sensorgrams Search Results


spr sensorgrams  (Biacore)
86
Biacore spr sensorgrams
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/product/spr+binding+sensorgrams/sensorgrams+spr/10__1042_slash_bsr20160069-81-4-10
Average 86 stars, based on 1 article reviews
spr sensorgrams - by Bioz Stars, 2026-10
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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/product/spr+binding+sensorgrams/plasmon+resonance+surface/pmc12629334-154-1-52
Average 86 stars, based on 1 article reviews
surface plasmon resonance spr sensorgrams - by Bioz Stars, 2026-10
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zetasizer advance  (Malvern Panalytical)
99
Malvern Panalytical zetasizer advance
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.
Zetasizer Advance, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/spr+binding+sensorgrams/Zetasizer+Advance/custom%40zetasizer-advance-01%4035834580
Average 99 stars, based on 1 article reviews
zetasizer advance - by Bioz Stars, 2026-10
99/100 stars
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nanosight pro  (Micromeritics Instrument)
97
Micromeritics Instrument nanosight pro
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.
Nanosight Pro, supplied by Micromeritics Instrument, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/spr+binding+sensorgrams/NanoSight+Pro/custom%40hbg5000-01%4035834580
Average 97 stars, based on 1 article reviews
nanosight pro - by Bioz Stars, 2026-10
97/100 stars
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Image Search Results


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