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surface plasmon resonance spr sensorgrams  (Biacore)

 
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    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

    Images

    1) Product Images from "Preclinical pharmacology, pharmacokinetics, and pharmacodynamics of veligrotug, a full antagonist antibody to the IGF-1 receptor in development for thyroid eye disease"

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

    Journal: mAbs

    doi: 10.1080/19420862.2025.2585616

    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.
    Figure Legend 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.

    Techniques Used: 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).
    Figure Legend 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).

    Techniques Used: SPR Assay



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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/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
    surface plasmon resonance sensorgrams  (Biacore)
    90
    Biacore surface plasmon resonance 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 Sensorgrams, 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
    https://www.bioz.com/result/surface plasmon resonance sensorgrams/product/Biacore
    Average 90 stars, based on 1 article reviews
    surface plasmon resonance sensorgrams - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier
    surface plasmon resonance sensorgram  (Biacore)
    90
    Biacore surface plasmon resonance sensorgram
    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 Sensorgram, 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
    https://www.bioz.com/result/surface plasmon resonance sensorgram/product/Biacore
    Average 90 stars, based on 1 article reviews
    surface plasmon resonance sensorgram - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier
    surface plasmon resonance binding sensorgrams  (Biacore)
    90
    Biacore surface plasmon resonance binding 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 Binding Sensorgrams, 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
    https://www.bioz.com/result/surface plasmon resonance binding sensorgrams/product/Biacore
    Average 90 stars, based on 1 article reviews
    surface plasmon resonance binding sensorgrams - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

    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