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surface plasmon resonance (spr) using a biacore method  (Biacore)

 
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    Biacore surface plasmon resonance (spr) using a biacore method
    Surface Plasmon Resonance (Spr) Using A Biacore Method, 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/product/surface+plasmon+resonance+(spr)+using+a+biacore+method/surface+plasmon+resonance/us12359000-77-11-19
    Average 90 stars, based on 1 article reviews
    surface plasmon resonance (spr) using a biacore method - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Binding Assay:

    Article Title: Protective effects of polysialic acid on proteolytic cleavage of FGF2 and proBDNF/BDNF.
    Article Snippet: To confirm that polySia is able to bind intact, but not heat denatured, FGF2, we analyzed the direct binding of polySia moieties on NCAM to the intact and heat-denatured FGF2 (Weltrowski et al. 2012) using a surface plasmon resonance (SPR)-based procedure (Biacore).

    Article Title: Methods and compositions for regulation of cell aging, carcinogenesis and reprogramming
    Article Snippet: Alternatively, the binding of antibodies to Sp100 can be detected directly using, for example, a surface plasmon resonance (SPR) procedure such as, for example, Biacore®, microcalorimetry or nano-cantilivers.

    Article Title: Methods and compositions for the diagnosis and treatment of thyroid cancer
    Article Snippet: Alternatively, the binding of antibodies to Polypeptide Thyroid Cancer Markers can be detected directly using, for example, a surface plasmon resonance (SPR) procedure such as, for example, Biacore®, microcalorimetry or nano-cantilivers.

    Article Title: Anti-TIGIT antibodies
    Article Snippet: In turn, KD can be determined by measurement of the kinetics of complex formation and dissociation using, as a nonlimiting example, the surface plasmon resonance (SPR) method (Biacore™).

    SPR Assay:

    Article Title: Protective effects of polysialic acid on proteolytic cleavage of FGF2 and proBDNF/BDNF.
    Article Snippet: To confirm that polySia is able to bind intact, but not heat denatured, FGF2, we analyzed the direct binding of polySia moieties on NCAM to the intact and heat-denatured FGF2 (Weltrowski et al. 2012) using a surface plasmon resonance (SPR)-based procedure (Biacore).

    Article Title: Methods and compositions for regulation of cell aging, carcinogenesis and reprogramming
    Article Snippet: Alternatively, the binding of antibodies to Sp100 can be detected directly using, for example, a surface plasmon resonance (SPR) procedure such as, for example, Biacore®, microcalorimetry or nano-cantilivers.

    Article Title: Methods and compositions for the diagnosis and treatment of thyroid cancer
    Article Snippet: Alternatively, the binding of antibodies to Polypeptide Thyroid Cancer Markers can be detected directly using, for example, a surface plasmon resonance (SPR) procedure such as, for example, Biacore®, microcalorimetry or nano-cantilivers.

    Article Title: Anti-TIGIT antibodies
    Article Snippet: In turn, KD can be determined by measurement of the kinetics of complex formation and dissociation using, as a nonlimiting example, the surface plasmon resonance (SPR) method (Biacore™).



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    Design and characterization <t>of</t> <t>FGFR-agonist.</t> ( A ) The secondary structures of the FGFR-binder and FGFR-agonist determined using Mfold software are presented, indicating the formation of a stem-loop structure. ( B ) The secondary structure of DNA-based FGFR-agonist is verified using native polyacrylamide gel electrophoresis (PAGE). This panel also includes the determined molecular weights of the single-stranded FGFR-binder, FGFR1-agonist, and a control oligonucleotide (Ctrl oligo). ( C ) <t>SPR</t> sensorgrams showing the real-time binding kinetics of FGFR-agonist aptamer to immobilized FGFR1 extracellular domain at various concentrations. The sensorgrams are color-coded based on the concentrations of the FGFR-binder (1, 2, 4, 8, 16 and 32 nM) and FGFR-agonist (0.16, 0.31, 0.625, 1.25, 2.5, 5 and 10 nM), respectively. ( D ) The relative binding performance of FGFR-binder and FGFR-agonist to the NIH3T3 cells was determined by flow cytometry (refer to Fig. for additional details)
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    Design and characterization of FGFR-agonist. ( A ) The secondary structures of the FGFR-binder and FGFR-agonist determined using Mfold software are presented, indicating the formation of a stem-loop structure. ( B ) The secondary structure of DNA-based FGFR-agonist is verified using native polyacrylamide gel electrophoresis (PAGE). This panel also includes the determined molecular weights of the single-stranded FGFR-binder, FGFR1-agonist, and a control oligonucleotide (Ctrl oligo). ( C ) SPR sensorgrams showing the real-time binding kinetics of FGFR-agonist aptamer to immobilized FGFR1 extracellular domain at various concentrations. The sensorgrams are color-coded based on the concentrations of the FGFR-binder (1, 2, 4, 8, 16 and 32 nM) and FGFR-agonist (0.16, 0.31, 0.625, 1.25, 2.5, 5 and 10 nM), respectively. ( D ) The relative binding performance of FGFR-binder and FGFR-agonist to the NIH3T3 cells was determined by flow cytometry (refer to Fig. for additional details)

    Journal: Biological Research

    Article Title: Development of synthetic modulator enabling long-term propagation and neurogenesis of human embryonic stem cell-derived neural progenitor cells

    doi: 10.1186/s40659-023-00471-0

    Figure Lengend Snippet: Design and characterization of FGFR-agonist. ( A ) The secondary structures of the FGFR-binder and FGFR-agonist determined using Mfold software are presented, indicating the formation of a stem-loop structure. ( B ) The secondary structure of DNA-based FGFR-agonist is verified using native polyacrylamide gel electrophoresis (PAGE). This panel also includes the determined molecular weights of the single-stranded FGFR-binder, FGFR1-agonist, and a control oligonucleotide (Ctrl oligo). ( C ) SPR sensorgrams showing the real-time binding kinetics of FGFR-agonist aptamer to immobilized FGFR1 extracellular domain at various concentrations. The sensorgrams are color-coded based on the concentrations of the FGFR-binder (1, 2, 4, 8, 16 and 32 nM) and FGFR-agonist (0.16, 0.31, 0.625, 1.25, 2.5, 5 and 10 nM), respectively. ( D ) The relative binding performance of FGFR-binder and FGFR-agonist to the NIH3T3 cells was determined by flow cytometry (refer to Fig. for additional details)

    Article Snippet: The sensorgrams are color-coded based on the concentrations of the FGFR-binder (1, 2, 4, 8, 16 and 32 nM) and FGFR-agonist (0.16, 0.31, 0.625, 1.25, 2.5, 5 and 10 nM), respectively. ( D ) The relative binding performance of FGFR-binder and FGFR-agonist to the NIH3T3 cells was determined by flow cytometry (refer to Fig. for additional details) To elucidate the molecular binding properties of the monomeric FGFR-binder and bivalent FGFR1-agonist with the extracellular domain of FGFR1, we employed Surface Plasmon Resonance (SPR) analysis using the Biacore method.

    Techniques: Software, Polyacrylamide Gel Electrophoresis, Control, Binding Assay, Flow Cytometry