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surface plasmon resonance (spr) experiments  (Verlag GmbH)

 
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    Verlag GmbH surface plasmon resonance (spr) experiments
    Surface Plasmon Resonance (Spr) Experiments, supplied by Verlag GmbH, 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/spr+experiments/surface+plasmon+resonance++spr++experiments/pm23868291-65-22-2
    Average 90 stars, based on 1 article reviews
    surface plasmon resonance (spr) experiments - by Bioz Stars, 2026-10
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    Related Articles

    SPR Assay:

    Article Title: N-Lauroylation during the Expression of Recombinant N-Myristoylated Proteins: Implications and Solutions
    Article Snippet: Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim84 formed surface plasmon resonance (SPR) experiments with immobilized liposomes.

    Article Title: Strand invasion of DNA quadruplexes by PNA: comparison of homologous and complementary hybridization.
    Article Snippet: 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim ChemBioChem 2013, 14, 1476 – 1484 1477 SPR analysis of PNA hybridization to the Myc19 quadruplex Surface plasmon resonance (SPR) experiments were previously helpful in studying heteroquadruplex formation at high ionic strength, at which UV melting temperatures are too high to determine; they allow the study of these nanomolar binding interactions from both kinetic and equilibrium perspectives.

    Liposomes:

    Article Title: N-Lauroylation during the Expression of Recombinant N-Myristoylated Proteins: Implications and Solutions
    Article Snippet: Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim84 formed surface plasmon resonance (SPR) experiments with immobilized liposomes.

    Article Title: Strand invasion of DNA quadruplexes by PNA: comparison of homologous and complementary hybridization.
    Article Snippet: 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim ChemBioChem 2013, 14, 1476 – 1484 1477 SPR analysis of PNA hybridization to the Myc19 quadruplex Surface plasmon resonance (SPR) experiments were previously helpful in studying heteroquadruplex formation at high ionic strength, at which UV melting temperatures are too high to determine; they allow the study of these nanomolar binding interactions from both kinetic and equilibrium perspectives.

    Hybridization:

    Article Title: N-Lauroylation during the Expression of Recombinant N-Myristoylated Proteins: Implications and Solutions
    Article Snippet: Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim84 formed surface plasmon resonance (SPR) experiments with immobilized liposomes.

    Article Title: Strand invasion of DNA quadruplexes by PNA: comparison of homologous and complementary hybridization.
    Article Snippet: 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim ChemBioChem 2013, 14, 1476 – 1484 1477 SPR analysis of PNA hybridization to the Myc19 quadruplex Surface plasmon resonance (SPR) experiments were previously helpful in studying heteroquadruplex formation at high ionic strength, at which UV melting temperatures are too high to determine; they allow the study of these nanomolar binding interactions from both kinetic and equilibrium perspectives.

    Binding Assay:

    Article Title: N-Lauroylation during the Expression of Recombinant N-Myristoylated Proteins: Implications and Solutions
    Article Snippet: Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim84 formed surface plasmon resonance (SPR) experiments with immobilized liposomes.

    Article Title: Strand invasion of DNA quadruplexes by PNA: comparison of homologous and complementary hybridization.
    Article Snippet: 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim ChemBioChem 2013, 14, 1476 – 1484 1477 SPR analysis of PNA hybridization to the Myc19 quadruplex Surface plasmon resonance (SPR) experiments were previously helpful in studying heteroquadruplex formation at high ionic strength, at which UV melting temperatures are too high to determine; they allow the study of these nanomolar binding interactions from both kinetic and equilibrium perspectives.



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    CAM12203 directly binds <t>to</t> <t>DGK</t> ζ . (A) Structure of the biotinylated probe. (B) RAW264.7 cells (pretreated with or without the probe for 2 h) were stimulated with LPS for 4 h. The mRNA level of Il1b was detected by Q-PCR. (C) BMDMs (pretreated with or without the probe for 2 h) were stimulated with LPS (4 h) + ATP (another 45 min). The IL-1 β concentration in culture medium (CM) was examined by HTRF. (D) Overall scheme of the experiments to identify the targets of CAM12203 (created with Biorender.com ). (E) The list of gene names of CAM12203 -binding proteins. (F) RAW264.7 lysate was pretreated with or without CAM12203 for 2 h (4 °C), followed by incubation with the probe for another 2 h (4 °C). The level of DGK ζ pulled down was determined by Western blotting. (G) RAW264.7 lysate was treated with or without CAM12203 , and the protein stability of DGK ζ resistant to pronase E was determined by DARTS. (H) RAW264.7 lysate was treated with or without CAM12203 , and the thermostability of DGK ζ was determined by CETSA. (I) DGK ζ protein was treated with CAM12203 , and the binding affinity was determined by <t>SPR.</t> Data are displayed as mean ± SEM ( n = 3). ∗ P < 0.05, ∗∗ P < 0.01 vs . the indicated group.
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    CAM12203 directly binds to DGK ζ . (A) Structure of the biotinylated probe. (B) RAW264.7 cells (pretreated with or without the probe for 2 h) were stimulated with LPS for 4 h. The mRNA level of Il1b was detected by Q-PCR. (C) BMDMs (pretreated with or without the probe for 2 h) were stimulated with LPS (4 h) + ATP (another 45 min). The IL-1 β concentration in culture medium (CM) was examined by HTRF. (D) Overall scheme of the experiments to identify the targets of CAM12203 (created with Biorender.com ). (E) The list of gene names of CAM12203 -binding proteins. (F) RAW264.7 lysate was pretreated with or without CAM12203 for 2 h (4 °C), followed by incubation with the probe for another 2 h (4 °C). The level of DGK ζ pulled down was determined by Western blotting. (G) RAW264.7 lysate was treated with or without CAM12203 , and the protein stability of DGK ζ resistant to pronase E was determined by DARTS. (H) RAW264.7 lysate was treated with or without CAM12203 , and the thermostability of DGK ζ was determined by CETSA. (I) DGK ζ protein was treated with CAM12203 , and the binding affinity was determined by SPR. Data are displayed as mean ± SEM ( n = 3). ∗ P < 0.05, ∗∗ P < 0.01 vs . the indicated group.

    Journal: Acta Pharmaceutica Sinica. B

    Article Title: Macrophage DGK ζ -mediated phosphatidic acid remodeling aggravates acute liver failure

    doi: 10.1016/j.apsb.2025.06.019

    Figure Lengend Snippet: CAM12203 directly binds to DGK ζ . (A) Structure of the biotinylated probe. (B) RAW264.7 cells (pretreated with or without the probe for 2 h) were stimulated with LPS for 4 h. The mRNA level of Il1b was detected by Q-PCR. (C) BMDMs (pretreated with or without the probe for 2 h) were stimulated with LPS (4 h) + ATP (another 45 min). The IL-1 β concentration in culture medium (CM) was examined by HTRF. (D) Overall scheme of the experiments to identify the targets of CAM12203 (created with Biorender.com ). (E) The list of gene names of CAM12203 -binding proteins. (F) RAW264.7 lysate was pretreated with or without CAM12203 for 2 h (4 °C), followed by incubation with the probe for another 2 h (4 °C). The level of DGK ζ pulled down was determined by Western blotting. (G) RAW264.7 lysate was treated with or without CAM12203 , and the protein stability of DGK ζ resistant to pronase E was determined by DARTS. (H) RAW264.7 lysate was treated with or without CAM12203 , and the thermostability of DGK ζ was determined by CETSA. (I) DGK ζ protein was treated with CAM12203 , and the binding affinity was determined by SPR. Data are displayed as mean ± SEM ( n = 3). ∗ P < 0.05, ∗∗ P < 0.01 vs . the indicated group.

    Article Snippet: For the SPR experiment, 6 × His-tagged, recombinant full-length human DGK ζ (expressed in HEK293T cells, purified by Ni-NTA His-Tag purification agarose (HY–K0210, MedChemExpress)) was prepared.

    Techniques: Concentration Assay, Binding Assay, Incubation, Western Blot