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spr based biacore t200 instrument  (Biacore)

 
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    Biacore spr based biacore t200 instrument
    Spr Based Biacore T200 Instrument, 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+based+biacore+t200+instrument/based+spr+technology/pm27190591__ml5b00420_si_001-58-2-3
    Average 86 stars, based on 1 article reviews
    spr based biacore t200 instrument - by Bioz Stars, 2026-11
    86/100 stars

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    Related Articles

    SPR Assay:

    Article Title: Supporting Information
    Article Snippet: .. Using the SPR-based Biacore T200 instrument for quantitative binding-affinity experiments, we set the immobilization level of HipA(D309Q) protein at 800 RUs for most tests (i.e. compounds 2 and 4), and at 250 RUs for the compounds with high nonspecific binding or low solubility (i.e. compounds 1 and 3). ..

    Article Title: Supporting Information
    Article Snippet: At last, we purchased 30 compounds from Chemdiv kinase library and 160 compounds from SPECS compounds library for experimental tests. .. The SPR-based Biacore T200 instrument was used to exclude false-negatives. ..

    Affinity Binding Assay:

    Article Title: Supporting Information
    Article Snippet: .. Using the SPR-based Biacore T200 instrument for quantitative binding-affinity experiments, we set the immobilization level of HipA(D309Q) protein at 800 RUs for most tests (i.e. compounds 2 and 4), and at 250 RUs for the compounds with high nonspecific binding or low solubility (i.e. compounds 1 and 3). ..

    Binding Assay:

    Article Title: Supporting Information
    Article Snippet: .. Using the SPR-based Biacore T200 instrument for quantitative binding-affinity experiments, we set the immobilization level of HipA(D309Q) protein at 800 RUs for most tests (i.e. compounds 2 and 4), and at 250 RUs for the compounds with high nonspecific binding or low solubility (i.e. compounds 1 and 3). ..

    Solubility:

    Article Title: Supporting Information
    Article Snippet: .. Using the SPR-based Biacore T200 instrument for quantitative binding-affinity experiments, we set the immobilization level of HipA(D309Q) protein at 800 RUs for most tests (i.e. compounds 2 and 4), and at 250 RUs for the compounds with high nonspecific binding or low solubility (i.e. compounds 1 and 3). ..

    other:

    Article Title: Mycobacterial crypto-AcpM as a tool to investigate the consequence of drug binding on its key FAS II partner enzyme HadAB.
    Article Snippet: Background Mycobacterial FASII pathway is governed by the Protein-Protein Interaction mediated dynamics existent between Acyl Carrier Protein and its partner enzymes.. The dehydratase HadAB, involved in the third step of FASII synthesis has remained a key target of drugs like Thiacetazone (TAC) and its consequence on AcpM binding is yet to be deciphered.. Owing to the transient nature of these interactions, analysing their implications as a drug target has been exhausting.



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    spr based biacore t200 instrument  (Biacore)
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    Biacore spr based biacore t200 instrument
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    surface plasmon resonance (spr)-based assay on biacore t200 instruments  (Biacore)
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    Affinity analysis of the designed antibodies. ( A ) Initial affinity screening of designed antibodies binding to Aβ1-42 oligomers and AL fibrils, respectively, by ELISA. For each experiment, control group using PBS incubated with Aβ1-42 oligomers or AL fibrils was carried out. Experiments were performed three times, and each sample was run in triplicate. Data are expressed as mean ± SEM. M1–M30: different designed mutants; wild-type: crenezumab; control: PBS. ( B ) SPR profile of a direct comparison of wild-type (WT) and mutant (M5) binding to Aβ42 oligomers and AL fibrils using the Biacore <t>T200.</t> ( C ) Further affinity analysis of M5, M10, and M29 mutants binding to Aβ1-42 oligomers and AL fibrils, respectively, by Biacore T200.
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    spr-based biacore t200 instrument  (Biacore)
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    Biacore spr-based biacore t200 instrument
    (A) Residual enzyme activity versus compound concentration. The IC 50 values were 34.8±1.3 for compound 1 , and 58.0±9.0 µM for compound 2 . The AC 50 value was 34.7±4.5 nM for compound 2. (B) Enzyme inhibition dose-response curves of compound 3. The fitted IC 50 value was 131±12 µM. (C–D) SPR dose-response curves of compound 1 , compound 2 with immobilized PGDH, respectively. The K D values were 42.6±2.1 for compound 1 (C), and 19.0±1.9 µM for compound 2 (D). K D values of the compounds 1 and 2 were obtained by fitting the data sets to 1:1 Langmuir binding model using Biacore <t>T200</t> Evaluation Software. Residuals for all SPR sensorgrams were less than 2 RU. Chi-square values were 2.4 for C and 1.2 for D.
    Spr Based Biacore T200 Instrument, 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/spr+based+biacore+t200+instrument/biacore+3000+instrument/pmc03986399-77-19-18
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    Affinity analysis of the designed antibodies. ( A ) Initial affinity screening of designed antibodies binding to Aβ1-42 oligomers and AL fibrils, respectively, by ELISA. For each experiment, control group using PBS incubated with Aβ1-42 oligomers or AL fibrils was carried out. Experiments were performed three times, and each sample was run in triplicate. Data are expressed as mean ± SEM. M1–M30: different designed mutants; wild-type: crenezumab; control: PBS. ( B ) SPR profile of a direct comparison of wild-type (WT) and mutant (M5) binding to Aβ42 oligomers and AL fibrils using the Biacore T200. ( C ) Further affinity analysis of M5, M10, and M29 mutants binding to Aβ1-42 oligomers and AL fibrils, respectively, by Biacore T200.

    Journal: International Journal of Molecular Sciences

    Article Title: Re-Engineering Therapeutic Anti-Aβ Monoclonal Antibody to Target Amyloid Light Chain

    doi: 10.3390/ijms25031593

    Figure Lengend Snippet: Affinity analysis of the designed antibodies. ( A ) Initial affinity screening of designed antibodies binding to Aβ1-42 oligomers and AL fibrils, respectively, by ELISA. For each experiment, control group using PBS incubated with Aβ1-42 oligomers or AL fibrils was carried out. Experiments were performed three times, and each sample was run in triplicate. Data are expressed as mean ± SEM. M1–M30: different designed mutants; wild-type: crenezumab; control: PBS. ( B ) SPR profile of a direct comparison of wild-type (WT) and mutant (M5) binding to Aβ42 oligomers and AL fibrils using the Biacore T200. ( C ) Further affinity analysis of M5, M10, and M29 mutants binding to Aβ1-42 oligomers and AL fibrils, respectively, by Biacore T200.

    Article Snippet: Based on the ELISA assay results, eight engineered antibodies were screening out for further binding affinity verification using a surface plasmon resonance (SPR)-based assay on Biacore T200 instruments.

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Incubation, Comparison, Mutagenesis

    (A) Residual enzyme activity versus compound concentration. The IC 50 values were 34.8±1.3 for compound 1 , and 58.0±9.0 µM for compound 2 . The AC 50 value was 34.7±4.5 nM for compound 2. (B) Enzyme inhibition dose-response curves of compound 3. The fitted IC 50 value was 131±12 µM. (C–D) SPR dose-response curves of compound 1 , compound 2 with immobilized PGDH, respectively. The K D values were 42.6±2.1 for compound 1 (C), and 19.0±1.9 µM for compound 2 (D). K D values of the compounds 1 and 2 were obtained by fitting the data sets to 1:1 Langmuir binding model using Biacore T200 Evaluation Software. Residuals for all SPR sensorgrams were less than 2 RU. Chi-square values were 2.4 for C and 1.2 for D.

    Journal: PLoS ONE

    Article Title: Discovery of Novel Allosteric Effectors Based on the Predicted Allosteric Sites for Escherichia coli D-3-Phosphoglycerate Dehydrogenase

    doi: 10.1371/journal.pone.0094829

    Figure Lengend Snippet: (A) Residual enzyme activity versus compound concentration. The IC 50 values were 34.8±1.3 for compound 1 , and 58.0±9.0 µM for compound 2 . The AC 50 value was 34.7±4.5 nM for compound 2. (B) Enzyme inhibition dose-response curves of compound 3. The fitted IC 50 value was 131±12 µM. (C–D) SPR dose-response curves of compound 1 , compound 2 with immobilized PGDH, respectively. The K D values were 42.6±2.1 for compound 1 (C), and 19.0±1.9 µM for compound 2 (D). K D values of the compounds 1 and 2 were obtained by fitting the data sets to 1:1 Langmuir binding model using Biacore T200 Evaluation Software. Residuals for all SPR sensorgrams were less than 2 RU. Chi-square values were 2.4 for C and 1.2 for D.

    Article Snippet: The binding affinity of compounds 1 and 2 towards PGDH and its mutants were assayed using the SPR-based Biacore T200 instrument.

    Techniques: Activity Assay, Concentration Assay, Enzyme Inhibition Assay, Binding Assay, Software