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5(6)-carboxytetramethylrhodamine succinimidyl ester tmr-nhs ester  (Thermo Fisher)


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    Structured Review

    Thermo Fisher 5(6)-carboxytetramethylrhodamine succinimidyl ester tmr-nhs ester
    5(6) Carboxytetramethylrhodamine Succinimidyl Ester Tmr Nhs Ester, supplied by Thermo Fisher, 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/tmr+nhs-ester/alexa+fluor+647+nhs+ester/pm39221867__ja4c10533_si_001-11-0-19
    Average 90 stars, based on 1 article reviews
    5(6)-carboxytetramethylrhodamine succinimidyl ester tmr-nhs ester - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Staining:

    Article Title: Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor.
    Article Snippet: Cells were washed with TBS- a Tx, stained with 0.5 g/ml TMR NHS-ester (Molecular Probes t C-1171) for 10 min, washed with TBS-Tx, incubated with 1 g/ml Hoechst for 2 min (found to be necessary for uniform NHS-ester staining, possibly by quenching any remaining NHS-ester), washed A2 times with TBS-Tx, and mounted.

    Incubation:

    Article Title: Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor.
    Article Snippet: Cells were washed with TBS- a Tx, stained with 0.5 g/ml TMR NHS-ester (Molecular Probes t C-1171) for 10 min, washed with TBS-Tx, incubated with 1 g/ml Hoechst for 2 min (found to be necessary for uniform NHS-ester staining, possibly by quenching any remaining NHS-ester), washed A2 times with TBS-Tx, and mounted.



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    Fluorescence polarization was used to measure the competitive displacement of <t>BODIPY</t> TMR-X-labeled P11 from RTA by the unlabeled P11 peptide (A) and small molecule inhibitors (B–F). Reactions containing labeled P11 (1 μM), and RTA (3 μM) were incubated with varying concentrations of inhibitors in 40 μL of 1X FP buffer (25 mM Tris-HCl pH 8.0 and 100 mM NaCl) for 30 min in the dark at room temperature followed by centrifugation at 400g for two minutes and scanned using BioTek Synergy 4 microplate reader. Anisotropy values were obtained using 530/25 nm excitation bandpass and 590/35 emission filters. Normalized values for the percentage of binding (%) were plotted against the inhibitor concentration and the IC 50 values obtained by FP were used to calculate the K i values as described in the Materials and Methods. The different colored data points represent 4 different measurements.
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    Image Search Results


    Fluorescence polarization was used to measure the competitive displacement of BODIPY TMR-X-labeled P11 from RTA by the unlabeled P11 peptide (A) and small molecule inhibitors (B–F). Reactions containing labeled P11 (1 μM), and RTA (3 μM) were incubated with varying concentrations of inhibitors in 40 μL of 1X FP buffer (25 mM Tris-HCl pH 8.0 and 100 mM NaCl) for 30 min in the dark at room temperature followed by centrifugation at 400g for two minutes and scanned using BioTek Synergy 4 microplate reader. Anisotropy values were obtained using 530/25 nm excitation bandpass and 590/35 emission filters. Normalized values for the percentage of binding (%) were plotted against the inhibitor concentration and the IC 50 values obtained by FP were used to calculate the K i values as described in the Materials and Methods. The different colored data points represent 4 different measurements.

    Journal: Bioorganic & medicinal chemistry

    Article Title: Structure-based design and optimization of a new class of small molecule inhibitors targeting the P-stalk binding pocket of ricin

    doi: 10.1016/j.bmc.2024.117614

    Figure Lengend Snippet: Fluorescence polarization was used to measure the competitive displacement of BODIPY TMR-X-labeled P11 from RTA by the unlabeled P11 peptide (A) and small molecule inhibitors (B–F). Reactions containing labeled P11 (1 μM), and RTA (3 μM) were incubated with varying concentrations of inhibitors in 40 μL of 1X FP buffer (25 mM Tris-HCl pH 8.0 and 100 mM NaCl) for 30 min in the dark at room temperature followed by centrifugation at 400g for two minutes and scanned using BioTek Synergy 4 microplate reader. Anisotropy values were obtained using 530/25 nm excitation bandpass and 590/35 emission filters. Normalized values for the percentage of binding (%) were plotted against the inhibitor concentration and the IC 50 values obtained by FP were used to calculate the K i values as described in the Materials and Methods. The different colored data points represent 4 different measurements.

    Article Snippet: P11 was labeled with the BODIPY TM TMR-X NHS ester dye (ThermoFisher) at the N -terminus and separated from a free dye by semi-preparative HPLC (ACCQPrep, Gemini 30 × 150 mm C-18 column,42.5 mL/min flow rate, eluent A: 0.1 % TFA in water, eluent B 0.1 % TFA in acetonitrile; gradient: B 5 to 100 % in 40 min).

    Techniques: Fluorescence, Labeling, Incubation, Centrifugation, Binding Assay, Concentration Assay