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tris glycine polyacrylamide native gel  (Bio-Rad)


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    Bio-Rad tris glycine polyacrylamide native gel
    Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
    Tris Glycine Polyacrylamide Native Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 7125 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/tris+glycine+polyacrylamide+native+gel/Glycine/pmc13014935-271-28-33
    Average 97 stars, based on 7125 article reviews
    tris glycine polyacrylamide native gel - by Bioz Stars, 2026-09
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    1) Product Images from "PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa"

    Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2026.111314

    Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM Tris (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
    Figure Legend Snippet: Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM Tris (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.

    Techniques Used: Binding Assay, Variant Assay, Circular Dichroism, Fluorescence, Concentration Assay

    Related Articles

    Incubation:

    Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa
    Article Snippet: .. 30 PM of oligonucleotides were added and incubated further at 37 ̊C for another 20 min. After the incubation, the protein-DNA binding reactions were run on a 10% Tris glycine polyacrylamide native gel (Bio-Rad). ..

    Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa.
    Article Snippet: .. 30 pM of oligonucleotides were added and incubated further at 37 ̊C for another 20 min. After the incubation, the protein-DNA binding reactions were run on a 10% Tris glycine polyacrylamide native gel (Bio-Rad). ..

    Binding Assay:

    Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa
    Article Snippet: .. 30 PM of oligonucleotides were added and incubated further at 37 ̊C for another 20 min. After the incubation, the protein-DNA binding reactions were run on a 10% Tris glycine polyacrylamide native gel (Bio-Rad). ..

    Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa.
    Article Snippet: .. 30 pM of oligonucleotides were added and incubated further at 37 ̊C for another 20 min. After the incubation, the protein-DNA binding reactions were run on a 10% Tris glycine polyacrylamide native gel (Bio-Rad). ..



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    Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
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    Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM Tris (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.

    Journal: The Journal of Biological Chemistry

    Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa

    doi: 10.1016/j.jbc.2026.111314

    Figure Lengend Snippet: Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM Tris (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.

    Article Snippet: 30 PM of oligonucleotides were added and incubated further at 37 ̊C for another 20 min. After the incubation, the protein-DNA binding reactions were run on a 10% Tris glycine polyacrylamide native gel (Bio-Rad).

    Techniques: Binding Assay, Variant Assay, Circular Dichroism, Fluorescence, Concentration Assay