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sypro orange protein dye  (Lumiprobe)


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    Structured Review

    Lumiprobe sypro orange protein dye
    ArgD binds CphB in both LAH and PAT conditions. A , the relative levels of ArgD and CphB under PAT and LAH in WT and Δ cphB were determined by immunodetection. Whole-cell lysates were separated on SDS-PAGE and blotted onto a PVDF membrane, and the ArgD and <t>CphB</t> <t>proteins</t> were detected using specific antibodies. The Ponceau staining of the membrane is shown for the loading control. Repetitions of the experiment and their statistical analysis are presented in . B , coimmunopurification of f.ArgD with CphB was performed using the same amounts of PAT- or LAH-grown f.argD/ Δ argD cells. The eluates were separated by SDS-PAGE together with the input lysates, including 50% of the lysate from the PAT-grown cells (PAT 50 ). The <t>SYPRO-stained</t> gel was subsequently blotted to a PVDF membrane, which was probed with specific antibodies against CphB and the FLAG tag of ArgD. The control f.ArgD pull-down prepared from the Δ cphB cells is shown in Ref. . CphB, cyanophycinase; f.ArgD, FLAG-tagged variant of ArgD; LAH, light-activated heterotrophic; PAT, photoautotroph; PVDF, polyvinylidene fluoride.
    Sypro Orange Protein Dye, supplied by Lumiprobe, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/proteorange+protein+gel+stain+5000/ProteOrange+Protein+Gel+Stain%2C+5000%C3%97/pmc12661447-222-6-10
    Average 93 stars, based on 11 article reviews
    sypro orange protein dye - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Cyanophycinase is required for heterotrophy in cyanobacteria"

    Article Title: Cyanophycinase is required for heterotrophy in cyanobacteria

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2025.110791

    ArgD binds CphB in both LAH and PAT conditions. A , the relative levels of ArgD and CphB under PAT and LAH in WT and Δ cphB were determined by immunodetection. Whole-cell lysates were separated on SDS-PAGE and blotted onto a PVDF membrane, and the ArgD and CphB proteins were detected using specific antibodies. The Ponceau staining of the membrane is shown for the loading control. Repetitions of the experiment and their statistical analysis are presented in . B , coimmunopurification of f.ArgD with CphB was performed using the same amounts of PAT- or LAH-grown f.argD/ Δ argD cells. The eluates were separated by SDS-PAGE together with the input lysates, including 50% of the lysate from the PAT-grown cells (PAT 50 ). The SYPRO-stained gel was subsequently blotted to a PVDF membrane, which was probed with specific antibodies against CphB and the FLAG tag of ArgD. The control f.ArgD pull-down prepared from the Δ cphB cells is shown in Ref. . CphB, cyanophycinase; f.ArgD, FLAG-tagged variant of ArgD; LAH, light-activated heterotrophic; PAT, photoautotroph; PVDF, polyvinylidene fluoride.
    Figure Legend Snippet: ArgD binds CphB in both LAH and PAT conditions. A , the relative levels of ArgD and CphB under PAT and LAH in WT and Δ cphB were determined by immunodetection. Whole-cell lysates were separated on SDS-PAGE and blotted onto a PVDF membrane, and the ArgD and CphB proteins were detected using specific antibodies. The Ponceau staining of the membrane is shown for the loading control. Repetitions of the experiment and their statistical analysis are presented in . B , coimmunopurification of f.ArgD with CphB was performed using the same amounts of PAT- or LAH-grown f.argD/ Δ argD cells. The eluates were separated by SDS-PAGE together with the input lysates, including 50% of the lysate from the PAT-grown cells (PAT 50 ). The SYPRO-stained gel was subsequently blotted to a PVDF membrane, which was probed with specific antibodies against CphB and the FLAG tag of ArgD. The control f.ArgD pull-down prepared from the Δ cphB cells is shown in Ref. . CphB, cyanophycinase; f.ArgD, FLAG-tagged variant of ArgD; LAH, light-activated heterotrophic; PAT, photoautotroph; PVDF, polyvinylidene fluoride.

    Techniques Used: Immunodetection, SDS Page, Membrane, Staining, Control, FLAG-tag, Variant Assay

    Related Articles

    Fluorescence:

    Article Title: Targeted Modification of Mammalian DNA by a Novel Type V Cas12a Endonuclease from Ruminococcus bromii
    Article Snippet: .. To investigate RbCas12a thermostability, a fluorescent-based assay was performed using ProteOrange Protein Gel Stain 5000× (Lumiprobe RUS Ltd., Moscow, Russia) under the following conditions: we used 9 μg purified RbCas12a, 12.5 μL NEBuffer 2 (New England Biolabs, Ipswich, MA, USA), and 2.5 μL ProteOrange Protein Gel Stain (diluted to 50×) in 25-μL reactions. ..

    Article Title: Targeted Modification of Mammalian DNA by a Novel Type V Cas12a Endonuclease from Ruminococcus bromii .
    Article Snippet: .. To investigate RbCas12a thermostability, a fluorescent-based assay was performed using ProteOrange Protein Gel Stain 5000× (Lumiprobe RUS Ltd., Moscow, Russia) under the following conditions: we used 9 μg purified RbCas12a, 12.5 μL NEBuffer 2 (New England Biolabs, Ipswich, MA, USA), and 2.5 μL ProteOrange Protein Gel Stain (diluted Int. ..

    Staining:

    Article Title: Targeted Modification of Mammalian DNA by a Novel Type V Cas12a Endonuclease from Ruminococcus bromii
    Article Snippet: .. To investigate RbCas12a thermostability, a fluorescent-based assay was performed using ProteOrange Protein Gel Stain 5000× (Lumiprobe RUS Ltd., Moscow, Russia) under the following conditions: we used 9 μg purified RbCas12a, 12.5 μL NEBuffer 2 (New England Biolabs, Ipswich, MA, USA), and 2.5 μL ProteOrange Protein Gel Stain (diluted to 50×) in 25-μL reactions. ..

    Article Title: Targeted Modification of Mammalian DNA by a Novel Type V Cas12a Endonuclease from Ruminococcus bromii .
    Article Snippet: .. To investigate RbCas12a thermostability, a fluorescent-based assay was performed using ProteOrange Protein Gel Stain 5000× (Lumiprobe RUS Ltd., Moscow, Russia) under the following conditions: we used 9 μg purified RbCas12a, 12.5 μL NEBuffer 2 (New England Biolabs, Ipswich, MA, USA), and 2.5 μL ProteOrange Protein Gel Stain (diluted Int. ..

    Purification:

    Article Title: Targeted Modification of Mammalian DNA by a Novel Type V Cas12a Endonuclease from Ruminococcus bromii
    Article Snippet: .. To investigate RbCas12a thermostability, a fluorescent-based assay was performed using ProteOrange Protein Gel Stain 5000× (Lumiprobe RUS Ltd., Moscow, Russia) under the following conditions: we used 9 μg purified RbCas12a, 12.5 μL NEBuffer 2 (New England Biolabs, Ipswich, MA, USA), and 2.5 μL ProteOrange Protein Gel Stain (diluted to 50×) in 25-μL reactions. ..

    Article Title: Targeted Modification of Mammalian DNA by a Novel Type V Cas12a Endonuclease from Ruminococcus bromii .
    Article Snippet: .. To investigate RbCas12a thermostability, a fluorescent-based assay was performed using ProteOrange Protein Gel Stain 5000× (Lumiprobe RUS Ltd., Moscow, Russia) under the following conditions: we used 9 μg purified RbCas12a, 12.5 μL NEBuffer 2 (New England Biolabs, Ipswich, MA, USA), and 2.5 μL ProteOrange Protein Gel Stain (diluted Int. ..



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    ArgD binds CphB in both LAH and PAT conditions. A , the relative levels of ArgD and CphB under PAT and LAH in WT and Δ cphB were determined by immunodetection. Whole-cell lysates were separated on SDS-PAGE and blotted onto a PVDF membrane, and the ArgD and <t>CphB</t> <t>proteins</t> were detected using specific antibodies. The Ponceau staining of the membrane is shown for the loading control. Repetitions of the experiment and their statistical analysis are presented in . B , coimmunopurification of f.ArgD with CphB was performed using the same amounts of PAT- or LAH-grown f.argD/ Δ argD cells. The eluates were separated by SDS-PAGE together with the input lysates, including 50% of the lysate from the PAT-grown cells (PAT 50 ). The <t>SYPRO-stained</t> gel was subsequently blotted to a PVDF membrane, which was probed with specific antibodies against CphB and the FLAG tag of ArgD. The control f.ArgD pull-down prepared from the Δ cphB cells is shown in Ref. . CphB, cyanophycinase; f.ArgD, FLAG-tagged variant of ArgD; LAH, light-activated heterotrophic; PAT, photoautotroph; PVDF, polyvinylidene fluoride.
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    Image Search Results


    ArgD binds CphB in both LAH and PAT conditions. A , the relative levels of ArgD and CphB under PAT and LAH in WT and Δ cphB were determined by immunodetection. Whole-cell lysates were separated on SDS-PAGE and blotted onto a PVDF membrane, and the ArgD and CphB proteins were detected using specific antibodies. The Ponceau staining of the membrane is shown for the loading control. Repetitions of the experiment and their statistical analysis are presented in . B , coimmunopurification of f.ArgD with CphB was performed using the same amounts of PAT- or LAH-grown f.argD/ Δ argD cells. The eluates were separated by SDS-PAGE together with the input lysates, including 50% of the lysate from the PAT-grown cells (PAT 50 ). The SYPRO-stained gel was subsequently blotted to a PVDF membrane, which was probed with specific antibodies against CphB and the FLAG tag of ArgD. The control f.ArgD pull-down prepared from the Δ cphB cells is shown in Ref. . CphB, cyanophycinase; f.ArgD, FLAG-tagged variant of ArgD; LAH, light-activated heterotrophic; PAT, photoautotroph; PVDF, polyvinylidene fluoride.

    Journal: The Journal of Biological Chemistry

    Article Title: Cyanophycinase is required for heterotrophy in cyanobacteria

    doi: 10.1016/j.jbc.2025.110791

    Figure Lengend Snippet: ArgD binds CphB in both LAH and PAT conditions. A , the relative levels of ArgD and CphB under PAT and LAH in WT and Δ cphB were determined by immunodetection. Whole-cell lysates were separated on SDS-PAGE and blotted onto a PVDF membrane, and the ArgD and CphB proteins were detected using specific antibodies. The Ponceau staining of the membrane is shown for the loading control. Repetitions of the experiment and their statistical analysis are presented in . B , coimmunopurification of f.ArgD with CphB was performed using the same amounts of PAT- or LAH-grown f.argD/ Δ argD cells. The eluates were separated by SDS-PAGE together with the input lysates, including 50% of the lysate from the PAT-grown cells (PAT 50 ). The SYPRO-stained gel was subsequently blotted to a PVDF membrane, which was probed with specific antibodies against CphB and the FLAG tag of ArgD. The control f.ArgD pull-down prepared from the Δ cphB cells is shown in Ref. . CphB, cyanophycinase; f.ArgD, FLAG-tagged variant of ArgD; LAH, light-activated heterotrophic; PAT, photoautotroph; PVDF, polyvinylidene fluoride.

    Article Snippet: The proteins were separated, visualized with SYPRO orange protein dye (Lumiprobe ProteOrange, catalog no.: 40210) and transferred onto a polyvinylidene fluoride membrane (Sigma–Aldrich, Immobilon-P, catalog no.: IPVH00010) that was subsequently incubated with primary anti-CphB and anti-ArgD antibodies ( ).

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