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ogt polyclonal antibody  (Proteintech)


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    Structured Review

    Proteintech ogt polyclonal antibody
    Ogt Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ogt polyclonal antibody/product/Proteintech
    Average 96 stars, based on 112 article reviews
    ogt polyclonal antibody - by Bioz Stars, 2026-06
    96/100 stars

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    Proteintech ogt polyclonal antibody
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    O-GlcNAcylation enhances the stability of NONO protein. A Left panel: O-GlcNAcylation promotes NONO recruitment to DNA damage sites. U2OS cells expressing GFP-NONO were subjected to laser microirradiation, with or without OSMI-1 treatment. Scale bar: 5 μm. Right panel: Quantification of GFP-NONO intensity at laser-induced damage sites. The intensity of GFP-NONO at laser stripes was quantified at indicated time points using Image J, and peak fluorescence density in the micro-irradiated areas was plotted against time. B Left panel: Inhibition of O-GlcNAcylation reduces NONO binding to chromatin. HEK293T cells were transfected with SFB-NONO and treated with either DMSO or 20 μM OSMI-1 for 48 h. Whole cell extract (WCE), non-chromatin, and chromatin fractions of cells were harvested and analyzed by immunoblotting with the indicated antibodies. Right panel: Quantification of Flag (NONO) level, normalized to <t>histone</t> <t>H3</t> levels in chromatin and presented as fold change relative to control samples ( n = 3 per condition). C Left panel: Time-dependent degradation of NONO upon OGT inhibition. HEK293T cells were treated with 20 μM OSMI-1 or mock treatment for up to 72 h. NONO protein levels were assessed using Western blot, with GAPDH serving as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH levels and presented as fold change relative to control samples ( n = 3 per condition). D Left panel: Inhibition of O-GlcNAcylation accelerates NONO degradation. HEK293T cells were treated with either DMSO or 20 μM OSMI-1 for 48 h, followed by 50 μM CHX treatment for up to 8 h. NONO protein levels were monitored using Western blot analysis, with GAPDH as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH and presented as fold change relative to control samples ( n = 3 per condition)
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    O-GlcNAcylation enhances the stability of NONO protein. A Left panel: O-GlcNAcylation promotes NONO recruitment to DNA damage sites. U2OS cells expressing GFP-NONO were subjected to laser microirradiation, with or without OSMI-1 treatment. Scale bar: 5 μm. Right panel: Quantification of GFP-NONO intensity at laser-induced damage sites. The intensity of GFP-NONO at laser stripes was quantified at indicated time points using Image J, and peak fluorescence density in the micro-irradiated areas was plotted against time. B Left panel: Inhibition of O-GlcNAcylation reduces NONO binding to chromatin. HEK293T cells were transfected with SFB-NONO and treated with either DMSO or 20 μM OSMI-1 for 48 h. Whole cell extract (WCE), non-chromatin, and chromatin fractions of cells were harvested and analyzed by immunoblotting with the indicated antibodies. Right panel: Quantification of Flag (NONO) level, normalized to <t>histone</t> <t>H3</t> levels in chromatin and presented as fold change relative to control samples ( n = 3 per condition). C Left panel: Time-dependent degradation of NONO upon OGT inhibition. HEK293T cells were treated with 20 μM OSMI-1 or mock treatment for up to 72 h. NONO protein levels were assessed using Western blot, with GAPDH serving as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH levels and presented as fold change relative to control samples ( n = 3 per condition). D Left panel: Inhibition of O-GlcNAcylation accelerates NONO degradation. HEK293T cells were treated with either DMSO or 20 μM OSMI-1 for 48 h, followed by 50 μM CHX treatment for up to 8 h. NONO protein levels were monitored using Western blot analysis, with GAPDH as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH and presented as fold change relative to control samples ( n = 3 per condition)
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    O-GlcNAcylation enhances the stability of NONO protein. A Left panel: O-GlcNAcylation promotes NONO recruitment to DNA damage sites. U2OS cells expressing GFP-NONO were subjected to laser microirradiation, with or without OSMI-1 treatment. Scale bar: 5 μm. Right panel: Quantification of GFP-NONO intensity at laser-induced damage sites. The intensity of GFP-NONO at laser stripes was quantified at indicated time points using Image J, and peak fluorescence density in the micro-irradiated areas was plotted against time. B Left panel: Inhibition of O-GlcNAcylation reduces NONO binding to chromatin. HEK293T cells were transfected with SFB-NONO and treated with either DMSO or 20 μM OSMI-1 for 48 h. Whole cell extract (WCE), non-chromatin, and chromatin fractions of cells were harvested and analyzed by immunoblotting with the indicated antibodies. Right panel: Quantification of Flag (NONO) level, normalized to <t>histone</t> <t>H3</t> levels in chromatin and presented as fold change relative to control samples ( n = 3 per condition). C Left panel: Time-dependent degradation of NONO upon OGT inhibition. HEK293T cells were treated with 20 μM OSMI-1 or mock treatment for up to 72 h. NONO protein levels were assessed using Western blot, with GAPDH serving as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH levels and presented as fold change relative to control samples ( n = 3 per condition). D Left panel: Inhibition of O-GlcNAcylation accelerates NONO degradation. HEK293T cells were treated with either DMSO or 20 μM OSMI-1 for 48 h, followed by 50 μM CHX treatment for up to 8 h. NONO protein levels were monitored using Western blot analysis, with GAPDH as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH and presented as fold change relative to control samples ( n = 3 per condition)
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    Reagents and tools table
    Rabbit Anti Ogt Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ogt Rabbit Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc ogt rabbit polyclonal antibody

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    Proteintech rabbit polyclonal antibodies recognizing ogt

    Rabbit Polyclonal Antibodies Recognizing Ogt, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    O-GlcNAcylation enhances the stability of NONO protein. A Left panel: O-GlcNAcylation promotes NONO recruitment to DNA damage sites. U2OS cells expressing GFP-NONO were subjected to laser microirradiation, with or without OSMI-1 treatment. Scale bar: 5 μm. Right panel: Quantification of GFP-NONO intensity at laser-induced damage sites. The intensity of GFP-NONO at laser stripes was quantified at indicated time points using Image J, and peak fluorescence density in the micro-irradiated areas was plotted against time. B Left panel: Inhibition of O-GlcNAcylation reduces NONO binding to chromatin. HEK293T cells were transfected with SFB-NONO and treated with either DMSO or 20 μM OSMI-1 for 48 h. Whole cell extract (WCE), non-chromatin, and chromatin fractions of cells were harvested and analyzed by immunoblotting with the indicated antibodies. Right panel: Quantification of Flag (NONO) level, normalized to histone H3 levels in chromatin and presented as fold change relative to control samples ( n = 3 per condition). C Left panel: Time-dependent degradation of NONO upon OGT inhibition. HEK293T cells were treated with 20 μM OSMI-1 or mock treatment for up to 72 h. NONO protein levels were assessed using Western blot, with GAPDH serving as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH levels and presented as fold change relative to control samples ( n = 3 per condition). D Left panel: Inhibition of O-GlcNAcylation accelerates NONO degradation. HEK293T cells were treated with either DMSO or 20 μM OSMI-1 for 48 h, followed by 50 μM CHX treatment for up to 8 h. NONO protein levels were monitored using Western blot analysis, with GAPDH as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH and presented as fold change relative to control samples ( n = 3 per condition)

    Journal: Genome Biology

    Article Title: O-GlcNAcylation of NONO mediates alternative splicing of SETMAR and facilitates NHEJ repair

    doi: 10.1186/s13059-026-03930-5

    Figure Lengend Snippet: O-GlcNAcylation enhances the stability of NONO protein. A Left panel: O-GlcNAcylation promotes NONO recruitment to DNA damage sites. U2OS cells expressing GFP-NONO were subjected to laser microirradiation, with or without OSMI-1 treatment. Scale bar: 5 μm. Right panel: Quantification of GFP-NONO intensity at laser-induced damage sites. The intensity of GFP-NONO at laser stripes was quantified at indicated time points using Image J, and peak fluorescence density in the micro-irradiated areas was plotted against time. B Left panel: Inhibition of O-GlcNAcylation reduces NONO binding to chromatin. HEK293T cells were transfected with SFB-NONO and treated with either DMSO or 20 μM OSMI-1 for 48 h. Whole cell extract (WCE), non-chromatin, and chromatin fractions of cells were harvested and analyzed by immunoblotting with the indicated antibodies. Right panel: Quantification of Flag (NONO) level, normalized to histone H3 levels in chromatin and presented as fold change relative to control samples ( n = 3 per condition). C Left panel: Time-dependent degradation of NONO upon OGT inhibition. HEK293T cells were treated with 20 μM OSMI-1 or mock treatment for up to 72 h. NONO protein levels were assessed using Western blot, with GAPDH serving as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH levels and presented as fold change relative to control samples ( n = 3 per condition). D Left panel: Inhibition of O-GlcNAcylation accelerates NONO degradation. HEK293T cells were treated with either DMSO or 20 μM OSMI-1 for 48 h, followed by 50 μM CHX treatment for up to 8 h. NONO protein levels were monitored using Western blot analysis, with GAPDH as the loading control. Right panel: Quantification of NONO level, normalized to GAPDH and presented as fold change relative to control samples ( n = 3 per condition)

    Article Snippet: Antibodies used in this study include the following: Anti-DDDDK-tag mAb (MBL, M185-3L), Anti-Myc-tag mAb (MBL, M047-3), Anti-GAPDH (Proteintech, 60,004–1-Ig), OGT polyclonal antibody (Proteintech, 11,576–2-AP), NONO polyclonal antibody (Proteintech, 11,058–1-AP), RL2 (Santa cruz biotechnology, SC-59624, which is an antibody against O-GlcNAc), Histone-H3 polyclonal antibody (Proteintech, 17,168–1-AP), anti-HA (Sigma, 66,006–2-Ig), Anti-PAR monoclonal antibody (R&D, 4335-MC-100-AC), Ku80 polyclonal antibody (Proteintech, 16,389–1-AP), SFPQ polyclonal antibody (Proteintech, 15,585–1-AP), anti-Histone H3(di-methyl K36) polyclonal antibody (abcam, AB9049), Ku70 polyclonal antibody (Proteintech, 10,723–1-AP), anti-SETMAR polyclonal antibody (abcam, ab129455), anti-RAD51 monoclonal antibody(abcam, ab133534).

    Techniques: Expressing, Fluorescence, Irradiation, Inhibition, Binding Assay, Transfection, Western Blot, Control

    Reagents and tools table

    Journal: The EMBO Journal

    Article Title: FOXP1 phosphorylation antagonizes its O-GlcNAcylation in regulating ATR activation in response to replication stress

    doi: 10.1038/s44318-024-00323-x

    Figure Lengend Snippet: Reagents and tools table

    Article Snippet: Rabbit anti-OGT polyclonal antibody , Proteintech Group , Cat # 11576-2-AP.

    Techniques: Recombinant, Sequencing, shRNA, Modification, Transfection, Protease Inhibitor, Cloning, In Situ, Software

    Journal: iScience

    Article Title: OGT/HIF-2α axis promotes the progression of clear cell renal cell carcinoma and regulates its sensitivity to ferroptosis

    doi: 10.1016/j.isci.2023.108148

    Figure Lengend Snippet:

    Article Snippet: OGT Rabbit Polyclonal antibody , Cell Signaling Technology , Cat#24083.

    Techniques: Ubiquitin Proteomics, Recombinant, Luciferase, CRISPR, Plasmid Preparation, Software