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dimethyloxalylglycine dmog  (Frontier Specialty Chemicals Inc)


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    Frontier Specialty Chemicals Inc dimethyloxalylglycine dmog
    Dimethyloxalylglycine Dmog, supplied by Frontier Specialty Chemicals Inc, used in various techniques. Bioz Stars score: 94/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 124 article reviews
    dimethyloxalylglycine dmog - by Bioz Stars, 2026-01
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    Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, <t>dimethyloxalylglycine;</t> ns, non-specific.
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    Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, <t>dimethyloxalylglycine;</t> ns, non-specific.
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    Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, <t>dimethyloxalylglycine;</t> ns, non-specific.
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    Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, <t>dimethyloxalylglycine;</t> ns, non-specific.
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    Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, <t>dimethyloxalylglycine;</t> ns, non-specific.
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    Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, dimethyloxalylglycine; ns, non-specific.

    Journal: Molecular and cellular biology

    Article Title: Selective Hypoxia-Sensitive Oxomer Formation by FIH Prevents Binding of the NF-κB Inhibitor IκBβ to NF-κB Subunits.

    doi: 10.1080/10985549.2024.2338727

    Figure Lengend Snippet: Figure 1. Selective oxomer formation between FIH and IjBb. (A) Immunoblot analysis of the oxomer formation between ectopically expressed FIH-V5 and V5-IjBb in HEK293 cells, using FIH-OTUB1 oxomer formation via ectopic expression of FIH-V5 and FLAG-OTUB1 as control. (B) Immunoblot analysis of FIH-IjBb oxomer for mation in HepG2, Hep3B and MCF7 cells with ectopic FIH-V5 and IjBb-FLAG expression. (C) Immunoprecipitation of endogenous IjBb from HEK293 cells. A signal was detected at a molecular weight consistent with a FIH-IjBb oxomer (highlighted by ). This complex was absent in the presence of the hydroxylase inhibitor DMOG (1 mM for 24 h) and in FIH knockout (KO) cells. (D) Immunoblot analysis of oxomer formation between FIH-V5 and the Indicated members of the IjB protein family following transient transfection of HEK293 cells with corresponding vectors for ectopic expression. Predicted molecular weights of putative FIH oxomers (without post-translational protein modifications): FIH-IjBa, 76 kDa; FIH-IjBb, 78 kDa; FIH-Bcl-3, 88 kDa; FIH-IjBd, 90 kDa; FIH-IjBe, 78 kDa; FIH-p105, 145 kDa; FIH- p100, 137 kDa. Data are representative of three (A, B, D) and two (C) independent experiments. F, FIH-V5; I, V5-IjBb; F-O, FIH-OTUB1 oxomer; F-I, FIH-IjBb oxomer; interm., intermediate; exp, exposure; DMOG, dimethyloxalylglycine; ns, non-specific.

    Article Snippet: Cells were treated with the following compounds dissolved in dimethylsulfoxide (DMSO, Sigma-Aldrich)56 and the final concentrations indicated: dimethyloxalylglycine (DMOG; Frontier Scientific, Logan, UT, USA; 1 mM), FG-4592 (roxadustat; Selleckchem, Houston, TX, USA; 0.1 mM) and dimethyl N-oxalyl-D-phenylalanine (DM-NOFD; Sigma-Aldrich; 1 mM).

    Techniques: Western Blot, Expressing, Control, Immunoprecipitation, Molecular Weight, Knock-Out, Transfection