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mouse macrophage cell line raw264 7  (ATCC)


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    Structured Review

    ATCC mouse macrophage cell line raw264 7
    O-linked β-N-acetylglucosamine in <t>RAW264.7</t> Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.
    Mouse Macrophage Cell Line Raw264 7, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse macrophage cell line raw264 7/product/ATCC
    Average 86 stars, based on 1 article reviews
    mouse macrophage cell line raw264 7 - by Bioz Stars, 2025-03
    86/100 stars

    Images

    1) Product Images from "O-linked β-N-acetylglucosamine transferase regulates macrophage polarization in diabetic periodontitis: In vivo and in vitro study"

    Article Title: O-linked β-N-acetylglucosamine transferase regulates macrophage polarization in diabetic periodontitis: In vivo and in vitro study

    Journal: World Journal of Diabetes

    doi: 10.4239/wjd.v16.i3.95092

    O-linked β-N-acetylglucosamine in RAW264.7 Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.
    Figure Legend Snippet: O-linked β-N-acetylglucosamine in RAW264.7 Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.

    Techniques Used: Western Blot, Control

    O-GlcNAc transferase promotes O-linked β-N-acetylglucosamine and phosphorylation of p38. A: The interaction between O-GlcNAc transferase (OGT) and p38 was analyzed using co-immunoprecipitation; B: The localization of OGT and p38 in RAW264.7 cells was observed using immunofluorescence staining. Scale bar: 20 μm; C: Potential O-linked β-N-acetylglucosamine (O-GlcNAcylation) sites in p38 were predicted using the DictyOGlyc 1.1 Server software; D: The O-GlcNAcylation sites were confirmed, and the effects on p38 phosphorylation were measured using Western blot; E: The relative protein expression levels were quantified. a P < 0.05. P value calculated vs wild-type. OGT: O-GlcNAc transferase; DAPI: 4’,6-Diamidino-2-phenylindole; WT: Wild-type; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; RL2: O-GlcNAc.
    Figure Legend Snippet: O-GlcNAc transferase promotes O-linked β-N-acetylglucosamine and phosphorylation of p38. A: The interaction between O-GlcNAc transferase (OGT) and p38 was analyzed using co-immunoprecipitation; B: The localization of OGT and p38 in RAW264.7 cells was observed using immunofluorescence staining. Scale bar: 20 μm; C: Potential O-linked β-N-acetylglucosamine (O-GlcNAcylation) sites in p38 were predicted using the DictyOGlyc 1.1 Server software; D: The O-GlcNAcylation sites were confirmed, and the effects on p38 phosphorylation were measured using Western blot; E: The relative protein expression levels were quantified. a P < 0.05. P value calculated vs wild-type. OGT: O-GlcNAc transferase; DAPI: 4’,6-Diamidino-2-phenylindole; WT: Wild-type; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; RL2: O-GlcNAc.

    Techniques Used: Immunoprecipitation, Immunofluorescence, Staining, Software, Western Blot, Expressing



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    O-linked β-N-acetylglucosamine in <t>RAW264.7</t> Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.
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    O-linked β-N-acetylglucosamine in <t>RAW264.7</t> Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.
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    Cell uptake and targeting capacity of MP NPs. ( A ) Representative fluorescence images of RD@P and RD@PM internalized by <t>RAW264.7</t> cells. ( B ) FACS results of cellular uptake of RD@P and RD @PM in RAW264.7 cells. ( C ) Quantification of cellular uptake of RD@P and RD@PM in RAW264.7 cells (n = 3, ∗∗ p < 0.01). ( D ) The experimental scheme of drug targeting in vivo in the implant infection model. Representative ex vivo fluorescence images ( E ) and quantification analysis ( F ) for PBS, free RD, RD@P, and RD@PM accumulation in the silicone sheets and major organs of IAI mice at 24 h after intravenous injection (n = 3, ∗∗ p < 0.01).
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    Image Search Results


    O-linked β-N-acetylglucosamine in RAW264.7 Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.

    Journal: World Journal of Diabetes

    Article Title: O-linked β-N-acetylglucosamine transferase regulates macrophage polarization in diabetic periodontitis: In vivo and in vitro study

    doi: 10.4239/wjd.v16.i3.95092

    Figure Lengend Snippet: O-linked β-N-acetylglucosamine in RAW264.7 Cells Treated with high glucose and lipopolysaccharide. A: Total O-linked β-N-acetylglucosamine levels; B: Protein levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) were measured by Western blot; C: Protein levels of OGT and OGA were quantified. a P < 0.001. P value calculated vs control. LPS: Lipopolysaccharide; HG: High glucose; OGT: O-GlcNAc transferase; OGA: O-GlcNAcase; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase.

    Article Snippet: Mouse macrophage cell line RAW264.7 was obtained from American type culture collection (Manassas, VA, United States).

    Techniques: Western Blot, Control

    O-GlcNAc transferase promotes O-linked β-N-acetylglucosamine and phosphorylation of p38. A: The interaction between O-GlcNAc transferase (OGT) and p38 was analyzed using co-immunoprecipitation; B: The localization of OGT and p38 in RAW264.7 cells was observed using immunofluorescence staining. Scale bar: 20 μm; C: Potential O-linked β-N-acetylglucosamine (O-GlcNAcylation) sites in p38 were predicted using the DictyOGlyc 1.1 Server software; D: The O-GlcNAcylation sites were confirmed, and the effects on p38 phosphorylation were measured using Western blot; E: The relative protein expression levels were quantified. a P < 0.05. P value calculated vs wild-type. OGT: O-GlcNAc transferase; DAPI: 4’,6-Diamidino-2-phenylindole; WT: Wild-type; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; RL2: O-GlcNAc.

    Journal: World Journal of Diabetes

    Article Title: O-linked β-N-acetylglucosamine transferase regulates macrophage polarization in diabetic periodontitis: In vivo and in vitro study

    doi: 10.4239/wjd.v16.i3.95092

    Figure Lengend Snippet: O-GlcNAc transferase promotes O-linked β-N-acetylglucosamine and phosphorylation of p38. A: The interaction between O-GlcNAc transferase (OGT) and p38 was analyzed using co-immunoprecipitation; B: The localization of OGT and p38 in RAW264.7 cells was observed using immunofluorescence staining. Scale bar: 20 μm; C: Potential O-linked β-N-acetylglucosamine (O-GlcNAcylation) sites in p38 were predicted using the DictyOGlyc 1.1 Server software; D: The O-GlcNAcylation sites were confirmed, and the effects on p38 phosphorylation were measured using Western blot; E: The relative protein expression levels were quantified. a P < 0.05. P value calculated vs wild-type. OGT: O-GlcNAc transferase; DAPI: 4’,6-Diamidino-2-phenylindole; WT: Wild-type; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; RL2: O-GlcNAc.

    Article Snippet: Mouse macrophage cell line RAW264.7 was obtained from American type culture collection (Manassas, VA, United States).

    Techniques: Immunoprecipitation, Immunofluorescence, Staining, Software, Western Blot, Expressing

    Cell uptake and targeting capacity of MP NPs. ( A ) Representative fluorescence images of RD@P and RD@PM internalized by RAW264.7 cells. ( B ) FACS results of cellular uptake of RD@P and RD @PM in RAW264.7 cells. ( C ) Quantification of cellular uptake of RD@P and RD@PM in RAW264.7 cells (n = 3, ∗∗ p < 0.01). ( D ) The experimental scheme of drug targeting in vivo in the implant infection model. Representative ex vivo fluorescence images ( E ) and quantification analysis ( F ) for PBS, free RD, RD@P, and RD@PM accumulation in the silicone sheets and major organs of IAI mice at 24 h after intravenous injection (n = 3, ∗∗ p < 0.01).

    Journal: Materials Today Bio

    Article Title: A macrophage-like biomimetic nanoparticle with high-efficiency biofilm disruption and innate immunity activation for implant-related infection therapy

    doi: 10.1016/j.mtbio.2025.101575

    Figure Lengend Snippet: Cell uptake and targeting capacity of MP NPs. ( A ) Representative fluorescence images of RD@P and RD@PM internalized by RAW264.7 cells. ( B ) FACS results of cellular uptake of RD@P and RD @PM in RAW264.7 cells. ( C ) Quantification of cellular uptake of RD@P and RD@PM in RAW264.7 cells (n = 3, ∗∗ p < 0.01). ( D ) The experimental scheme of drug targeting in vivo in the implant infection model. Representative ex vivo fluorescence images ( E ) and quantification analysis ( F ) for PBS, free RD, RD@P, and RD@PM accumulation in the silicone sheets and major organs of IAI mice at 24 h after intravenous injection (n = 3, ∗∗ p < 0.01).

    Article Snippet: Mouse mononuclear macrophage leukemia cell line RAW264.7 and human umbilical vein endothelial cells line (HUVEC) were obtained from Southwest Jiaotong University (Chengdu, China) and cultured in DMEM high glucose medium and F12 medium, respectively, both of which contained 10 % FBS, at 37 °C in a 5 % CO 2 humidified environment incubator (Thermo Scientific, Sunnyvale, CA).

    Techniques: Fluorescence, In Vivo, Infection, Ex Vivo, Injection

    Immunomodulatory effects of F/R@PM on macrophages in vitro. ( A ) Typical scatter plots of macrophage surface markers CD86 (M1 macrophage marker) as detected using a flow cytometer. ( B ) Representative western blot results of the expression of CD86 protein after various treatments. ( C ) Corresponding quantitative analyses of western blot results (n = 3, ∗∗ P < 0.01). ( D ) ELISA results of cytokines (TNF- α and IL-6) secreted by RAW264.7 in different groups (n = 3, ∗∗ P < 0.01). ( E ) Counted results of phagocytized S. aureus by RAW264.7 treated in different conditions (n = 3, ∗∗ P < 0.01). ( F ) Swallowed S. aureus was observed by using TEM. Yellow arrows indicate S. aureus . (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Journal: Materials Today Bio

    Article Title: A macrophage-like biomimetic nanoparticle with high-efficiency biofilm disruption and innate immunity activation for implant-related infection therapy

    doi: 10.1016/j.mtbio.2025.101575

    Figure Lengend Snippet: Immunomodulatory effects of F/R@PM on macrophages in vitro. ( A ) Typical scatter plots of macrophage surface markers CD86 (M1 macrophage marker) as detected using a flow cytometer. ( B ) Representative western blot results of the expression of CD86 protein after various treatments. ( C ) Corresponding quantitative analyses of western blot results (n = 3, ∗∗ P < 0.01). ( D ) ELISA results of cytokines (TNF- α and IL-6) secreted by RAW264.7 in different groups (n = 3, ∗∗ P < 0.01). ( E ) Counted results of phagocytized S. aureus by RAW264.7 treated in different conditions (n = 3, ∗∗ P < 0.01). ( F ) Swallowed S. aureus was observed by using TEM. Yellow arrows indicate S. aureus . (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Article Snippet: Mouse mononuclear macrophage leukemia cell line RAW264.7 and human umbilical vein endothelial cells line (HUVEC) were obtained from Southwest Jiaotong University (Chengdu, China) and cultured in DMEM high glucose medium and F12 medium, respectively, both of which contained 10 % FBS, at 37 °C in a 5 % CO 2 humidified environment incubator (Thermo Scientific, Sunnyvale, CA).

    Techniques: In Vitro, Marker, Flow Cytometry, Western Blot, Expressing, Enzyme-linked Immunosorbent Assay