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signaling inhibitors targeting p38 mapk  (MedChemExpress)


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    MedChemExpress signaling inhibitors targeting p38 mapk
    Effect of 12‐HETE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 12‐HETE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), <t>p38</t> (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).
    Signaling Inhibitors Targeting P38 Mapk, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mapk+signaling+inhibitor/pmc12997140-60-11-17?v=MedChemExpress
    Average 93 stars, based on 35 article reviews
    signaling inhibitors targeting p38 mapk - by Bioz Stars, 2026-06
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    Images

    1) Product Images from "ALOX15‐Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a Gα q –PLC–PKC Pathway"

    Article Title: ALOX15‐Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a Gα q –PLC–PKC Pathway

    Journal: The FASEB Journal

    doi: 10.1096/fj.202600272R

    Effect of 12‐HETE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 12‐HETE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).
    Figure Legend Snippet: Effect of 12‐HETE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 12‐HETE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

    Techniques Used: Protein-Protein interactions, Western Blot, Control

    Effect of 13‐HODE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 13‐HODE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).
    Figure Legend Snippet: Effect of 13‐HODE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 13‐HODE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

    Techniques Used: Protein-Protein interactions, Western Blot, Control



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    Image Search Results


    Effect of 12‐HETE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 12‐HETE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

    Journal: The FASEB Journal

    Article Title: ALOX15‐Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a Gα q –PLC–PKC Pathway

    doi: 10.1096/fj.202600272R

    Figure Lengend Snippet: Effect of 12‐HETE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 12‐HETE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

    Article Snippet: To examine the inflammatory signaling pathways involved in LPS‐mediated cytokine production, signaling inhibitors targeting p38 MAPK (SB239063; MedChemExpress, Monmouth Junction NJ, USA), NF‐κB (APDC; Merck KGaA), MEK1/2 (U0126; MedChemExpress), phosphatidyl inositol‐3 kinase (PI3K; Wortmannin; Merck KGaA), and c‐Jun N‐terminal kinase (JNK; SP600125; Merck KGaA) were administered 30 min prior to LPS treatment.

    Techniques: Protein-Protein interactions, Western Blot, Control

    Effect of 13‐HODE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 13‐HODE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

    Journal: The FASEB Journal

    Article Title: ALOX15‐Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a Gα q –PLC–PKC Pathway

    doi: 10.1096/fj.202600272R

    Figure Lengend Snippet: Effect of 13‐HODE on LPS‐induced inflammatory signaling pathways in RAW264.7 cells. RAW264.7 cells were stimulated with lipopolysaccharide (LPS; 1 ng/mL) for 30 min. Cells were pretreated with 13‐HODE (0.1–1 μmol/L) for 1 h prior to LPS stimulation. Phosphorylated p65 (B), p38 (D), ERK (E), Akt (F), and JNK (G), and IκBα protein levels (C) were analyzed by immunoblotting. Representative immunoblot images are shown (A). Because the number of samples exceeded the capacity of a single gel, samples were run on separate gels. Composite images are indicated by clearly demarcated dividing lines. Control samples were included on each gel to allow normalization across gels. Data are presented as mean ± SEM. Statistical significance was assessed using the Tukey–Kramer post hoc test. Groups not sharing a common letter differ significantly ( p < 0.05).

    Article Snippet: To examine the inflammatory signaling pathways involved in LPS‐mediated cytokine production, signaling inhibitors targeting p38 MAPK (SB239063; MedChemExpress, Monmouth Junction NJ, USA), NF‐κB (APDC; Merck KGaA), MEK1/2 (U0126; MedChemExpress), phosphatidyl inositol‐3 kinase (PI3K; Wortmannin; Merck KGaA), and c‐Jun N‐terminal kinase (JNK; SP600125; Merck KGaA) were administered 30 min prior to LPS treatment.

    Techniques: Protein-Protein interactions, Western Blot, Control