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mitogen activated protein kinase mapk signaling pathway  (MedChemExpress)


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    Structured Review

    MedChemExpress mitogen activated protein kinase mapk signaling pathway
    Mitogen Activated Protein Kinase Mapk Signaling Pathway, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mapk+pathway/PD318088/10__34133_slash_cancomm__0048-53-7-23
    Average 94 stars, based on 2 article reviews
    mitogen activated protein kinase mapk signaling pathway - by Bioz Stars, 2026-09
    94/100 stars

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    Related Articles

    Sequencing:

    Article Title: m6A‐Mediated Stabilization of PRMT9 mRNA by IGF2BP1 Drives Proliferation and Metastasis in Lung Adenocarcinoma
    Article Snippet: The overexpression vector or siRNA mentioned above was mixed with Lipofectamine 2000 reagent (Invitrogen, Carlsbad, CA, USA) and added to the cell culture medium for transfection into LUAD cells. .. In addition, the cells were also treated with inhibitors of RAS (RAS/RAS‐RAF‐IN‐1, 5.0 μM; CAS No. : 2447039‐81‐6; MCE, Monmouth Junction, NJ, USA) and the MAPK pathway (MAPK‐IN‐1, 10.0 μM; CAS No. : 2470587‐69‐8, MCE) for 24 h. To investigate the transcriptional regulation of PRMT9 , the 2000 bp sequence upstream of the transcription start site was cloned and recombined into the pGL3‐Basic plasmid. .. After transfection of the recombinant plasmid into A549 and H1568 cells for 24 h, a fluorescent substrate was added and a double fluorescence assay was performed under a fluorescence microscope (Leica, Wetzlar, Germany).

    Clone Assay:

    Article Title: m6A‐Mediated Stabilization of PRMT9 mRNA by IGF2BP1 Drives Proliferation and Metastasis in Lung Adenocarcinoma
    Article Snippet: The overexpression vector or siRNA mentioned above was mixed with Lipofectamine 2000 reagent (Invitrogen, Carlsbad, CA, USA) and added to the cell culture medium for transfection into LUAD cells. .. In addition, the cells were also treated with inhibitors of RAS (RAS/RAS‐RAF‐IN‐1, 5.0 μM; CAS No. : 2447039‐81‐6; MCE, Monmouth Junction, NJ, USA) and the MAPK pathway (MAPK‐IN‐1, 10.0 μM; CAS No. : 2470587‐69‐8, MCE) for 24 h. To investigate the transcriptional regulation of PRMT9 , the 2000 bp sequence upstream of the transcription start site was cloned and recombined into the pGL3‐Basic plasmid. .. After transfection of the recombinant plasmid into A549 and H1568 cells for 24 h, a fluorescent substrate was added and a double fluorescence assay was performed under a fluorescence microscope (Leica, Wetzlar, Germany).

    Plasmid Preparation:

    Article Title: m6A‐Mediated Stabilization of PRMT9 mRNA by IGF2BP1 Drives Proliferation and Metastasis in Lung Adenocarcinoma
    Article Snippet: The overexpression vector or siRNA mentioned above was mixed with Lipofectamine 2000 reagent (Invitrogen, Carlsbad, CA, USA) and added to the cell culture medium for transfection into LUAD cells. .. In addition, the cells were also treated with inhibitors of RAS (RAS/RAS‐RAF‐IN‐1, 5.0 μM; CAS No. : 2447039‐81‐6; MCE, Monmouth Junction, NJ, USA) and the MAPK pathway (MAPK‐IN‐1, 10.0 μM; CAS No. : 2470587‐69‐8, MCE) for 24 h. To investigate the transcriptional regulation of PRMT9 , the 2000 bp sequence upstream of the transcription start site was cloned and recombined into the pGL3‐Basic plasmid. .. After transfection of the recombinant plasmid into A549 and H1568 cells for 24 h, a fluorescent substrate was added and a double fluorescence assay was performed under a fluorescence microscope (Leica, Wetzlar, Germany).

    Activation Assay:

    Article Title: CD36 promotes iron accumulation and dysfunction in CD8 + T cells via the p38-CEBPB-TfR1 axis in earlystage hepatocellular carcinoma
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, divalent metal transporter 1 (DMT1), CD36 and acyl-CoA synthetase long-chain family 4 (ACSL4) in CD8+ T cells following treatment with FAC for 4 and 12 hours. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n=3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+ T cells following treatment with FAC for 4 and 12 hours. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+ T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC stimulation (5 mM) for 12 hours. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY112847A MCE, 10 μM). ..

    Article Title: CD36 Promotes Iron Accumulation and Dysfunction in CD8+ T Cells via the p38-CEBPB-TfR1 Axis in Early-stage Hepatocellular Carcinoma.
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, DMT1, CD36 and ACSL4 in CD8+ T cells following treatment with FAC for 4 and 12 h. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n = 3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+T cells following treatment with FAC for 4 and 12 h. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC-stimulation (5mM) for 12h. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY-112847A MCE, 10 μM). ..

    Quantitative RT-PCR:

    Article Title: CD36 promotes iron accumulation and dysfunction in CD8 + T cells via the p38-CEBPB-TfR1 axis in earlystage hepatocellular carcinoma
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, divalent metal transporter 1 (DMT1), CD36 and acyl-CoA synthetase long-chain family 4 (ACSL4) in CD8+ T cells following treatment with FAC for 4 and 12 hours. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n=3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+ T cells following treatment with FAC for 4 and 12 hours. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+ T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC stimulation (5 mM) for 12 hours. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY112847A MCE, 10 μM). ..

    Article Title: CD36 Promotes Iron Accumulation and Dysfunction in CD8+ T Cells via the p38-CEBPB-TfR1 Axis in Early-stage Hepatocellular Carcinoma.
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, DMT1, CD36 and ACSL4 in CD8+ T cells following treatment with FAC for 4 and 12 h. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n = 3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+T cells following treatment with FAC for 4 and 12 h. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC-stimulation (5mM) for 12h. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY-112847A MCE, 10 μM). ..

    Western Blot:

    Article Title: CD36 promotes iron accumulation and dysfunction in CD8 + T cells via the p38-CEBPB-TfR1 axis in earlystage hepatocellular carcinoma
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, divalent metal transporter 1 (DMT1), CD36 and acyl-CoA synthetase long-chain family 4 (ACSL4) in CD8+ T cells following treatment with FAC for 4 and 12 hours. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n=3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+ T cells following treatment with FAC for 4 and 12 hours. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+ T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC stimulation (5 mM) for 12 hours. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY112847A MCE, 10 μM). ..

    Article Title: CD36 Promotes Iron Accumulation and Dysfunction in CD8+ T Cells via the p38-CEBPB-TfR1 Axis in Early-stage Hepatocellular Carcinoma.
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, DMT1, CD36 and ACSL4 in CD8+ T cells following treatment with FAC for 4 and 12 h. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n = 3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+T cells following treatment with FAC for 4 and 12 h. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC-stimulation (5mM) for 12h. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY-112847A MCE, 10 μM). ..

    Expressing:

    Article Title: CD36 promotes iron accumulation and dysfunction in CD8 + T cells via the p38-CEBPB-TfR1 axis in earlystage hepatocellular carcinoma
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, divalent metal transporter 1 (DMT1), CD36 and acyl-CoA synthetase long-chain family 4 (ACSL4) in CD8+ T cells following treatment with FAC for 4 and 12 hours. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n=3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+ T cells following treatment with FAC for 4 and 12 hours. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+ T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC stimulation (5 mM) for 12 hours. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY112847A MCE, 10 μM). ..

    Article Title: CD36 Promotes Iron Accumulation and Dysfunction in CD8+ T Cells via the p38-CEBPB-TfR1 Axis in Early-stage Hepatocellular Carcinoma.
    Article Snippet: .. CD36 contributes to the activation of p38-CEBPB-TfR1 signaling. (A) Protein levels of TfR1, DMT1, CD36 and ACSL4 in CD8+ T cells following treatment with FAC for 4 and 12 h. (B) Efficiency of CD36 depletion in splenic CD8+ T cells of CD36-/- mice, measured by qRT-PCR and western blotting. n = 3 mice. (C) Protein levels of IRP1 and IRP2 in CD8+ T cells or CD36-/- CD8+T cells following treatment with FAC for 4 and 12 h. (D) Heatmap showing relative expression of genes enriched in MAPK pathway. (E) phopho-p38, CEBPB and CEBPD protein expression levels in WT CD8+T cells, CD36-/- CD8+ T cells and CD36-/- CD8+ T cells overexpressing CD36 with or without FAC-stimulation (5mM) for 12h. (F) WT CD8+ T cells were treated with FAC, the combination of oxLDL and FAC with or without the presence of CD36 inhibitor SSO (HY-112847A MCE, 10 μM). ..



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    Image Search Results


    Oba inhibits the TLR4/MyD88/p38 MAPK signaling pathway in both in vivo and in vitro experiments. ( A – D ) Molecular docking analysis of Oba with TLR4. ( E – H ) Molecular docking analysis of Oba with MyD88. ( I – L ) Molecular docking analysis of Oba with p38. For each protein, the analysis is presented as: an overall docking pose with the binding region outlined by a red dashed box ( A, E, I ); a close-up view of the binding region ( B, F, J ); a surface representation ( C, G, K ); and a two-dimensional interaction diagram ( D, H, L ). ( M ) Representative Western blot image of TLR4, MyD88, p-p38 and p38 protein in BV-2 cells. The plus and minus signs (+, -) denote the presence or absence of the following reagents in culture: LPS, and 50 μM Oba. ( N ) Quantitative analysis of TLR4 and MyD88 protein levels and p38 phosphorylation in BV-2 cells (n = 5). ( O ) Western blot analysis of TLR4, MyD88, p-p38, and p38 in spinal cord tissues from Sham, SCI, and SCI + Oba (20 mg/kg) groups at 3 days post-SCI. ( P ) Quantitative analysis of TLR4 and MyD88 protein levels and p38 phosphorylation in spinal cord tissues (n = 5). The values are presented as mean ± SD. *p<0.05, **p<0.01, ***p<0.001; NS, not significant.

    Journal: Drug Design, Development and Therapy

    Article Title: Obacunone Promotes Functional Recovery After Spinal Cord Injury by Attenuating Neuroinflammation by Targeting the TLR4/MyD88/p38 MAPK Pathway

    doi: 10.2147/DDDT.S577707

    Figure Lengend Snippet: Oba inhibits the TLR4/MyD88/p38 MAPK signaling pathway in both in vivo and in vitro experiments. ( A – D ) Molecular docking analysis of Oba with TLR4. ( E – H ) Molecular docking analysis of Oba with MyD88. ( I – L ) Molecular docking analysis of Oba with p38. For each protein, the analysis is presented as: an overall docking pose with the binding region outlined by a red dashed box ( A, E, I ); a close-up view of the binding region ( B, F, J ); a surface representation ( C, G, K ); and a two-dimensional interaction diagram ( D, H, L ). ( M ) Representative Western blot image of TLR4, MyD88, p-p38 and p38 protein in BV-2 cells. The plus and minus signs (+, -) denote the presence or absence of the following reagents in culture: LPS, and 50 μM Oba. ( N ) Quantitative analysis of TLR4 and MyD88 protein levels and p38 phosphorylation in BV-2 cells (n = 5). ( O ) Western blot analysis of TLR4, MyD88, p-p38, and p38 in spinal cord tissues from Sham, SCI, and SCI + Oba (20 mg/kg) groups at 3 days post-SCI. ( P ) Quantitative analysis of TLR4 and MyD88 protein levels and p38 phosphorylation in spinal cord tissues (n = 5). The values are presented as mean ± SD. *p<0.05, **p<0.01, ***p<0.001; NS, not significant.

    Article Snippet: To investigate the role of the p38 MAPK pathway in the anti-inflammatory effects of Oba, BV-2 cells were pre-treated for 3 hours with 50 μM Oba, 10 μM SB203580 (a p38 MAPK inhibitor; HY-10256, MCE, China), or a combination of both, prior to stimulation with LPS for 24 hours.

    Techniques: In Vivo, In Vitro, Binding Assay, Western Blot, Phospho-proteomics

    Oba attenuates inflammation by targeting the TLR4/MyD88/p38 MAPK pathway in BV-2 microglial cells. ( A ) Representative Western blot of TLR4 expression in BV-2 cells transfected with a TLR4 overexpression plasmid (pcDNA3.1-TLR4) or an empty vector. The plus and minus signs (+, -) denote the presence or absence of the following reagents in culture: empty plasmid (Oe-NC), and TLR4 overexpression plasmid (Oe-TLR4). ( B ) Quantitative analysis of TLR4 protein levels (n = 5). ( C ) Western blot images of iNOS, TLR4, TNFα and IL-1β protein expression in BV-2 cells. The plus and minus signs (+, -) denote the presence or absence of the following treatments in culture: Oe-NC, Oe-TLR4, LPS, and Oba. ( D – G ) Quantitative analysis of iNOS, TLR4, TNFα and IL-1β protein levels (n = 5). ( H ) Representative Western blot images of iNOS, TNFα, IL-1β, p-p38 and p38 in BV-2 cells. The plus and minus signs (+, -) denote the presence or absence of the following reagents in culture: LPS, Oba, and SB203580. ( I – L ) Quantitative analysis of iNOS, TNFα, IL-1β protein levels and p38 phosphorylation (n = 5). The values are presented as mean ± SD. *p<0.05, **p<0.01, ***p<0.001; NS, not significant.

    Journal: Drug Design, Development and Therapy

    Article Title: Obacunone Promotes Functional Recovery After Spinal Cord Injury by Attenuating Neuroinflammation by Targeting the TLR4/MyD88/p38 MAPK Pathway

    doi: 10.2147/DDDT.S577707

    Figure Lengend Snippet: Oba attenuates inflammation by targeting the TLR4/MyD88/p38 MAPK pathway in BV-2 microglial cells. ( A ) Representative Western blot of TLR4 expression in BV-2 cells transfected with a TLR4 overexpression plasmid (pcDNA3.1-TLR4) or an empty vector. The plus and minus signs (+, -) denote the presence or absence of the following reagents in culture: empty plasmid (Oe-NC), and TLR4 overexpression plasmid (Oe-TLR4). ( B ) Quantitative analysis of TLR4 protein levels (n = 5). ( C ) Western blot images of iNOS, TLR4, TNFα and IL-1β protein expression in BV-2 cells. The plus and minus signs (+, -) denote the presence or absence of the following treatments in culture: Oe-NC, Oe-TLR4, LPS, and Oba. ( D – G ) Quantitative analysis of iNOS, TLR4, TNFα and IL-1β protein levels (n = 5). ( H ) Representative Western blot images of iNOS, TNFα, IL-1β, p-p38 and p38 in BV-2 cells. The plus and minus signs (+, -) denote the presence or absence of the following reagents in culture: LPS, Oba, and SB203580. ( I – L ) Quantitative analysis of iNOS, TNFα, IL-1β protein levels and p38 phosphorylation (n = 5). The values are presented as mean ± SD. *p<0.05, **p<0.01, ***p<0.001; NS, not significant.

    Article Snippet: To investigate the role of the p38 MAPK pathway in the anti-inflammatory effects of Oba, BV-2 cells were pre-treated for 3 hours with 50 μM Oba, 10 μM SB203580 (a p38 MAPK inhibitor; HY-10256, MCE, China), or a combination of both, prior to stimulation with LPS for 24 hours.

    Techniques: Western Blot, Expressing, Transfection, Over Expression, Plasmid Preparation, Phospho-proteomics