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p c jun  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc p c jun
    P C Jun, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 283 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p+jnk2/JNK2+Antibody/10__31083_slash_fbl48168-142-23-24
    Average 95 stars, based on 283 article reviews
    p c jun - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Saline:

    Article Title: Kinase inhibit region of SOCS3 attenuates IL6-induced proliferation and astrocytic differentiation of neural stem cells via cross talk between signaling pathways.
    Article Snippet: The proteins in supernatant were separated by electrophoresis with 10%– 12% sodium dodecyl sulfate polyacrylamide gel (SDS- PAGE) and then transferred onto 0.22 μm polyvinylidene difluoride membranes (PVDF; #IPVH00010, Millipore). .. The membranes were blocked in 5% BSA dissolved in Tris- buffered saline containing 0.1% Tween- 20 for 2 h at room temperature and then were incubated overnight at 4°C with primary antibodies, including GFAP (#ab7260, Abcam, 1:1000), β Tublin III (#MAB1637, Millipore, 1:1000), and STAT3, p- STAT3, P38, p- P38, ERK1/2, p- ERK1/2, AKT, p- AKT, JNK2, p- JNK2(#4904, 9145, 8690, 4511, 4695, 9101, 4685, 4060, 9258, 4668, Cell Signaling, all in 1:1000) and β- actin (#A01263, Boster Biological Technology, 1:20,000). ..

    Article Title: Kinase inhibit region of SOCS3 attenuates IL6 ‐induced proliferation and astrocytic differentiation of neural stem cells via cross talk between signaling pathways
    Article Snippet: The proteins in supernatant were separated by electrophoresis with 10%–12% sodium dodecyl sulfate polyacrylamide gel (SDS‐PAGE) and then transferred onto 0.22 μm polyvinylidene difluoride membranes (PVDF; #IPVH00010, Millipore). .. The membranes were blocked in 5% BSA dissolved in Tris‐buffered saline containing 0.1% Tween‐20 for 2 h at room temperature and then were incubated overnight at 4°C with primary antibodies, including GFAP (#ab7260, Abcam, 1:1000), β Tublin III (#MAB1637, Millipore, 1:1000), and STAT3, p‐STAT3, P38, p‐P38, ERK1/2, p‐ERK1/2, AKT, p‐AKT, JNK2, p‐JNK2(#4904, 9145, 8690, 4511, 4695, 9101, 4685, 4060, 9258, 4668, Cell Signaling, all in 1:1000) and β‐actin (#A01263, Boster Biological Technology, 1:20,000). ..

    Incubation:

    Article Title: Kinase inhibit region of SOCS3 attenuates IL6-induced proliferation and astrocytic differentiation of neural stem cells via cross talk between signaling pathways.
    Article Snippet: The proteins in supernatant were separated by electrophoresis with 10%– 12% sodium dodecyl sulfate polyacrylamide gel (SDS- PAGE) and then transferred onto 0.22 μm polyvinylidene difluoride membranes (PVDF; #IPVH00010, Millipore). .. The membranes were blocked in 5% BSA dissolved in Tris- buffered saline containing 0.1% Tween- 20 for 2 h at room temperature and then were incubated overnight at 4°C with primary antibodies, including GFAP (#ab7260, Abcam, 1:1000), β Tublin III (#MAB1637, Millipore, 1:1000), and STAT3, p- STAT3, P38, p- P38, ERK1/2, p- ERK1/2, AKT, p- AKT, JNK2, p- JNK2(#4904, 9145, 8690, 4511, 4695, 9101, 4685, 4060, 9258, 4668, Cell Signaling, all in 1:1000) and β- actin (#A01263, Boster Biological Technology, 1:20,000). ..

    Article Title: Kinase inhibit region of SOCS3 attenuates IL6 ‐induced proliferation and astrocytic differentiation of neural stem cells via cross talk between signaling pathways
    Article Snippet: The proteins in supernatant were separated by electrophoresis with 10%–12% sodium dodecyl sulfate polyacrylamide gel (SDS‐PAGE) and then transferred onto 0.22 μm polyvinylidene difluoride membranes (PVDF; #IPVH00010, Millipore). .. The membranes were blocked in 5% BSA dissolved in Tris‐buffered saline containing 0.1% Tween‐20 for 2 h at room temperature and then were incubated overnight at 4°C with primary antibodies, including GFAP (#ab7260, Abcam, 1:1000), β Tublin III (#MAB1637, Millipore, 1:1000), and STAT3, p‐STAT3, P38, p‐P38, ERK1/2, p‐ERK1/2, AKT, p‐AKT, JNK2, p‐JNK2(#4904, 9145, 8690, 4511, 4695, 9101, 4685, 4060, 9258, 4668, Cell Signaling, all in 1:1000) and β‐actin (#A01263, Boster Biological Technology, 1:20,000). ..

    Article Title: HIF1α Deficiency in Dendritic Cells Attenuates Symptoms and Inflammatory Indicators of Allergic Rhinitis in a SIRT1-Dependent Manner.
    Article Snippet: Background: Allergic rhinitis is the most prevalent atopic disorder worldwide.. Inflammation is believed to participate in allergic rhinitis.. Previous studies indicate that hypoxia-inducible factor (HIF) promotes the development of allergic rhinitis, and dendritic cells are also involved in allergic rhinitis.

    Blocking Assay:

    Article Title: Polysaccharides from Citrus grandis L. Osbeck suppress inflammation and relieve chronic pharyngitis.
    Article Snippet: Chronic pharyngitis, a common inflammation of the pharyngeal mucosa, is often caused by bacteria, viruses, alcohol abuse, overuse of the voice and cigarettes.. This study aimed to explore the effects of polysaccharides of Citrus grandis L. Osbeck (PCG) in relieving chronic pharyngitis and illustrate the underlying mechanisms.. Polysaccharides were obtained from PCG by column chromatographic extraction.

    Membrane:

    Article Title: Polysaccharides from Citrus grandis L. Osbeck suppress inflammation and relieve chronic pharyngitis.
    Article Snippet: Chronic pharyngitis, a common inflammation of the pharyngeal mucosa, is often caused by bacteria, viruses, alcohol abuse, overuse of the voice and cigarettes.. This study aimed to explore the effects of polysaccharides of Citrus grandis L. Osbeck (PCG) in relieving chronic pharyngitis and illustrate the underlying mechanisms.. Polysaccharides were obtained from PCG by column chromatographic extraction.

    Staining:

    Article Title: SHARPIN overexpression promotes TAK1 expression and activates JNKs and NF-κB pathway in Mycosis Fungoides.
    Article Snippet: Primary cutaneous lymphoma (PCL) is a group of non‐Hodgkin lym‐ phomas including CTCL and cutaneous B‐cell lymphomas (CBCL) which originate from T cell and B cell, respectively.. CTCL accounts for 75% of PCL.. MF is the most common subtype of CTCL account‐ ing for approximately 50% of PCL.



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    Effects of AdipoRon on lipid accumulation, AMPK/PPARα and <t>JNK1</t> signaling pathway in the liver of CORT broilers. (A) Immunoblot of ACC, CPT-1, PPARα and ADPN protein level in the liver of CORT broiler. (B) The change of ACC, CPT-1, PPARα and ADPN protein expression in the liver of CORT broiler. (C) Immunoblot of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein level in the liver of CORT broiler. (D) The change of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein expression in the liver of CORT broiler. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter differ significantly between groups ( p < 0.05, n = 6, biological replicates per group). ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1; TNF-α, Tumor Necrosis Factor-alpha.
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    Fig. 4 H3K18la promotes pyroptosis in primary astrocytes through NOD2/MAPK and NOD2/NF-κB signalling pathways. (A) RT-qPCR and ELISA analysis of IL-1β in UCB-exposed astrocytes with or without NOD2 knockdown. (B) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in UCB- exposed astrocytes with or without NOD2 knockdown. (C) RT-qPCR and ELISA analysis of IL-1β in primary UCB-exposed astrocytes with or without NOD2 overexpression after transfected with si-LDHA. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in primary UCB-exposed astrocytes with or without NOD2 overexpression after LDHA knockdown. (E) Western blot analysis of RIK2, <t>p-p65,</t> p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in UCB-exposed astrocytes after LDHA or NOD2 knockdown. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance
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    Fig. 4 H3K18la promotes pyroptosis in primary astrocytes through NOD2/MAPK and NOD2/NF-κB signalling pathways. (A) RT-qPCR and ELISA analysis of IL-1β in UCB-exposed astrocytes with or without NOD2 knockdown. (B) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in UCB- exposed astrocytes with or without NOD2 knockdown. (C) RT-qPCR and ELISA analysis of IL-1β in primary UCB-exposed astrocytes with or without NOD2 overexpression after transfected with si-LDHA. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in primary UCB-exposed astrocytes with or without NOD2 overexpression after LDHA knockdown. (E) Western blot analysis of RIK2, <t>p-p65,</t> p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in UCB-exposed astrocytes after LDHA or NOD2 knockdown. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance
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    Fig. 4 H3K18la promotes pyroptosis in primary astrocytes through NOD2/MAPK and NOD2/NF-κB signalling pathways. (A) RT-qPCR and ELISA analysis of IL-1β in UCB-exposed astrocytes with or without NOD2 knockdown. (B) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in UCB- exposed astrocytes with or without NOD2 knockdown. (C) RT-qPCR and ELISA analysis of IL-1β in primary UCB-exposed astrocytes with or without NOD2 overexpression after transfected with si-LDHA. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in primary UCB-exposed astrocytes with or without NOD2 overexpression after LDHA knockdown. (E) Western blot analysis of RIK2, <t>p-p65,</t> p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in UCB-exposed astrocytes after LDHA or NOD2 knockdown. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance
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    Image Search Results


    Effects of AdipoRon on lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in the liver of CORT broilers. (A) Immunoblot of ACC, CPT-1, PPARα and ADPN protein level in the liver of CORT broiler. (B) The change of ACC, CPT-1, PPARα and ADPN protein expression in the liver of CORT broiler. (C) Immunoblot of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein level in the liver of CORT broiler. (D) The change of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein expression in the liver of CORT broiler. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter differ significantly between groups ( p < 0.05, n = 6, biological replicates per group). ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1; TNF-α, Tumor Necrosis Factor-alpha.

    Journal: Frontiers in Veterinary Science

    Article Title: Adiponectin receptor agonist reduces broiler hepatic lipid deposition

    doi: 10.3389/fvets.2025.1667501

    Figure Lengend Snippet: Effects of AdipoRon on lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in the liver of CORT broilers. (A) Immunoblot of ACC, CPT-1, PPARα and ADPN protein level in the liver of CORT broiler. (B) The change of ACC, CPT-1, PPARα and ADPN protein expression in the liver of CORT broiler. (C) Immunoblot of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein level in the liver of CORT broiler. (D) The change of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein expression in the liver of CORT broiler. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter differ significantly between groups ( p < 0.05, n = 6, biological replicates per group). ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1; TNF-α, Tumor Necrosis Factor-alpha.

    Article Snippet: The membranes were blocked with a 5% skim milk powder solution at room temperature for 2 h. Subsequently, membranes were incubated with primary antibodies at 4°C for 12 h. After incubation with corresponding secondary antibodies at RT for 1 h. The primary antibodies used in this study included: ADPN (bs-0471R; Bioss, Beijing, China), PPAR α (bs-3614R; Bioss, Beijing, China), TNF-α (bsm-33207 M; Bioss, Beijing, China), p-AMPK (bs-5551R; Bioss, Beijing, China), AMPK (bs-41337R; Bioss, Beijing, China), p-JNK1 (bs-17591R; Bioss, Beijing, China), JNK1 (bs-20760R; Bioss, Beijing, China), and GAPDH (bsm-33033 M; Bioss, Beijing, China) as an internal control.

    Techniques: Western Blot, Expressing, Software, Control

    Effects of AdipoRon on viability, lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in FE-induced LMH cells. (A) The cell viability. (B) The change of oil red O quantification in LMH cells. (C1–3) Liver oil red O staining in LMH cells. Bar = 20 μm. (D) Immunoblot of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1 PPARα, p-JNK1, JNK1 and TNF-α protein level in LMH cells. (E) The change of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1, PPARα, p-JNK1, JNK1 and TNF-α protein expression in LMH cells. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter (a, b, c) differ significantly between groups ( p < 0.05, n = 6 per group, biological replicates). FE, fat emulsion; AdipoRon, adiponectin receptor agonists; ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; TNF-α, tumor necrosis factor-alpha; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1.

    Journal: Frontiers in Veterinary Science

    Article Title: Adiponectin receptor agonist reduces broiler hepatic lipid deposition

    doi: 10.3389/fvets.2025.1667501

    Figure Lengend Snippet: Effects of AdipoRon on viability, lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in FE-induced LMH cells. (A) The cell viability. (B) The change of oil red O quantification in LMH cells. (C1–3) Liver oil red O staining in LMH cells. Bar = 20 μm. (D) Immunoblot of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1 PPARα, p-JNK1, JNK1 and TNF-α protein level in LMH cells. (E) The change of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1, PPARα, p-JNK1, JNK1 and TNF-α protein expression in LMH cells. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter (a, b, c) differ significantly between groups ( p < 0.05, n = 6 per group, biological replicates). FE, fat emulsion; AdipoRon, adiponectin receptor agonists; ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; TNF-α, tumor necrosis factor-alpha; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1.

    Article Snippet: The membranes were blocked with a 5% skim milk powder solution at room temperature for 2 h. Subsequently, membranes were incubated with primary antibodies at 4°C for 12 h. After incubation with corresponding secondary antibodies at RT for 1 h. The primary antibodies used in this study included: ADPN (bs-0471R; Bioss, Beijing, China), PPAR α (bs-3614R; Bioss, Beijing, China), TNF-α (bsm-33207 M; Bioss, Beijing, China), p-AMPK (bs-5551R; Bioss, Beijing, China), AMPK (bs-41337R; Bioss, Beijing, China), p-JNK1 (bs-17591R; Bioss, Beijing, China), JNK1 (bs-20760R; Bioss, Beijing, China), and GAPDH (bsm-33033 M; Bioss, Beijing, China) as an internal control.

    Techniques: Staining, Western Blot, Expressing, Software, Control, Emulsion

    Journal: iScience

    Article Title: Pharmacological inhibition of RAS overcomes FLT3 inhibitor resistance in FLT3-ITD+ AML through AP-1 and RUNX1

    doi: 10.1016/j.isci.2024.109576

    Figure Lengend Snippet:

    Article Snippet: Rabbit anti-p-Jnk1/Jnk2 (T183/Y185) , ThermoFisher , Cat# 700031; RRID: AB_2532273.

    Techniques: Control, Virus, Recombinant, Modification, Saline, Stripping Membranes, Protease Inhibitor, Reverse Transcription, Membrane, Labeling, Gel Extraction, Plasmid Preparation, RNA Library Preparation, Library Quantification, Software

    Fig. 4 H3K18la promotes pyroptosis in primary astrocytes through NOD2/MAPK and NOD2/NF-κB signalling pathways. (A) RT-qPCR and ELISA analysis of IL-1β in UCB-exposed astrocytes with or without NOD2 knockdown. (B) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in UCB- exposed astrocytes with or without NOD2 knockdown. (C) RT-qPCR and ELISA analysis of IL-1β in primary UCB-exposed astrocytes with or without NOD2 overexpression after transfected with si-LDHA. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in primary UCB-exposed astrocytes with or without NOD2 overexpression after LDHA knockdown. (E) Western blot analysis of RIK2, p-p65, p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in UCB-exposed astrocytes after LDHA or NOD2 knockdown. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance

    Journal: Journal of neuroinflammation

    Article Title: H3K18 lactylation-mediated nucleotide-binding oligomerization domain-2 (NOD2) expression promotes bilirubin-induced pyroptosis of astrocytes.

    doi: 10.1186/s12974-025-03399-2

    Figure Lengend Snippet: Fig. 4 H3K18la promotes pyroptosis in primary astrocytes through NOD2/MAPK and NOD2/NF-κB signalling pathways. (A) RT-qPCR and ELISA analysis of IL-1β in UCB-exposed astrocytes with or without NOD2 knockdown. (B) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in UCB- exposed astrocytes with or without NOD2 knockdown. (C) RT-qPCR and ELISA analysis of IL-1β in primary UCB-exposed astrocytes with or without NOD2 overexpression after transfected with si-LDHA. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in primary UCB-exposed astrocytes with or without NOD2 overexpression after LDHA knockdown. (E) Western blot analysis of RIK2, p-p65, p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in UCB-exposed astrocytes after LDHA or NOD2 knockdown. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance

    Article Snippet: The following antibodies were used in this experiment: H3K18la (1:2000, PTM1406RM, PTM BIO, China), the NOD-like receptor family pyrin domain containing 3 (NLRP3) (1:500, NBP2-12446, Novus, USA), Caspase-1 p20 (1:2000, 22915-1-AP, proteintech, China), gasdermin D N-terminal (GSDMD-N) (1:1000, ab219800, Abcam, USA), Histone 3 (1:2000, 9715 S, CST, USA), β-actin (1:5000, A5441, Sigma-Aldrich, USA), receptorinteracting protein kinase 2 (RIK2) (1:2000, 15366-1-AP, proteintech, China), p-p65 (1:2000, 82335-1-RR, proteintech, China), c-Jun-N-terminal-kinase (JNK) (1:1000, R24780, zenbio, China), p-JNK (1:1000, R381100, zenbio, China), p-38 (1:2000, 14064-1-AP, proteintech, China), p-p38 (1:2000, 28796-1-AP, proteintech, China), extracellular signal-regulated kinase 1/2 (ERK) (1:2000, 11257-1- AP, proteintech, China) and p-ERK (1:2000, 28733-1-AP, proteintech, China), α-tublin (1:5000, ER130905, HUABIO, China), NOD2 (1:2000, 54121, SAB, USA).

    Techniques: Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay, Knockdown, Western Blot, Over Expression, Transfection

    Fig. 5 H3K18la/NOD2 signaling axis aggravates pyroptosis in hippocampus of BE rats by upregulating MAPK and NF-κB signaling pathways. (A) Immuno fluorescence co-staining for NOD2 (red) and GFAP (green) in the hippocampal DG region of BE rats after OX intervention. Scale bars: 100 μm. (B) Western blot analysis of NOD2 in the hippocampus of BE rats after OX intervention. (C) RT-qPCR and ELISA analysis of IL-1β in hippocampus tissues of BE rats after GSK717 treatment. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in hippocampus tissues of BE rats after GSK717 treatment. (E) Western blot analysis of RIK2, p-p65, p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in hippocampus tissues of BE rats after OX or GSK717 administration. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance

    Journal: Journal of neuroinflammation

    Article Title: H3K18 lactylation-mediated nucleotide-binding oligomerization domain-2 (NOD2) expression promotes bilirubin-induced pyroptosis of astrocytes.

    doi: 10.1186/s12974-025-03399-2

    Figure Lengend Snippet: Fig. 5 H3K18la/NOD2 signaling axis aggravates pyroptosis in hippocampus of BE rats by upregulating MAPK and NF-κB signaling pathways. (A) Immuno fluorescence co-staining for NOD2 (red) and GFAP (green) in the hippocampal DG region of BE rats after OX intervention. Scale bars: 100 μm. (B) Western blot analysis of NOD2 in the hippocampus of BE rats after OX intervention. (C) RT-qPCR and ELISA analysis of IL-1β in hippocampus tissues of BE rats after GSK717 treatment. (D) Western blot analysis of Caspase-1 p20, GSDMD-N and NLRP3 levels in hippocampus tissues of BE rats after GSK717 treatment. (E) Western blot analysis of RIK2, p-p65, p-JNK, JNK, p-ERK, ERK, p-p38 and p-38 levels in hippocampus tissues of BE rats after OX or GSK717 administration. Data are presented as the mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 and ****P < 0.0001, ns, no significance

    Article Snippet: The following antibodies were used in this experiment: H3K18la (1:2000, PTM1406RM, PTM BIO, China), the NOD-like receptor family pyrin domain containing 3 (NLRP3) (1:500, NBP2-12446, Novus, USA), Caspase-1 p20 (1:2000, 22915-1-AP, proteintech, China), gasdermin D N-terminal (GSDMD-N) (1:1000, ab219800, Abcam, USA), Histone 3 (1:2000, 9715 S, CST, USA), β-actin (1:5000, A5441, Sigma-Aldrich, USA), receptorinteracting protein kinase 2 (RIK2) (1:2000, 15366-1-AP, proteintech, China), p-p65 (1:2000, 82335-1-RR, proteintech, China), c-Jun-N-terminal-kinase (JNK) (1:1000, R24780, zenbio, China), p-JNK (1:1000, R381100, zenbio, China), p-38 (1:2000, 14064-1-AP, proteintech, China), p-p38 (1:2000, 28796-1-AP, proteintech, China), extracellular signal-regulated kinase 1/2 (ERK) (1:2000, 11257-1- AP, proteintech, China) and p-ERK (1:2000, 28733-1-AP, proteintech, China), α-tublin (1:5000, ER130905, HUABIO, China), NOD2 (1:2000, 54121, SAB, USA).

    Techniques: Protein-Protein interactions, Fluorescence, Staining, Western Blot, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay