phospho p38 mapk  (Cell Signaling Technology Inc)

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Article Snippet: Membranes were blocked with 5 % BSA at 37°C for 2 h and incubated overnight at 4°C with the following primary antibodies: ITGAV Rabbit Ab, PLC Rabbit Ab, p-PLC Rabbit Ab, p-p65 Rabbit Ab, and Bcl2 Rabbit Ab were purchased from Bioss (Beijing, China); FAK Rabbit Ab, p-FAK Rabbit Ab, ERK Rabbit Ab, p-ERK Rabbit Ab, JNK Rabbit Ab, p-JNK Rabbit Ab, p38 MAPK Rabbit Ab, p-p38 MAPK Rabbit Ab, PI3K Rabbit Ab, p-PI3K Rabbit Ab, AKT Rabbit Ab, p-AKT Rabbit Ab, PKC Rabbit Ab, p-PKC Rabbit Ab, Bax Rabbit Ab, and Caspase 3 Rabbit Ab were purchased from Abmart (Shanghai, China); p65 Rabbit Ab (Proteintech, Wuhan, China).

Techniques: Expressing

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Article Snippet: Membranes were blocked with 5 % BSA at 37°C for 2 h and incubated overnight at 4°C with the following primary antibodies: ITGAV Rabbit Ab, PLC Rabbit Ab, p-PLC Rabbit Ab, p-p65 Rabbit Ab, and Bcl2 Rabbit Ab were purchased from Bioss (Beijing, China); FAK Rabbit Ab, p-FAK Rabbit Ab, ERK Rabbit Ab, p-ERK Rabbit Ab, JNK Rabbit Ab, p-JNK Rabbit Ab, p38 MAPK Rabbit Ab, p-p38 MAPK Rabbit Ab, PI3K Rabbit Ab, p-PI3K Rabbit Ab, AKT Rabbit Ab, p-AKT Rabbit Ab, PKC Rabbit Ab, p-PKC Rabbit Ab, Bax Rabbit Ab, and Caspase 3 Rabbit Ab were purchased from Abmart (Shanghai, China); p65 Rabbit Ab (Proteintech, Wuhan, China).

Techniques: Activity Assay

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Article Snippet: p-p38 MAPK Rabbit Ab , Abmart , TA4001 , 1: 1500.

Techniques: Expressing

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Article Snippet: p-p38 MAPK Rabbit Ab , Abmart , TA4001 , 1: 1500.

Techniques: Activity Assay

Journal: Genes & Diseases

Article Title: Network pharmacology reveals that Yanghe Decoction inhibits osteosarcoma progression via ROS-induced mitochondrial dysfunction and enhances cisplatin sensitivity

doi: 10.1016/j.gendis.2025.101862

Figure Lengend Snippet: YHD exerts anti-tumor effects on osteosarcoma (OS) cells through the PI3K/AKT and p38 signaling pathways. (A) Principal component analysis revealed a clear distinction in gene expression profiles between the control and YHD groups. (B) Volcano plot identified 3495 differentially expressed genes in the YHD group. (C) Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses. (D – G) Gene Set Enrichment Analysis (GSEA) of control and YHD groups. (H, I) Western blot analysis detected the effect of YHD on proteins related to the PI3K/AKT and MAPK pathways in OS cells. (J, K) After the addition of a PI3K activator and a P38 inhibitor, scratch healing assay showed that YHD inhibited the migration of OS cells. (L, M) After the addition of a PI3K activator and a P38 inhibitor, JC-1 staining detected the effect of YHD on the mitochondrial membrane potential in OS cells. Data were presented as mean ± standard deviation ( n = 3). ∗ p < 0.05 and ∗∗ p < 0.01 versus the blank group.

Article Snippet: Cyclin B (#4138), Vimentin (#5741), N-cadherin (#13116), p38 (#9212), and p-p38 (#4511S) antibodies were purchased from Cell Signaling Technology (USA).

Techniques: Protein-Protein interactions, Gene Expression, Control, Western Blot, Migration, Staining, Membrane, Standard Deviation

Journal: Genes & Diseases

Article Title: Network pharmacology reveals that Yanghe Decoction inhibits osteosarcoma progression via ROS-induced mitochondrial dysfunction and enhances cisplatin sensitivity

doi: 10.1016/j.gendis.2025.101862

Figure Lengend Snippet: YHD inhibits the growth of OS in vivo . (A) The effect of YHD on tumorigenesis in nude mice. (B) The effect of YHD on tumor volume. (C) The effect of YHD on mouse weight. (D) Hematoxylin-eosin staining of the mouse tumor tissue. (E) Hematoxylin-eosin staining of the mouse lung tissue. (F) PCNA, Bcl-2, Vimentin, p-AKT, and p-P38 of the mouse tumor tissue were detected by immunohistochemistry. (G) Hematoxylin-eosin staining of the mouse heart and liver tissue. Data were presented as mean ± standard deviation ( n = 6).

Article Snippet: Cyclin B (#4138), Vimentin (#5741), N-cadherin (#13116), p38 (#9212), and p-p38 (#4511S) antibodies were purchased from Cell Signaling Technology (USA).

Techniques: In Vivo, Staining, Immunohistochemistry, Standard Deviation

Journal: iScience

Article Title: Metabolic orchestration of NOD1 signaling by AMPK-mediated phosphorylation of ZDHHC5

doi: 10.1016/j.isci.2026.115245

Figure Lengend Snippet: Cellular energy stress suppresses PGN-induced NOD1 signaling (A) Mouse BMDM cells were treated with or without glucose for 6 h, then stimulated with C12-iE-DAP (1 μg/mL) for 30 min, p65 and p38 phosphorylation were analyzed by immunoblotting. (B) Mouse BMDM cells were treated with 2-DG (25 mM) in glucose-free medium for 6 h, then stimulated with C12-iE-DAP (1 μg/mL) for 30 min, p65 and p38 phosphorylation were analyzed by immunoblotting. (C) Mouse BMDM cells were treated with metformin (2 mM) for 6 h, then stimulated with C12-iE-DAP (1 μg/mL) for 30 min, p65 and p38 phosphorylation were analyzed by immunoblotting. (D) Mouse iBMDM cells were treated with or without glucose and stimulated with C12-iE-DAP (5 μg/mL) for 7 h. The IL-6 release in the medium was measured with ELISA. For each experimental group, three supernatant samples were analyzed. ∗∗ p < 0.01, NS, p > 0.05. mean ± s.d., Student’s t test. (E) Mouse iBMDM cells were treated with 2-DG (25 mM) in glucose-free medium and stimulated with C12-iE-DAP (5 μg/mL) for 7 h. The IL-6 release in the medium was measured with ELISA. For each experimental group, three supernatant samples were analyzed. ∗∗ p < 0.01, NS, p > 0.05. mean ± s.d., Student’s t test. (F) Mouse iBMDM cells were pre-treated with DMSO or Compound C (5 μM) and treated with or without glucose for 6 h, then stimulated with C12-iE-DAP (1 μg/mL) for 30 min, p65 and p38 kinase phosphorylation were analyzed by immunoblotting. (G) Mouse iBMDM cells were pre-treated with DMSO or Compound C (5 μM) and then treated with or without glucose and stimulated with C12-iE-DAP (5 μg/mL) for 7 h. The IL-6 release in the medium was measured with ELISA. For each experimental group, three supernatant samples were analyzed. ∗∗ p < 0.01, NS, p > 0.05. mean ± s.d., Student’s t test. (H) Mouse iBMDM cells were treated with MK-8722 (2 μM) for 8 h, then stimulated with C12-iE-DAP (1 μg/mL) for 30 min, p65 and p38 phosphorylation were analyzed by immunoblotting. (I) HEK293T cells were treated with or without glucose for 6 h. Representative fluorescence images show the localization of GFP-NOD1 were presented. Scale bar = 10 μm for all images. (J) HEK-293T cells expressing FLAG-NOD1 were treated with or without glucose for 6h. Total, cytosolic, and membrane fractions were immunoblotted with the indicated antibodies. (K) HEK293T cells were pre-treated with DMSO or Compound C (5 μM) and then treated with glucose starvation for 6h. Representative fluorescence images show the localization of GFP-NOD1 were presented. Scale bar = 10 μm for all images. (L) HEK-293T cells expressing FLAG-NOD1 were pre-treated with DMSO or Compound C (5 μM) and treated with or without glucose for 6h. Total, cytosolic, and membrane fractions were immunoblotted with the indicated antibodies.

Article Snippet: Rabbit-Anti-Phospho-p38 MAPK (Thr180/Tyr182) , Cell Signaling Technology , Cat# 4511; RRID: AB_2139682.

Techniques: Phospho-proteomics, Western Blot, Enzyme-linked Immunosorbent Assay, Fluorescence, Expressing, Membrane

Journal: iScience

Article Title: Metabolic orchestration of NOD1 signaling by AMPK-mediated phosphorylation of ZDHHC5

doi: 10.1016/j.isci.2026.115245

Figure Lengend Snippet: AMPK-mediated ZDHHC5 phosphorylation inhibits NOD1 activation (A) ZDHHC5-knockout HEK293T cells reconstituted with ZDHHC5 wild-type (WT) or 2A mutant were transfected to express FLAG-NOD1, then treated with metformin (5 mM) and labeled with alk-C16 for 6 h. NOD1 palmitoylation was detected by click chemistry reaction. (B) ZDHHC5-knockout HEK293T cells reconstituted with ZDHHC5 wild-type (WT) or 2A mutant were treated with metformin (5 mM) for 6 h. Representative fluorescence images show the localization of GFP-NOD1 were presented. Scale bar = 10 μm for all images. (C) ZDHHC5-knockout HEK293T cells reconstituted with ZDHHC5 wild-type (WT) or 2A mutant were treated with or without glucose for 6 h. Representative fluorescence images show the localization of GFP-NOD1 were presented. Scale bar = 10 μm for all images. (D) ZDHHC5-knockout HEK293T cells reconstituted with ZDHHC5 wild-type (WT) or 2A mutant were transfected to express FLAG-NOD1, and treated with metformin (5 mM) for 6 h. Total, cytosolic, and membrane fractions were immunoblotted with the indicated antibodies. (E) BMDMs were generated from Zdhhc5 −/− mice, and were reconstituted with ZDHHC5 wild-type (WT) or 2A mutant using lentiviral transduction. The reconstituted BMDM cells were treated with metformin (2 mM) for 6 h, followed by stimulation with C12-iE-DAP (1 μg/mL) for 30 min. p65 and p38 kinase phosphorylation were analyzed by immunoblotting. (F) ZDHHC5-knockdown iBMDMs were reconstituted with ZDHHC5 wild-type (WT) or 2A mutant using lentiviral transduction. The reconstituted iBMDM cells were treated with metformin (2 mM) for 6 h, followed by stimulation with C12-iE-DAP (1 μg/mL) for 30 min, p65 and p38 kinase phosphorylation were analyzed by immunoblotting. (G) ZDHHC5-knockdown iBMDMs were reconstituted with ZDHHC5 wild-type (WT) or 2A mutant using lentiviral transduction. The reconstituted iBMDMs cells were treated with or without glucose and stimulated with C12-iE-DAP (5 μg/mL) for 7 h. The IL-6 release in the medium was measured with ELISA. For each experimental group, three supernatant samples were analyzed. ∗∗ p < 0.01, NS, p > 0.05. mean ± s.d., Student’s t test.

Article Snippet: Rabbit-Anti-Phospho-p38 MAPK (Thr180/Tyr182) , Cell Signaling Technology , Cat# 4511; RRID: AB_2139682.

Techniques: Phospho-proteomics, Activation Assay, Knock-Out, Mutagenesis, Transfection, Labeling, Fluorescence, Membrane, Generated, Transduction, Western Blot, Knockdown, Enzyme-linked Immunosorbent Assay