Journal: Cell Death & Disease

Article Title: CXCR4 uses STAT3-mediated slug expression to maintain radioresistance of non-small cell lung cancer cells: emerges as a potential prognostic biomarker for lung cancer

doi: 10.1038/s41419-020-03280-5

Figure Lengend Snippet: A Western blot analysis of phopho-STAT3 (Y705 and S727) in NSCLC cells (A549, H460, and A549/GR) transfected with the vectors described in the Figure. B Western blot (WB, upper) and RT-PCR (lower) analysis (left) and IR clonogenic survival assay (right) of A549/GR cells transfected with control siRNA (siCon) or siRNA against STAT3 (siSTAT3-1 and 3-2). C , G γ-H2AX foci assay of A549/GR (C) and A549/CXCR4 (upper) and H460/CXCR4 (lower) ( G ) cells. Cells were exposed to IR (6 Gy) and fixed at the indicated time points in the Figure. Representative ICC images of γ-H2AX (left) and quantification of the results (right). * P < 0.05, ** P < 0.01, *** P < 0.005. White bar: 20 μm. D , H Western blot analysis of A549/GR ( D ) and A549/CXCR4 (left) and H460/CXCR4 (right) ( H ). Cells exposed to IR (6 Gy) at the indicated time points transfected with control siRNA (siCon) or siRNA against Stat3 (siSTAT3-1). E , F Western bot analysis of p-STAT3 (S727 and Y705) (left) and IR clonogenic survival assay (right) in A549 ( E ) and H460 ( F ) cells transfected with control siRNA (siCon) or siRNA against STAT3 (siSTAT3-1 and siSTAT3-3).

Article Snippet: Antibody such as p-STAT3 (S727) and β-actin were purchased from Santa Cruz Biotechnology (Santa Cruz, CA). p-STAT3 (Y705) and Slug were obtained from Cell Signaling Biotechnology (Denvers, MA).

Techniques: Western Blot, Transfection, Reverse Transcription Polymerase Chain Reaction, Clonogenic Cell Survival Assay, Control

Journal: Cellular and Molecular Immunology

Article Title: A novel cytokine consisting of the p40 and EBI3 subunits suppresses experimental autoimmune arthritis via reciprocal regulation of Th17 and Treg cells

doi: 10.1038/s41423-021-00798-2

Figure Lengend Snippet: The p40-EBI3-Fc protein suppressed Th17 cells via regulation of IL-12Rb1 and gp130 receptor signaling. A Splenocytes from C57BL/6 mice were cultured with 10 ng/mL IL-6 in the presence or absence of the p40-EBI3-Fc protein (1 or 10 μg/mL). After 1 h, protein was isolated from the cultured cells. p -STAT3 Tyr705, STAT3, p -STAT5, STAT5, and GAPDH were analyzed by western blotting. Representative western blots from one of three independent experiments are shown (bottom panel); the results are depicted as the mean ± SD of three independent experiments per group (right). B Splenocytes isolated from C57BL/6 mice were stimulated with IL-6 in the presence or absence of the p40-EBI3-Fc protein (1 or 10 μg/mL) for 15 min. CD4 + T cells expressing pSTAT3 Tyr705, pSTAT3 Ser727, or pSTAT5 were then analyzed by flow cytometry. C A IL-12Rβ1 and gp130 overexpression vector was transfected into the Ba/F3 cell line using a P4 Primary cell 4D-nucleofector TM X kit. The proliferation of Ba/F3 cells was determined with a [ 3 H] thymidine incorporation assay under p40-EBI3-Fc (0.01–1 μg/mL) treatment. D IL-12Rβ1- and gp130-expressing Ba/F3 cells were stimulated with p40-EBI3-Fc for 1 h. p -STAT5, STAT5, and GAPDH in the cell lysates were analyzed using western blotting. Representative western blots from one of three independent experiments are shown; the results represent the mean ± SD of three independent experiments per group (right). E , F Alterations in IL-17 production in anti-CD3-stimulated murine splenic CD4 + T cells induced by p40-EBI3-Fc treatment and transfection with IL-12Rβ1-, gp130-, or WSX1-siRNA. Th17 cell expression was determined by FACS, and IL-17 expression was evaluated by ELISA. Bars show the mean ± SD of three independent experiments per group (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: The permeabilized cells were stained with anti-p-STAT3 Y705-PE, anti-p-STAT3-S727-PE, or anti-p-STAT5-PE (BD Pharmingen) and subjected to flow cytometric analysis (CytoFLEX; Beckman Coulter, Fullerton, CA, USA).

Techniques: Cell Culture, Isolation, Western Blot, Expressing, Flow Cytometry, Over Expression, Plasmid Preparation, Transfection, Thymidine Incorporation Assay, Enzyme-linked Immunosorbent Assay

Journal: Nature Communications

Article Title: Blockade of glucagon receptor induces α-cell hypersecretion by hyperaminoacidemia in mice

doi: 10.1038/s41467-025-57786-7

Figure Lengend Snippet: a Venn diagrams showing transcription factors that can bind to the VGF promoter, as identified in the animalTFDB3.0, GTRD and TFBIND databases. b Amino acids increased VGF promoter luciferase activity in αTC1-6 cells incubated with 4 mM glutamine and alanine for 72 h ( n = 6). c Screening for transcription factors involved in amino acid-induced VGF promoter activity. αTC1-6 cells were transfected with indicated siRNA and incubated with amino acids for 72 h. Data were generated from 3 independent experiments. d Western blot analysis of p-STAT3-S727, p-STAT3-Y705 and total STAT3 protein levels in αTC1-6 cells incubated amino acids for 72 h. e Quantification of relevant protein levels in ( d ). Data were generated from 3 independent experiments. f Representative confocal images of p-STAT3-S727 expression in the pancreatic sections from WT or GCGR-KO mice. Scale bar indicates 50 μm. g Western blot analysis of p-STAT3-S727, STAT3, VGF and pro-glucagon protein levels in αTC1-6 cells treated with S3I-201 (STAT3 inhibitor). h Quantification of relevant protein levels in ( g ). Data were generated from 3 independent experiments. i . Representative confocal microscopy images of VGF and glucagon expression in αTC1-6 cells treated with amino acids alone or plus S3I-201 for 72 h. Scale bar, 10 μm. j VGF promoter activity in αTC1-6 cells transfected with empty vector, wild-type STAT3 or constitutively active STAT3 mutant (STAT3-S727D) for 72 h. Data were generated from 3 independent experiments. k Diagram of STAT3 binding sites at VGF promoter. l Chip-qPCR analysis of STAT3 binding activity at VGF promoter. Data were generated from 3 independent experiments. m Western blot analysis of protein levels after treatment with amino acids or amino acids plus rapamycin in αTC1−6 cells for 72 h. n Quantification of relevant protein levels in ( m ). Data were generated from 3 independent experiments. Data presented in ( b , c , e , h , j , l , n ) are mean ± SEM. Data in ( b , e , l ) were analyzed using two-tailed unpaired t-tests. Data in ( c , h , j , n ) were analyzed by one-way ANOVA with Bonferroni’s post hoc test. p -values < 0.05 are displayed. Source data are provided as a Source Data file.

Article Snippet: The remaining supernatant was immunoprecipitated with p-STAT3-S727 antibodies (CST, 9198).

Techniques: Luciferase, Activity Assay, Incubation, Transfection, Generated, Western Blot, Expressing, Confocal Microscopy, Plasmid Preparation, Mutagenesis, Binding Assay, ChIP-qPCR, Two Tailed Test

Journal: Nature Communications

Article Title: Blockade of glucagon receptor induces α-cell hypersecretion by hyperaminoacidemia in mice

doi: 10.1038/s41467-025-57786-7

Figure Lengend Snippet: a Upon glucagon receptor blockade, the organism increases its demand for glucagon. Several factors (particularly elevated amino acids), arise from the GCGR-deficient liver and act on pancreatic islets, leading to α cell hyperplasia and enhanced α cell secretion. All these changes collectively contribute to hyperglucagonemia. b Increased circulating amino acids (especially glutamine and alanine) activate the mTOR-STAT3 and ERK-CREB signaling pathways. STAT3 enhances VGF transcription, while CREB promotes both VGF and GCG expression. Consequently, glucagon granule biogenesis and glucagon secretion are significantly increased. Conversely, blocking amino acid-induced VGF expression by inhibiting mTOR or STAT3 activation reduces levels of the glucagon granule component VGF, thereby decreasing glucagon granule biogenesis and glucagon secretion.

Article Snippet: The remaining supernatant was immunoprecipitated with p-STAT3-S727 antibodies (CST, 9198).

Techniques: Protein-Protein interactions, Expressing, Blocking Assay, Activation Assay

Journal: The FASEB Journal

Article Title: Inhibition of Janus kinase signaling during controlled mechanical ventilation prevents ventilation-induced diaphragm dysfunction

doi: 10.1096/fj.13-244210

Figure Lengend Snippet: CMV results in activated phosphorylation of STAT3 on Tyr705 and diaphragm contractile dysfunction. Diaphragms from mechanically ventilated (MV) rats and unfed controls were analyzed. A ) Ex vivo force–frequency relationship from mechanically ventilated ( n =13) rats and unfed controls ( n =7). B ) Western blots for total STAT3 and phospho-STAT3 Y705 from a representative set of mechanically ventilated rats and unfed controls (1, 3, 6, and 9 h, n =5–6 rats/group; 18 h, n =6–8). C ) Messenger RNA levels of the STAT3 downstream target genes SOCS3 and Myf5 from mechanically ventilated ( n =9) rats and unfed controls ( n =10). Mechanical ventilation period of 18 h. Results are means ± sem . * P < 0.05; Student's t test.

Article Snippet: Proteins electroblotted onto PVDF membranes were incubated with the following primary antibodies and the appropriate secondary antibodies: phospho-STAT3 [9131; Tyr705; Cell Signaling Technology (CST), Danvers, MA, USA], STAT3 (9132; CST), pSTAT3-S727 (NB2-12965; Novus Biologicals, Littleton, CO, USA), phospho-p38 (9215; Thr180/Tyr182; CST), myogenin (ab124800; Abcam, Cambridge, MA, USA), Ac-Histone H3 (9649; CST), tubulin (5346; CST), GRIM-19 [sc-136431; Santa Cruz Biotechnology (SCB), Dallas, TX, USA], 4-hydroxynonenal (4-HNE; ab46545; Abcam), lactate dehydrogenase A (LDHA; 2012S; CST), proliferating cell nuclear antigen (PCNA; sc-56; SCB), voltage-dependent anion channel (VDAC; 4661; CST), cytochrome c (4272; CST), caspase-3 (9664; CST), calpain 1 (2556; CST), and α-spectrin (sc-48382; SCB).

Techniques: Phospho-proteomics, Ex Vivo, Western Blot

Journal: The FASEB Journal

Article Title: Inhibition of Janus kinase signaling during controlled mechanical ventilation prevents ventilation-induced diaphragm dysfunction

doi: 10.1096/fj.13-244210

Figure Lengend Snippet: CMV increases Ser705 phosphorylation and mitochondrial accumulation of phospho-STAT3 (Ser727 and/or Tyr705/Ser727) within diaphragm muscle. A ) Diaphragms from unfed control rats ( n =8), MV-R548 rats ( n =9), or MV-Veh rats ( n =9) were analyzed by Western blot of total muscle lysate (representative animals depicted in blot) and quantitation. Correlation between increases in phospho-STAT3 S727 and phospho-STAT3 Y705 were determined. B ) Purified mitochondrial fractions (mito) and total lysates (total) were subjected to Western blot analysis for pSTAT3 S727 , pSTAT3 Y705 , total STAT3, GRIM-19, VDAC (mitochondrial marker), LDHA (cytoplasmic marker) and PCNA (nuclear marker). Unfed (U) controls, n = 10; MV-Veh (MV), n = 6; MV-R548, n = 7. Results are means ± sem . Mechanical ventilation period of 18 h. P values calculated by 1-way ANOVA with Tukey's post hoc analysis.

Article Snippet: Proteins electroblotted onto PVDF membranes were incubated with the following primary antibodies and the appropriate secondary antibodies: phospho-STAT3 [9131; Tyr705; Cell Signaling Technology (CST), Danvers, MA, USA], STAT3 (9132; CST), pSTAT3-S727 (NB2-12965; Novus Biologicals, Littleton, CO, USA), phospho-p38 (9215; Thr180/Tyr182; CST), myogenin (ab124800; Abcam, Cambridge, MA, USA), Ac-Histone H3 (9649; CST), tubulin (5346; CST), GRIM-19 [sc-136431; Santa Cruz Biotechnology (SCB), Dallas, TX, USA], 4-hydroxynonenal (4-HNE; ab46545; Abcam), lactate dehydrogenase A (LDHA; 2012S; CST), proliferating cell nuclear antigen (PCNA; sc-56; SCB), voltage-dependent anion channel (VDAC; 4661; CST), cytochrome c (4272; CST), caspase-3 (9664; CST), calpain 1 (2556; CST), and α-spectrin (sc-48382; SCB).

Techniques: Phospho-proteomics, Control, Western Blot, Quantitation Assay, Purification, Marker

Journal: The FASEB Journal

Article Title: Inhibition of Janus kinase signaling during controlled mechanical ventilation prevents ventilation-induced diaphragm dysfunction

doi: 10.1096/fj.13-244210

Figure Lengend Snippet: Proposed model for role of JAK signaling in VIDD. JAK signaling is activated by CMV and functions as a critical triggering mechanism upstream of STAT3 phosphorylation (Tyr705 and Ser705), mitochondrial dysfunction, ROS production, atrophy, and muscle weakness. Mechanical ventilation results in the mitochondrial accumulation of phospho-STAT3 (singly phosphorylated on Ser727 or doubly phosphorylated at both Ser727 and Tyr705). Import into mitochondria is facilitated through interaction of phospho-STAT3 with GRIM-19, a component of complex I of the ETC, and may directly affect mitochondrial function and ROS generation. Induction of various myogenic transcription factors and muscle-specific E3 ubiquitin ligases (MURF-1 and atrogin-1) and activation of calpain, caspase 9, and caspase 3 can contribute to muscle atrophy and proteolytic cleavage of myofilament proteins. Mitochondrial dysfunction may also lead to ROS-mediated modification of myofilament proteins in a manner that negatively affects contractile function.

Article Snippet: Proteins electroblotted onto PVDF membranes were incubated with the following primary antibodies and the appropriate secondary antibodies: phospho-STAT3 [9131; Tyr705; Cell Signaling Technology (CST), Danvers, MA, USA], STAT3 (9132; CST), pSTAT3-S727 (NB2-12965; Novus Biologicals, Littleton, CO, USA), phospho-p38 (9215; Thr180/Tyr182; CST), myogenin (ab124800; Abcam, Cambridge, MA, USA), Ac-Histone H3 (9649; CST), tubulin (5346; CST), GRIM-19 [sc-136431; Santa Cruz Biotechnology (SCB), Dallas, TX, USA], 4-hydroxynonenal (4-HNE; ab46545; Abcam), lactate dehydrogenase A (LDHA; 2012S; CST), proliferating cell nuclear antigen (PCNA; sc-56; SCB), voltage-dependent anion channel (VDAC; 4661; CST), cytochrome c (4272; CST), caspase-3 (9664; CST), calpain 1 (2556; CST), and α-spectrin (sc-48382; SCB).

Techniques: Phospho-proteomics, Ubiquitin Proteomics, Activation Assay, Modification

Journal: Clinical Cancer Research

Article Title: Reciprocal Regulation of c-Src and STAT3 in Non-Small Cell Lung Cancer

doi: 10.1158/1078-0432.ccr-09-0767

Figure Lengend Snippet: Fig. 4. Phosphorylated c-Src, STAT3, and downstream Src targets were measured in paired normal lung and NSCLC tumor tissues from patients who had previously undergone resection. A, tumors had higher mean c-Src activity, as indicated by decreased levels of inactive c-Src (pSrc Y527). Conversely, mean activated STAT3 (pSTAT3 Y705) was lower in tumor tissue than in normal lung. B, levels of inactive c-Src (pSrc Y527) correlated directly with activated STAT3 (pSTAT3 Y705) when analyzed as total levels of phosphorylated protein or ratio of phosphorylated protein to total protein. C, levels of phosphorylated FAK, p130Cas, and paxillin were inversely correlated with pSTAT3 Y705.

Article Snippet: Antibodies used in the Western blot analysis included c-Src and pSTAT3 S727 (Santa Cruz Biotechnology); pSrc Y419, pSTAT3 Y705, STAT3, pFAK Y861, Lyn, Yes, Bcl-XL, survivin, and STAT5 (Cell Signaling Technology); and β-actin (Sigma Chemical Company).

Techniques: Activity Assay

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: STAT3 pathway activation and intrinsic radioresistance of human malignant glioma cell lines. Densitometric analyses of the blots are presented as relative ratio of phosphoprotein/total protein. Data are presented as mean values ± standard error of triplicate determinations (arbitrary units). Abbreviation: SF2 = surviving fraction at 2 Gy; ND = not determined

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Activation Assay, Western Blot

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: Gö6976 radiosensitizes pSTAT3‐Y705‐negative human glioblastoma cells. A–F. Cells were seeded at a density of 5000 per well of 96‐well plates. 6 h later, Gö6976 was added to growth medium. Single 4‐Gy dose irradiation was performed at 24‐h time course incubation with Gö6976. After 90 h of cell growth in Gö6976, cell number was estimated by MTT assay. Results represent mean values ± SEM of relative cell normalized to untreated cells (n = 5, *P < 0.05, Mann–Whitney test). G–I. SF763, SF767 or U118MG cells were incubated 60 h in different concentrations of Gö6976 and PE was determined 10 days after seeding. J–L. For clonogenic survival assay, SF763 and U118MG cells were treated with 1000 nM of Gö6976 and 200 nM for SF767. After 72 h of incubation, cells were irradiated and the surviving fraction was compared with that of control. Data are fitted to linear‐quadratic model. They were represented by their mean ± SEM of values of three independent experiments, each condition performed in triplicate (random‐effects model). Y705‐ : pSTAT3‐Y705 negative.

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Irradiation, Incubation, MTT Assay, MANN-WHITNEY, Clonogenic Cell Survival Assay

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: STAT3 activation in glioblastoma clinical samples. Percentage of stained tumor cells and staining intensity is presented for pSTAT3 ‐ Y705 and pSTAT3 ‐ S727 . Negative = no staining; positive + = weak staining; positive ++ = moderate staining; positive +++ = strong staining

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Activation Assay, Staining

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: Gö6976 down‐modulates pSTAT3‐S727 only in pSTAT3‐Y705‐negative human glioblastoma cells. Cells were grown 72 h in indicated concentration of Gö6976 or DMSO (control) before harvest. Thirty micrograms of total proteins were loaded per lane and electrophoresed by SDS‐PAGE. Transfer membranes were immunoblotted with anti‐STAT3, anti‐pSTAT3‐Y705 and anti‐pSTAT3‐S727 specific antibodies. To ensure equal protein loading, β‐actin was used as control.

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Concentration Assay, SDS Page

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: Subcellular distribution of phosphorylated STAT3 in human glioblastoma cell lines treated by Gö6976. Cells were treated with Gö6976 or DMSO (control) and fixed at 24‐ and 72‐h incubation with Gö6976, respectively, for pSTAT3‐Y705 and pSTAT3‐S727 detection. Anti‐pSTAT3‐Y705 and anti‐pSTAT3‐S727 antibodies were used. DAPI and Cy3‐conjugated secondary goat anti‐rabbit antibody were used. Histograms represent the mean observed intensity of fluorescence in each condition (scale bars are equal to 20 μm, 40×/1.15).

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Incubation, Fluorescence

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: Gö6976 effects after irradiation. Cells were grown 72 h in growth medium with indicated concentration of Gö6976 or DMSO (control) prior to 4‐Gy irradiation. Cells were then harvested 24 h later. Thirty micrograms of total proteins were loaded per lane and electrophoresed by SDS‐PAGE. Transfer membranes were immunoblotted with anti‐STAT3, anti‐pSTAT3‐Y705 and anti‐pSTAT3‐S727 specific antibodies. To ensure equal protein loading, β‐actin was used as control.

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Irradiation, Concentration Assay, SDS Page

Journal: Brain Pathology

Article Title: STAT3 Serine 727 Phosphorylation: A Relevant Target to Radiosensitize Human Glioblastoma

doi: 10.1111/bpa.12254

Figure Lengend Snippet: STAT3 activation in glioblastoma clinical samples. Immunostaining of pSTAT3 was performed on paraffin‐embedded sections. A. Negative pSTAT3‐Y705 stained section (×40). B,C. Positive pSTAT3‐Y705 staining of GBM and vascular endothelial cells (×20). D. Heterogeneous pSTAT3‐Y705 staining of endothelial cells (×40). E. pSTAT3‐S727 staining of a transitional zone in a tumor periphery, displaying positively stained GBM cells and unstained non‐neoplastic glial cells (×20). F. pSTAT3‐S727 staining of GBM cells (×20). G. pSTAT3‐S727 staining of vascular endothelial cells (×40). H. pSTAT3‐S727 staining in case of capillary endothelial cell proliferation (×40).

Article Snippet: Antibodies For Western blot, immunofluorescence and immunohistochemistry, anti‐pSTAT3‐Y705 monoclonal antibody (mAb, No 9145) was purchased from Ozyme (Saint‐Quentin‐en‐Yvelines, France) and anti‐pSTAT3‐S727 mAb (No 1121‐1) from Euromedex (Souffelweyersheim, France).

Techniques: Activation Assay, Immunostaining, Staining

Journal: Journal of Inflammation Research

Article Title: Anti-Inflammatory Regulatory Role of Signal Transducer and Activator of Transcription 3 Phosphorylation in Regulating Hypersensitivity Responses to Echinococcus granulosus Hydatid Cyst Fluid

doi: 10.2147/JIR.S509286

Figure Lengend Snippet: The inhibitory effect of different concentrations of inhibitors on STAT3 phosphorylation.

Article Snippet: The STAT3 inhibitors Stattic and JSI-124 were procured from Shanghai Haoyuan Chemexpress Co., Ltd. Antibodies for STAT3, phosphorylated p-STAT3 (S727), p-STAT3 (Y705), and ACTIN, as well as secondary antibodies, were purchased from Wuhan ABclonal Biotechnology Co., Ltd. High-resolution rapid electrophoresis liquid and ice-free rapid transfer liquid were obtained from Wuhan Servicebio Technology Co., Ltd. Immunoglobulin E (IgE) was purchased from Sigma-Aldrich, USA.

Techniques: Phospho-proteomics