Journal: Frontiers in Immunology

Article Title: The CXCR4–STAT3–IL-10 Pathway Controls the Immunoregulatory Function of Chronic Lymphocytic Leukemia and Is Modulated by Lenalidomide

doi: 10.3389/fimmu.2017.01773

Figure Lengend Snippet: CXC chemokine ligand 12 (CXCL12)–CXCR4 interaction induces phosphorylation of S727-STAT3 and IL-10 production by chronic lymphocytic leukemia (CLL) cells. (A) CXCL12 phosphorylates S727-STAT3 in CLL cells through interaction with the CXCR4 receptor. CLL cells were stimulated with 250 ng/ml CXCL12 for 20 min, fixed, permeabilized, and stained for p-S727-STAT3. Exposure to 0.05 µM/ml of the STAT3 inhibitor cucurbitacin for 2 h or CXCR4 blocking antibody, prevented the CXCL12-induced S727-STAT3 phosphorylation ( n = 19). (B,C) Cytoplasmic IL-10 expression by CLL cells after CXCL12 stimulation. CLL cells were cultured for 8–10 h with either 250 ng/ml CXC12 or 4 µg/ml CpG (positive control), followed by addition of Phorbol myristate acetate (PMA), ionomycin, and BFA (PIB), and then incubated for another 6 h before performing intracellular staining. CXCL12 induced an increase in IL-10+ CLL cells, both in frequencies (B) and in absolute counts (C) .

Article Snippet: After one wash and 20 min of surface staining with CD19-APC (BD Biosciences) and CD5-FITC (BioLegend) antibodies, the cells were washed, permeabilized (Phospho-Epitopes Exposure kit-Beckman Coulter kit), and stained with p-S727-STAT3-PE mAb Phosflow antibody (BD Biosciences) for 30 min at room temperature.

Techniques: Staining, Blocking Assay, Expressing, Cell Culture, Positive Control, Incubation

Journal: Frontiers in Immunology

Article Title: The CXCR4–STAT3–IL-10 Pathway Controls the Immunoregulatory Function of Chronic Lymphocytic Leukemia and Is Modulated by Lenalidomide

doi: 10.3389/fimmu.2017.01773

Figure Lengend Snippet: STAT3 inhibition abrogates CXC chemokine ligand 12 (CXCL12)–CXCR4 induced IL-10 production in chronic lymphocytic leukemia (CLL) cells. (A) The STAT3 inhibitor cucurbitacin inhibits CXCL12-induced IL-10 production by CLL cells. CLL cells were primed with 0.05 µM of the STAT3 inhibitor cucurbitacin for 2 h, and then stimulated with CXCL12 and phorbol myristate acetate (PMA), ionomycin and BFA (PIB) ( n = 9). (B) STAT3 knockdown using a green fluorescence protein (GFP)-lentivirus STAT3 short hairpin RNA (shRNA) resulted in abrogation of CXCL12 and CpG-induced IL-10 production in GFP+ CLL cells compared to CLL cells transfected with the empty vector ( n = 3).

Article Snippet: After one wash and 20 min of surface staining with CD19-APC (BD Biosciences) and CD5-FITC (BioLegend) antibodies, the cells were washed, permeabilized (Phospho-Epitopes Exposure kit-Beckman Coulter kit), and stained with p-S727-STAT3-PE mAb Phosflow antibody (BD Biosciences) for 30 min at room temperature.

Techniques: Inhibition, Fluorescence, shRNA, Transfection, Plasmid Preparation

Journal: Frontiers in Immunology

Article Title: The CXCR4–STAT3–IL-10 Pathway Controls the Immunoregulatory Function of Chronic Lymphocytic Leukemia and Is Modulated by Lenalidomide

doi: 10.3389/fimmu.2017.01773

Figure Lengend Snippet: The CXC chemokine ligand 12 (CXCL12)-mediated IL-10 production by chronic lymphocytic leukemia (CLL) cells induces T-cell suppression through phosphorylation of Y705-STAT3 in T cells. IL-10 from CLL cells induces phosphorylation of Y705-STAT3 in T cells. T cells were stimulated with 10 ng/ml of IL-10 or with supernatant from the coculture of CLL+CXCL12 for 20 min, fixed, permeabilized, and stained for p-Y705-STAT3 ( n = 12).

Article Snippet: After one wash and 20 min of surface staining with CD19-APC (BD Biosciences) and CD5-FITC (BioLegend) antibodies, the cells were washed, permeabilized (Phospho-Epitopes Exposure kit-Beckman Coulter kit), and stained with p-S727-STAT3-PE mAb Phosflow antibody (BD Biosciences) for 30 min at room temperature.

Techniques: Staining

Journal: Frontiers in Immunology

Article Title: The CXCR4–STAT3–IL-10 Pathway Controls the Immunoregulatory Function of Chronic Lymphocytic Leukemia and Is Modulated by Lenalidomide

doi: 10.3389/fimmu.2017.01773

Figure Lengend Snippet: Lenalidomide can reverse chronic lymphocytic leukemia (CLL)-induced T-cell dysfunction by inhibiting CXC chemokine ligand 12 (CXCL12)-mediated IL-10 production by CLL cells. (A) Lenalidomide exposure reverses CXCL12-induced S727-STAT3 phosphorylation in CLL cells. CLL cells were incubated with 10 µM lenalidomide for 2 ( n = 10) or 24 h ( n = 8) at 37°C and then stimulated with 250 ng/ml CXCL12 for 20 min, fixed, permeabilized, and stained for p-S727-STAT3. (B) . Lenalidomide exposure reverses CXCL12-induced IL-10 production by CLL cells. CLL cells were cultured for 2 h with 10 µM lenalidomide. The cells were then stimulated with CXCL12, fixed, and stained according to our IL-10 staining protocol ( n = 11).

Article Snippet: After one wash and 20 min of surface staining with CD19-APC (BD Biosciences) and CD5-FITC (BioLegend) antibodies, the cells were washed, permeabilized (Phospho-Epitopes Exposure kit-Beckman Coulter kit), and stained with p-S727-STAT3-PE mAb Phosflow antibody (BD Biosciences) for 30 min at room temperature.

Techniques: Incubation, Staining, Cell Culture

Journal: Frontiers in Immunology

Article Title: The CXCR4–STAT3–IL-10 Pathway Controls the Immunoregulatory Function of Chronic Lymphocytic Leukemia and Is Modulated by Lenalidomide

doi: 10.3389/fimmu.2017.01773

Figure Lengend Snippet: Lenalidomide can reverse chronic lymphocytic leukemia (CLL)-induced T-cell dysfunction by inhibiting IL-10 induced Y705-STAT3 phosphorylation in T cells. (A) Lenalidomide exposure prevents IL-10-induced Y705-STAT3 phosphorylation in T cells. T cells were stimulated with 10 ng/ml IL-10 or with the supernatant from CLL+CXC chemokine ligand 12 (CXCL12) cultures in the presence or absence of lenalidomide. Cells were then fixed and stained for p-Y705-STAT3 phosflow ( n = 5). (B) Lenalidomide protects T cells from CLL-induced suppression. T cells were cocultured with CLL cells (1:10 ratio) alone or with 250 ng/ml CXCL12 in the presence or absence of 10 µM lenalidomide for 48 h. T cells were then isolated and stimulated with anti-CD3/CD28 beads for 6 h and stained for IFNγ, TNFα, IL-2, and CD107a, gated on CD3+ cells ( n = 8).

Article Snippet: After one wash and 20 min of surface staining with CD19-APC (BD Biosciences) and CD5-FITC (BioLegend) antibodies, the cells were washed, permeabilized (Phospho-Epitopes Exposure kit-Beckman Coulter kit), and stained with p-S727-STAT3-PE mAb Phosflow antibody (BD Biosciences) for 30 min at room temperature.

Techniques: Staining, Isolation

Journal: Frontiers in Immunology

Article Title: The CXCR4–STAT3–IL-10 Pathway Controls the Immunoregulatory Function of Chronic Lymphocytic Leukemia and Is Modulated by Lenalidomide

doi: 10.3389/fimmu.2017.01773

Figure Lengend Snippet: Lenalidomide blocks CXC chemokine ligand 12 (CXCL12)-induced S727-STAT3 phosphorylation and IL-10 production by chronic lymphocytic leukemia (CLL) cells in vivo . PBMCs were collected from five patients treated with lenalidomide monotherapy (clinical trial 2006-0715, NCT00535873) before and after 3 months of treatment. (A) Lenalidomide therapy reduced CXCL12-induced p-S727-STAT3 in CLL cells. CLL cells were cultured in the presence or absence of 250 ng/ml of CXCL12 for 20 min. The cells were then fixed, permeabilized, and stained for p-S727-STAT3. (B) Lenalidomide therapy reduces CXCL12-induced IL-10 production by CLL cells. CLL cells were stimulated with 250 ng/ml CXC12 and cultured for 8–10 h, followed by addition of phorbol myristate acetate (PMA), ionomycin, BFA (PIB), then incubated for 6 h before performing intracellular staining.

Article Snippet: After one wash and 20 min of surface staining with CD19-APC (BD Biosciences) and CD5-FITC (BioLegend) antibodies, the cells were washed, permeabilized (Phospho-Epitopes Exposure kit-Beckman Coulter kit), and stained with p-S727-STAT3-PE mAb Phosflow antibody (BD Biosciences) for 30 min at room temperature.

Techniques: In Vivo, Cell Culture, Staining, Incubation

Journal: Nucleic Acids Research

Article Title: Precise and efficient C-to-U RNA base editing with SNAP-CDAR-S

doi: 10.1093/nar/gkad598

Figure Lengend Snippet: Benchmark with Cas13-RESCUE-S on endogenous targets and applications. ( A ) Comparison of editing yields at various sites on various endogenous targets and one disease-relevant cDNA (APOE) comparing SNAP-CDAR-S with standard guide RNAs (30 nt, 6-C-23, 2′OMe gapmer) versus Cas13 RESCUE-S with plasmid-borne optimized Cas guide RNAs. Both editing enzymes were expressed from the same single genomic locus. ( B ) Comparing both tools, SNAP-CADR-S versus Cas RESCUE-S, for the activation of β-catenin by RNA editing. Given are C-to-U editing yields (T41I) and the luminescence-based read-out of pathway activation. For further controls, see . ( C ) Editing of the regulatory phospho-site serine 727-to-glycine in STAT3, read-out of editing yield by Sanger sequencing, and amount of total STAT3 and pS727 STAT3 protein by western blot. Data in (A), (B) and (C) are shown as the mean ± s.d. of N = 3 independent experiments.

Article Snippet: 30 μg of total protein was run on a NovexTM WedgeWellTM 8 to 16%, Tris-glycine, 1.0 mm, Mini Protein Gel (ThermoFisher Scientific) with 200 V for 60 min. Blotting was performed with a Mini Trans-Blot Cell ® (BioRad) at 100 V for 60 min. For protein detection, membranes were incubated with monoclonal anti-β-actin antibody produced in mouse (Sigma, 1:5000 dil.) and either Stat3 (DRZ2G) Rabbit mAb (CellSignaling, 1:1000 dil.) or P-Stat3 (S727) (D8C2Z) Rabbit mAb (CellSignaling, 1:1000 dil.).

Techniques: Comparison, Plasmid Preparation, Activation Assay, Sequencing, Western Blot

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: 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: International Journal of Biological Sciences

Article Title: Chemical and genetic inhibition of STAT3 sensitizes hepatocellular carcinoma cells to sorafenib induced cell death

doi: 10.7150/ijbs.22220

Figure Lengend Snippet: JAK inhibitor I enhanced sorafenib induced cell death in STAT3 active HCC cells. (A, C, E) HCC cells were treated with 2uM JAK inhibitor I (JAKi), 5uM Sorafenib or their combination. The expression levels of STAT3, phospho-STAT3 (Y705) phospho-STAT3 (S727), Mcl-1 and GAPDH were determined by Western Blot. (B, D, F) Cell death assays were performed by pI staining and photographed under microscopy. Cell death rate was calculated by Image J. Data of three independent replicates are presented as the mean+/-s.e.m., n=3. (G) Huh7 cells were treated with JAKi (2uM), Sorafenib (5uM) and their combination for 60hours. Cell death assay was performed by pI staining and followed by flow cytometry analysis.

Article Snippet: Antibodies of anti STAT3 (#9139), anti phospho-STAT3 at Y705 (#9145) or anti phospho-STAT3 at S727 (#94994) were from Cell Signaling (Davers, MA).

Techniques: Expressing, Western Blot, Staining, Microscopy, Flow Cytometry

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