anti-stat3 antibody Search Results


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  • 99
    Cell Signaling Technology Inc anti stat 3 antibody
    RANKL induces the activation of NF-κB. (A) 4T1 and NMuMG cells were incubated with 100 ng/mL RANKL. At various time points, the cytoplasmic fractions and nuclear fractions were extracted and then subjected to SDS-PAGE/immunoblotting with anti-NF-κB p65, anti-phospho-ERK1/2, anti-phospho-Akt, anti-phospho-mTOR, anti-phospho-JNK, <t>anti-phospho-STAT3,</t> anti-ERK1/2, anti-Akt, anti-mTOR, anti-JNK, and anti-STAT3 antibodies. Anti-β-actin and anti-lamin antibodies were used as internal standards. (B) Quantification of the amount of NF-κB p65, phospho-ERK1/2, phospho-Akt, phospho-mTOR or phospho-STAT3, normalized to the amounts of the corresponding proteins, respectively. The results are representative of 5 independent experiments. *p
    Anti Stat 3 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1666 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti stat 3 antibody/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1666 article reviews
    Price from $9.99 to $1999.99
    anti stat 3 antibody - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    93
    Boster Bio anti stat3
    RANKL induces the activation of NF-κB. (A) 4T1 and NMuMG cells were incubated with 100 ng/mL RANKL. At various time points, the cytoplasmic fractions and nuclear fractions were extracted and then subjected to SDS-PAGE/immunoblotting with anti-NF-κB p65, anti-phospho-ERK1/2, anti-phospho-Akt, anti-phospho-mTOR, anti-phospho-JNK, <t>anti-phospho-STAT3,</t> anti-ERK1/2, anti-Akt, anti-mTOR, anti-JNK, and anti-STAT3 antibodies. Anti-β-actin and anti-lamin antibodies were used as internal standards. (B) Quantification of the amount of NF-κB p65, phospho-ERK1/2, phospho-Akt, phospho-mTOR or phospho-STAT3, normalized to the amounts of the corresponding proteins, respectively. The results are representative of 5 independent experiments. *p
    Anti Stat3, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti stat3/product/Boster Bio
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    anti stat3 - by Bioz Stars, 2020-05
    93/100 stars
      Buy from Supplier

    95
    Abcam anti stat3 antibody
    LncRNA PTCSC3 regulated INO80 through <t>STAT3.</t> (A) The expression levels of INO80 mRNA and protein in FTC238 cells were examined by qRT-PCR and western blot, respectively. ** P
    Anti Stat3 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti stat3 antibody/product/Abcam
    Average 95 stars, based on 112 article reviews
    Price from $9.99 to $1999.99
    anti stat3 antibody - by Bioz Stars, 2020-05
    95/100 stars
      Buy from Supplier

    99
    Abcam stat3 polyclonal antibody
    LncRNA PTCSC3 regulated INO80 through <t>STAT3.</t> (A) The expression levels of INO80 mRNA and protein in FTC238 cells were examined by qRT-PCR and western blot, respectively. ** P
    Stat3 Polyclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/stat3 polyclonal antibody/product/Abcam
    Average 99 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    stat3 polyclonal antibody - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    Image Search Results


    RANKL induces the activation of NF-κB. (A) 4T1 and NMuMG cells were incubated with 100 ng/mL RANKL. At various time points, the cytoplasmic fractions and nuclear fractions were extracted and then subjected to SDS-PAGE/immunoblotting with anti-NF-κB p65, anti-phospho-ERK1/2, anti-phospho-Akt, anti-phospho-mTOR, anti-phospho-JNK, anti-phospho-STAT3, anti-ERK1/2, anti-Akt, anti-mTOR, anti-JNK, and anti-STAT3 antibodies. Anti-β-actin and anti-lamin antibodies were used as internal standards. (B) Quantification of the amount of NF-κB p65, phospho-ERK1/2, phospho-Akt, phospho-mTOR or phospho-STAT3, normalized to the amounts of the corresponding proteins, respectively. The results are representative of 5 independent experiments. *p

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Activation of NF-?B by the RANKL/RANK system up-regulates snail and twist expressions and induces epithelial-to-mesenchymal transition in mammary tumor cell lines

    doi: 10.1186/1756-9966-32-62

    Figure Lengend Snippet: RANKL induces the activation of NF-κB. (A) 4T1 and NMuMG cells were incubated with 100 ng/mL RANKL. At various time points, the cytoplasmic fractions and nuclear fractions were extracted and then subjected to SDS-PAGE/immunoblotting with anti-NF-κB p65, anti-phospho-ERK1/2, anti-phospho-Akt, anti-phospho-mTOR, anti-phospho-JNK, anti-phospho-STAT3, anti-ERK1/2, anti-Akt, anti-mTOR, anti-JNK, and anti-STAT3 antibodies. Anti-β-actin and anti-lamin antibodies were used as internal standards. (B) Quantification of the amount of NF-κB p65, phospho-ERK1/2, phospho-Akt, phospho-mTOR or phospho-STAT3, normalized to the amounts of the corresponding proteins, respectively. The results are representative of 5 independent experiments. *p

    Article Snippet: The membranes were blocked with a solution containing 3% skim milk and incubated overnight at 4°C with each of the following antibodies: anti-NF-κB p65, anti-phospho-extracellular signal-regulated kinase (ERK) 1/2 antibody, anti-phospho-Akt antibody, anti-phospho-mammalian target of rapamycin (mTOR) antibody, anti-phospho-c-Jun N-terminal kinase (JNK) antibody, anti-phospho-signal transducers and activator of transcription 3 (STAT3) antibody, anti-ERK1/2 antibody, anti-Akt antibody, anti-mTOR antibody, anti-JNK antibody, and anti-STAT3 antibody (Cell Signaling Technology).

    Techniques: Activation Assay, Incubation, SDS Page

    miR-19b inhibits STAT3 transcriptional activity in EA.hy 926 cells. (A) p-STAT3 levels were detected in EA.hy926 cells transfected with miR-19b mimic or NC mimic (final concentration, 30 pmol/ml) for 24 h by western blot analysis. Densitometry was performed and levels were normalized to t-STAT3 expression (n=3). (B) EA.hy926 cells were transfected with STAT3-driven promoter (2×APRE) firefly luciferase reporter plasmid, alongside miR-19b mimic or NC mimic. Luciferase activities were normalized to Renilla activities (n=4). Data are presented as the mean ± standard error of the mean. * P

    Journal: International Journal of Molecular Medicine

    Article Title: The potential inhibitory effects of miR-19b on vulnerable plaque formation via the suppression of STAT3 transcriptional activity

    doi: 10.3892/ijmm.2017.3263

    Figure Lengend Snippet: miR-19b inhibits STAT3 transcriptional activity in EA.hy 926 cells. (A) p-STAT3 levels were detected in EA.hy926 cells transfected with miR-19b mimic or NC mimic (final concentration, 30 pmol/ml) for 24 h by western blot analysis. Densitometry was performed and levels were normalized to t-STAT3 expression (n=3). (B) EA.hy926 cells were transfected with STAT3-driven promoter (2×APRE) firefly luciferase reporter plasmid, alongside miR-19b mimic or NC mimic. Luciferase activities were normalized to Renilla activities (n=4). Data are presented as the mean ± standard error of the mean. * P

    Article Snippet: The following antibodies were used in the present study: Anti-STAT3 (cat. no. 9132S; 1:1,000 diluted) and anti-phosphorylated-STAT3 (Tyr 705) (cat. no. 9131S; 1:1,000 diluted; both from Cell Signaling Technology, Inc., Beverly, MA, USA).

    Techniques: Activity Assay, Transfection, Concentration Assay, Western Blot, Expressing, Luciferase, Plasmid Preparation

    Phosphorylated STAT3 levels in injured hippocampus after CCI. (A) Representative western blots of protein homogenates from whole ipsilateral hippocampus (relative to side of CCI) of mice 6 hours, 24 hours, 48 hours, 1 week and 16 weeks after CCI probed with pSTAT3 and STAT3 antibodies. (B) Quantification of pSTAT3 levels from CCI-S, CCI-M and sham injured controls showed that from 6 hours to 72 hours post injury the pSTAT3 levels were higher in both the CCI-S and CCI-M injured group when compared to sham injured controls. Levels of pSTAT3 in the CCI-S groups were statistically higher than the levels in the CCI-M group at 6 hours post injury but, at all other time points there was no statistical difference between CCI-S and CCI-M groups in pSTAT3 protein levels. * P

    Journal: Experimental neurology

    Article Title: JAK/STAT pathway regulation of GABAA Receptor expression after differing severities of experimental TBI

    doi: 10.1016/j.expneurol.2015.07.001

    Figure Lengend Snippet: Phosphorylated STAT3 levels in injured hippocampus after CCI. (A) Representative western blots of protein homogenates from whole ipsilateral hippocampus (relative to side of CCI) of mice 6 hours, 24 hours, 48 hours, 1 week and 16 weeks after CCI probed with pSTAT3 and STAT3 antibodies. (B) Quantification of pSTAT3 levels from CCI-S, CCI-M and sham injured controls showed that from 6 hours to 72 hours post injury the pSTAT3 levels were higher in both the CCI-S and CCI-M injured group when compared to sham injured controls. Levels of pSTAT3 in the CCI-S groups were statistically higher than the levels in the CCI-M group at 6 hours post injury but, at all other time points there was no statistical difference between CCI-S and CCI-M groups in pSTAT3 protein levels. * P

    Article Snippet: Protein bands were detected with the use of chemiluminescent solution (Pierce), then membranes were stripped and reprobed with rabbit polyclonal antibody raised against total STAT3 (anti-STAT3) (Cell Signaling Technologies; 1:6,000) or β-actin (Sigma 1:40,000) and bands were quantified using Image J software (NIH) and expressed as percent or fold change with respect to mean control values in the same run (defined as 100 or 1, respectively).

    Techniques: Western Blot, Mouse Assay

    WP1066 administration after CCI-S reduces phosphorylated STAT3 levels in injured hippocampus. (A) Representative western blots of protein homogenates from whole ipsilateral hippocampus (relative to side of CCI) of mice 6 hours, 24 hours, 48 hours, 1 week and 16 weeks after CCI-S treated with vehicle or WP1066 probed with pSTAT3 and STAT3 antibodies. (B) Quantification of pSTAT3 levels from CCI-S, CCI-S + WP and sham injured controls showed that from 6 hours to 48 hours post injury that pSTAT3 levels were statistically lower than CCI-S injured mice treated with WP1066 compared to vehicle-treated CCI-S mice. * P

    Journal: Experimental neurology

    Article Title: JAK/STAT pathway regulation of GABAA Receptor expression after differing severities of experimental TBI

    doi: 10.1016/j.expneurol.2015.07.001

    Figure Lengend Snippet: WP1066 administration after CCI-S reduces phosphorylated STAT3 levels in injured hippocampus. (A) Representative western blots of protein homogenates from whole ipsilateral hippocampus (relative to side of CCI) of mice 6 hours, 24 hours, 48 hours, 1 week and 16 weeks after CCI-S treated with vehicle or WP1066 probed with pSTAT3 and STAT3 antibodies. (B) Quantification of pSTAT3 levels from CCI-S, CCI-S + WP and sham injured controls showed that from 6 hours to 48 hours post injury that pSTAT3 levels were statistically lower than CCI-S injured mice treated with WP1066 compared to vehicle-treated CCI-S mice. * P

    Article Snippet: Protein bands were detected with the use of chemiluminescent solution (Pierce), then membranes were stripped and reprobed with rabbit polyclonal antibody raised against total STAT3 (anti-STAT3) (Cell Signaling Technologies; 1:6,000) or β-actin (Sigma 1:40,000) and bands were quantified using Image J software (NIH) and expressed as percent or fold change with respect to mean control values in the same run (defined as 100 or 1, respectively).

    Techniques: Western Blot, Mouse Assay

    Elevated STAT3 expression and phosphorylation in SHH MB. Immunohistochemical staining for total STAT3, pY705 STAT3 or pS727 STAT3 in normal cerebellum and SHH medulloblastoma tumors from Ptch1 LacZ/ + mice. Representative fields from at least three independent mice. Scale bar = 100 μm.

    Journal: Cancers

    Article Title: A Sexually Dimorphic Role for STAT3 in Sonic Hedgehog Medulloblastoma

    doi: 10.3390/cancers11111702

    Figure Lengend Snippet: Elevated STAT3 expression and phosphorylation in SHH MB. Immunohistochemical staining for total STAT3, pY705 STAT3 or pS727 STAT3 in normal cerebellum and SHH medulloblastoma tumors from Ptch1 LacZ/ + mice. Representative fields from at least three independent mice. Scale bar = 100 μm.

    Article Snippet: The following antibodies and concentrations were used: anti-STAT3 (1/50, polyclonal H-190, Santa Cruz Biotechnology catalog #sc-7179), anti STAT3 pY705 (1/50 Cell Signaling Technology catalog #9145), anti-STAT3 pS727 (1/50 Cell Signaling Technology catalog #9134), anti-GFAP – 1/200, Millipore clone GA5, catalog #MAB360), anti-β-III Tubulin (1/200, Millipore catalog # MAB5564) Anti-NeuN, (1/100, clone A60, Millipore catalog # MAB377), anti-CD45 (1/100, BD Biosciences catalog #550539), anti-PCNA (1/200, DAKO catalog M0879).

    Techniques: Expressing, Immunohistochemistry, Staining, Mouse Assay

    miR-543 overexpression suppresses the migration and invasion of CRC cells in vitro and re-expression of KRAS, MTA1 and HMGA2 reverses the miR-543-induced effects on CRC cells ( A ) Transwell migration assays revealed that ectopic overexpression of miR-543 inhibits the migration ability of SW620 and LoVo cells. ( B ) Transwell invasion assay with Matrigel-coated membranes revealed that miR-543 overexpression inhibits the invasion ability of SW620 and LoVo cells. ( C ) qRT-PCR analysis revealed that miR-543 downregulates the mRNA expression of MTA1 and HMGA2 and their downstream genes STAT3, MMP2, MMP9 and LOX but upregulates miR-200b in SW620 (top) and LoVo (bottom) cells. ( D ) Western blot analysis of the effects of miR-543 overexpression on the expression of MTA1 and HMGA2 and their downstream targets STAT3, LOX and p-FAK in SW620 (left) and LoVo (right) cells. ( E ) Western blot analysis of KRAS, MTA1 or HMGA2 re-expression in LoVo-miR-543 cells. LoVo-miR-543 cells were transfected with miRNA-resistant expression constructs for KRAS, MTA1 or HMGA2. Control (Ctrl) represents scrambled miRNA, and vector represents the empty vector used in KRAS, MTA1 and HMGA2 re-expression. ( F, G ) MTT assay ( F ) and migration ( G ) analysis of the proliferation of LoVo-miR-543 cells transfected with miRNA-resistant expression constructs for KRAS, MTA1 or HMGA2. These results are representative of at least three independent experiments. Scale bars, 100 μm. * p

    Journal: Oncotarget

    Article Title: MicroRNA-543 suppresses colorectal cancer growth and metastasis by targeting KRAS, MTA1 and HMGA2

    doi: 10.18632/oncotarget.7989

    Figure Lengend Snippet: miR-543 overexpression suppresses the migration and invasion of CRC cells in vitro and re-expression of KRAS, MTA1 and HMGA2 reverses the miR-543-induced effects on CRC cells ( A ) Transwell migration assays revealed that ectopic overexpression of miR-543 inhibits the migration ability of SW620 and LoVo cells. ( B ) Transwell invasion assay with Matrigel-coated membranes revealed that miR-543 overexpression inhibits the invasion ability of SW620 and LoVo cells. ( C ) qRT-PCR analysis revealed that miR-543 downregulates the mRNA expression of MTA1 and HMGA2 and their downstream genes STAT3, MMP2, MMP9 and LOX but upregulates miR-200b in SW620 (top) and LoVo (bottom) cells. ( D ) Western blot analysis of the effects of miR-543 overexpression on the expression of MTA1 and HMGA2 and their downstream targets STAT3, LOX and p-FAK in SW620 (left) and LoVo (right) cells. ( E ) Western blot analysis of KRAS, MTA1 or HMGA2 re-expression in LoVo-miR-543 cells. LoVo-miR-543 cells were transfected with miRNA-resistant expression constructs for KRAS, MTA1 or HMGA2. Control (Ctrl) represents scrambled miRNA, and vector represents the empty vector used in KRAS, MTA1 and HMGA2 re-expression. ( F, G ) MTT assay ( F ) and migration ( G ) analysis of the proliferation of LoVo-miR-543 cells transfected with miRNA-resistant expression constructs for KRAS, MTA1 or HMGA2. These results are representative of at least three independent experiments. Scale bars, 100 μm. * p

    Article Snippet: Cell lysates were subjected to SDS–polyacrylamide gel and immunoblot analysis with antibodies against the following proteins: KRAS and HMGA2 (GeneTex); Vimentin (R & D); Cyclin D1 (Millipore); LOX (Abcam); p-FAK (Invitrogen); E-Cadherin, N-Cadherin and b-catenin (BD); MTA1, STAT3, ERK, p-ERK, MEK and p-MEK (Cell Signaling); b-actin (Sigma Aldrich).

    Techniques: Over Expression, Migration, In Vitro, Expressing, Transwell Invasion Assay, Quantitative RT-PCR, Western Blot, Transfection, Construct, Plasmid Preparation, MTT Assay

    miR-543 knockdown promotes the proliferation, invasion and metastasis of HCT116 cells in vitro and in vivo . ( A ) MTT analysis of the effects of miR-543 on the proliferation of HCT116 cells. ( B ) Representative images and quantification of colonies formed by HCT116-sh-Ctrl and HCT116-sh-miR-543 cells. ( C ) qRT-PCR analysis revealed that miR-543 knockdown upregulates the mRNA expression of KRAS, MTA1 and HMGA2 and their downstream genes Cyclin D1, STAT3, MMP2, MMP9 and LOX but downregulates miR-200b in HCT116 cells. ( D ) Western blot analysis of the levels of KRAS and the proliferation-related proteins p-MEK, MEK, p-ERK1/2, ERK and Cyclin D1 (left), and MTA1 and HMGA2 and their downstream genes STAT3, LOX and p-FAK (right) in HCT116-sh-Ctrl and HCT116-sh-miR-543 cells. ( E, F ) Transwell migration assays ( E ) and Matrigel-coated membrane Transwell invasion assays ( F ) demonstrated that miR-543 knockdown promotes the migration and invasion of HCT116 cells in vitro . ( G ) Bioluminescence images of nude mice showing tumors derived 28 days after subcutaneous injection in the lower back regions of nude mice with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells (left). Images of isolated tumors (middle) and quantitation of tumor weights (right) from mice 28 days after injection with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells. n = 5 per group. ( H ) Bioluminescence images of metastatic tumors in mice 28 days after intrasplenic injection with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells (left). Bioluminescence images of intestines and livers isolated from mice 28 days after intrasplenic injection with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells (middle). Quantitation of metastases in the whole bodies, intestines and livers of these mice (right). n = 5 per group. Scale bars, 200 μm. * p

    Journal: Oncotarget

    Article Title: MicroRNA-543 suppresses colorectal cancer growth and metastasis by targeting KRAS, MTA1 and HMGA2

    doi: 10.18632/oncotarget.7989

    Figure Lengend Snippet: miR-543 knockdown promotes the proliferation, invasion and metastasis of HCT116 cells in vitro and in vivo . ( A ) MTT analysis of the effects of miR-543 on the proliferation of HCT116 cells. ( B ) Representative images and quantification of colonies formed by HCT116-sh-Ctrl and HCT116-sh-miR-543 cells. ( C ) qRT-PCR analysis revealed that miR-543 knockdown upregulates the mRNA expression of KRAS, MTA1 and HMGA2 and their downstream genes Cyclin D1, STAT3, MMP2, MMP9 and LOX but downregulates miR-200b in HCT116 cells. ( D ) Western blot analysis of the levels of KRAS and the proliferation-related proteins p-MEK, MEK, p-ERK1/2, ERK and Cyclin D1 (left), and MTA1 and HMGA2 and their downstream genes STAT3, LOX and p-FAK (right) in HCT116-sh-Ctrl and HCT116-sh-miR-543 cells. ( E, F ) Transwell migration assays ( E ) and Matrigel-coated membrane Transwell invasion assays ( F ) demonstrated that miR-543 knockdown promotes the migration and invasion of HCT116 cells in vitro . ( G ) Bioluminescence images of nude mice showing tumors derived 28 days after subcutaneous injection in the lower back regions of nude mice with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells (left). Images of isolated tumors (middle) and quantitation of tumor weights (right) from mice 28 days after injection with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells. n = 5 per group. ( H ) Bioluminescence images of metastatic tumors in mice 28 days after intrasplenic injection with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells (left). Bioluminescence images of intestines and livers isolated from mice 28 days after intrasplenic injection with HCT116-sh-Ctrl or HCT116-sh-miR-543 cells (middle). Quantitation of metastases in the whole bodies, intestines and livers of these mice (right). n = 5 per group. Scale bars, 200 μm. * p

    Article Snippet: Cell lysates were subjected to SDS–polyacrylamide gel and immunoblot analysis with antibodies against the following proteins: KRAS and HMGA2 (GeneTex); Vimentin (R & D); Cyclin D1 (Millipore); LOX (Abcam); p-FAK (Invitrogen); E-Cadherin, N-Cadherin and b-catenin (BD); MTA1, STAT3, ERK, p-ERK, MEK and p-MEK (Cell Signaling); b-actin (Sigma Aldrich).

    Techniques: In Vitro, In Vivo, MTT Assay, Quantitative RT-PCR, Expressing, Western Blot, Migration, Mouse Assay, Derivative Assay, Injection, Isolation, Quantitation Assay

    NFATc2 contributes to gastric carcinogenesis by affecting the inflammatory pathways. a Cell anchorage-independent growth in transformed cells with NFATC2 siRNA knockdown. b Gene set enrichment plots of differentially expressed genes belonging to the NFATc pathway in NOC-treated cells. P value is determined by GSEA software. c IL-6 and IL-11 mRNA expression in malignant transformed cells by RT-qPCR. d IL-6 expression by PCR after NOC treatment at different times. e IL-6 production detected by ELISA after NOC treatment at different times. f RT-qPCR analysis of IL-6 and IL-11 mRNA levels after knockdown NFATc2 by siRNA. g The transformed cells were treated by cyclosporine A (CSA) 10 μM for 24 h, and STAT3 Y705 phosphorylation was detected by WB. h and i NFATc2 expression in 52 paired gastric cancer tissues by IHC, and TCGA database analysis, respectively. The analyses were repeated three times, and the results were expressed as mean ± SD. * p

    Journal: Oncogenesis

    Article Title: STAT3 activates MSK1-mediated histone H3 phosphorylation to promote NFAT signaling in gastric carcinogenesis

    doi: 10.1038/s41389-020-0195-2

    Figure Lengend Snippet: NFATc2 contributes to gastric carcinogenesis by affecting the inflammatory pathways. a Cell anchorage-independent growth in transformed cells with NFATC2 siRNA knockdown. b Gene set enrichment plots of differentially expressed genes belonging to the NFATc pathway in NOC-treated cells. P value is determined by GSEA software. c IL-6 and IL-11 mRNA expression in malignant transformed cells by RT-qPCR. d IL-6 expression by PCR after NOC treatment at different times. e IL-6 production detected by ELISA after NOC treatment at different times. f RT-qPCR analysis of IL-6 and IL-11 mRNA levels after knockdown NFATc2 by siRNA. g The transformed cells were treated by cyclosporine A (CSA) 10 μM for 24 h, and STAT3 Y705 phosphorylation was detected by WB. h and i NFATc2 expression in 52 paired gastric cancer tissues by IHC, and TCGA database analysis, respectively. The analyses were repeated three times, and the results were expressed as mean ± SD. * p

    Article Snippet: For ChIP assays, malignant transformed cells were treated with 50 μmol/L AG490 or mock for 24 h. Sheared chromatin was prepared and incubated with anti-MSK1 and anti-STAT3 antibodys (CST) for collecting the associated DNA.

    Techniques: Transformation Assay, Software, Expressing, Quantitative RT-PCR, Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Western Blot, Immunohistochemistry

    MSK1 and STAT3 can be recruited to the promoter of NFATC2, and activate its expression by coupling histone phosphorylation. a , b STAT3 and MSK1 protein interaction was derived from HEK 293T cells following the transfection with Myc-MSK1 and Flag-STAT3 by immunoprecipitation assay (IP). c Endogenous interaction between Stat3 and MSK1 by IP analysis derived from GES-1 or MNNG-transformed cells. d Flag-STAT3 fragments were co-expressed with Myc-MSK1 wild-type in HEK293T cells. After anti-Myc immunoprecipitation, coprecipitated STAT3 was revealed by immunoblotting. e RT-qPCR analysis of NFATc2 mRNA expression after STAT3 overexpression or siRNA knockdown. f The binding of MSK1 (left) or STAT3 (right) to the promoter of NFATc2 was analyzed by ChIP assay with anti-MSK1 or anti-STAT3 antibody in the MNNG-transformed cells treated with vehicle or AG490. Ctr: control site. MSK1-BS: MSK1 binding site. STAT3-BS1: STAT3 binding site 1. STAT3-BS2: STAT3 binding site 2. g The correlation between STAT3 and NFATc2 expression or MSK1 and NFATc2 expression of the TCGA database were analyzed by GEPIA. The analyses were repeated three times, and the results were expressed as mean ± SD. * p

    Journal: Oncogenesis

    Article Title: STAT3 activates MSK1-mediated histone H3 phosphorylation to promote NFAT signaling in gastric carcinogenesis

    doi: 10.1038/s41389-020-0195-2

    Figure Lengend Snippet: MSK1 and STAT3 can be recruited to the promoter of NFATC2, and activate its expression by coupling histone phosphorylation. a , b STAT3 and MSK1 protein interaction was derived from HEK 293T cells following the transfection with Myc-MSK1 and Flag-STAT3 by immunoprecipitation assay (IP). c Endogenous interaction between Stat3 and MSK1 by IP analysis derived from GES-1 or MNNG-transformed cells. d Flag-STAT3 fragments were co-expressed with Myc-MSK1 wild-type in HEK293T cells. After anti-Myc immunoprecipitation, coprecipitated STAT3 was revealed by immunoblotting. e RT-qPCR analysis of NFATc2 mRNA expression after STAT3 overexpression or siRNA knockdown. f The binding of MSK1 (left) or STAT3 (right) to the promoter of NFATc2 was analyzed by ChIP assay with anti-MSK1 or anti-STAT3 antibody in the MNNG-transformed cells treated with vehicle or AG490. Ctr: control site. MSK1-BS: MSK1 binding site. STAT3-BS1: STAT3 binding site 1. STAT3-BS2: STAT3 binding site 2. g The correlation between STAT3 and NFATc2 expression or MSK1 and NFATc2 expression of the TCGA database were analyzed by GEPIA. The analyses were repeated three times, and the results were expressed as mean ± SD. * p

    Article Snippet: For ChIP assays, malignant transformed cells were treated with 50 μmol/L AG490 or mock for 24 h. Sheared chromatin was prepared and incubated with anti-MSK1 and anti-STAT3 antibodys (CST) for collecting the associated DNA.

    Techniques: Expressing, Derivative Assay, Transfection, Immunoprecipitation, Transformation Assay, Quantitative RT-PCR, Over Expression, Binding Assay, Chromatin Immunoprecipitation

    STAT3/MSK1/NFATc2 axis is activated in carcinogen-induced gastric tumorigenesis and correlates with poor prognosis in patients with gastric cancer. a Heatmap of the mRNA levels of NFATc2, STAT3, MSK1, IL-6 and IL-11 in stomach tissues from mice treated with or without carcinogens. b The representative images of HE staining, p-STAT3 Y705, MSK1, p-H3S10, NFATc2 expression of stomach tissues from the mice treated with carcinogens by IHC. Scale bar: 200 μm. c The tumor volume of xenograft assay ( n = 8, for each group) in NOC-transformed cell and gastric cancer cell MKN45 following the inhibition of STAT3 or NFATc2 by AZD1480 or CSA, respectively. The results were expressed as mean ± SD. * p

    Journal: Oncogenesis

    Article Title: STAT3 activates MSK1-mediated histone H3 phosphorylation to promote NFAT signaling in gastric carcinogenesis

    doi: 10.1038/s41389-020-0195-2

    Figure Lengend Snippet: STAT3/MSK1/NFATc2 axis is activated in carcinogen-induced gastric tumorigenesis and correlates with poor prognosis in patients with gastric cancer. a Heatmap of the mRNA levels of NFATc2, STAT3, MSK1, IL-6 and IL-11 in stomach tissues from mice treated with or without carcinogens. b The representative images of HE staining, p-STAT3 Y705, MSK1, p-H3S10, NFATc2 expression of stomach tissues from the mice treated with carcinogens by IHC. Scale bar: 200 μm. c The tumor volume of xenograft assay ( n = 8, for each group) in NOC-transformed cell and gastric cancer cell MKN45 following the inhibition of STAT3 or NFATc2 by AZD1480 or CSA, respectively. The results were expressed as mean ± SD. * p

    Article Snippet: For ChIP assays, malignant transformed cells were treated with 50 μmol/L AG490 or mock for 24 h. Sheared chromatin was prepared and incubated with anti-MSK1 and anti-STAT3 antibodys (CST) for collecting the associated DNA.

    Techniques: Mouse Assay, Staining, Expressing, Immunohistochemistry, Xenograft Assay, Transformation Assay, Inhibition

    STAT3 contributes to enhanced H3S10 phosphorylation in gastric carcinogenesis. a Representative image of NOC ( N -methyl- N -nitroso-urea, MNU) and H. pylori plus NOC -induced mouse model of gastric cancer. b HE staining of stomach tissues from the carcinogen-treated mice. c Histone H3 phosphorylation was analyzed by WB of stomach tissues from the carcinogen-treated mice at different times. d WB analysis of signaling pathways related to cell proliferation in GES-1 and NOC-treated cells with the indicated antibodies. e Cell colony-forming ability in soft agar of p-H3S10 increased or unchanged subcloned NOC-treated cells. f , g AG490 50 μM, SB203580 10 μM, AZD1480 2 μM, Tocilizumab 10 μM, scramble siRNA (siCtr) or STAT3 siRNA were used to treat the MNU-transformed cells, respectively. The level of p-H3S10 was determined by WB. h STAT3 expression score by IHC in 52 paired gastric cancer tissues. i The representative images of STAT3 and p-H3S10 levels in human gastric cancer tissues by IHC. Scale bar: 200μm. The analyses were repeated three times, and the results were expressed as mean ± SD. * /# p

    Journal: Oncogenesis

    Article Title: STAT3 activates MSK1-mediated histone H3 phosphorylation to promote NFAT signaling in gastric carcinogenesis

    doi: 10.1038/s41389-020-0195-2

    Figure Lengend Snippet: STAT3 contributes to enhanced H3S10 phosphorylation in gastric carcinogenesis. a Representative image of NOC ( N -methyl- N -nitroso-urea, MNU) and H. pylori plus NOC -induced mouse model of gastric cancer. b HE staining of stomach tissues from the carcinogen-treated mice. c Histone H3 phosphorylation was analyzed by WB of stomach tissues from the carcinogen-treated mice at different times. d WB analysis of signaling pathways related to cell proliferation in GES-1 and NOC-treated cells with the indicated antibodies. e Cell colony-forming ability in soft agar of p-H3S10 increased or unchanged subcloned NOC-treated cells. f , g AG490 50 μM, SB203580 10 μM, AZD1480 2 μM, Tocilizumab 10 μM, scramble siRNA (siCtr) or STAT3 siRNA were used to treat the MNU-transformed cells, respectively. The level of p-H3S10 was determined by WB. h STAT3 expression score by IHC in 52 paired gastric cancer tissues. i The representative images of STAT3 and p-H3S10 levels in human gastric cancer tissues by IHC. Scale bar: 200μm. The analyses were repeated three times, and the results were expressed as mean ± SD. * /# p

    Article Snippet: For ChIP assays, malignant transformed cells were treated with 50 μmol/L AG490 or mock for 24 h. Sheared chromatin was prepared and incubated with anti-MSK1 and anti-STAT3 antibodys (CST) for collecting the associated DNA.

    Techniques: Staining, Mouse Assay, Western Blot, Transformation Assay, Expressing, Immunohistochemistry

    STAT3 induces transcriptional activation of MSK1 and forms a positive feedback loop with MSK1. a , b RT-PCR analysis of MSK1 expression after STAT3 overexpression or siRNA knockdown in GES-1 or NOC-transformed cells. c NOC-transformed cells were treated with vehicle or AG490. The binding of STAT3 in the specific sites of MSK1 promoter were analyzed by ChIP-qPCR with anti-STAT3 antibody. Ctr: control site. BS1: binding site 1. BS2: binding site 2. d pLG3-MSK1 promoter constructs and STAT3 full-length or muntants were co-transfected into the cells, and the transcriptional activity of MSK1 promoter was analyzed by the luciferase reporter assay. e STAT3 Y705 or S727 phosphorylation levels were examined by WB with the specific antibodies in malignantly transformed cells. f STAT3 phosphorylation levels in the transformed cells following MSK1 siRNA knockdown were detected by WB analysis. g TCGA database analysis of STAT3 expression. h The correlation between STAT3 and MSK1 expression of the TCGA database were generated by GEPIA (Gene Expression Profiling Interactive Analysis, http://gepia.cancer-pku.cn/ ). The analyses were repeated three times, and the results were expressed as mean ± SD. * p

    Journal: Oncogenesis

    Article Title: STAT3 activates MSK1-mediated histone H3 phosphorylation to promote NFAT signaling in gastric carcinogenesis

    doi: 10.1038/s41389-020-0195-2

    Figure Lengend Snippet: STAT3 induces transcriptional activation of MSK1 and forms a positive feedback loop with MSK1. a , b RT-PCR analysis of MSK1 expression after STAT3 overexpression or siRNA knockdown in GES-1 or NOC-transformed cells. c NOC-transformed cells were treated with vehicle or AG490. The binding of STAT3 in the specific sites of MSK1 promoter were analyzed by ChIP-qPCR with anti-STAT3 antibody. Ctr: control site. BS1: binding site 1. BS2: binding site 2. d pLG3-MSK1 promoter constructs and STAT3 full-length or muntants were co-transfected into the cells, and the transcriptional activity of MSK1 promoter was analyzed by the luciferase reporter assay. e STAT3 Y705 or S727 phosphorylation levels were examined by WB with the specific antibodies in malignantly transformed cells. f STAT3 phosphorylation levels in the transformed cells following MSK1 siRNA knockdown were detected by WB analysis. g TCGA database analysis of STAT3 expression. h The correlation between STAT3 and MSK1 expression of the TCGA database were generated by GEPIA (Gene Expression Profiling Interactive Analysis, http://gepia.cancer-pku.cn/ ). The analyses were repeated three times, and the results were expressed as mean ± SD. * p

    Article Snippet: For ChIP assays, malignant transformed cells were treated with 50 μmol/L AG490 or mock for 24 h. Sheared chromatin was prepared and incubated with anti-MSK1 and anti-STAT3 antibodys (CST) for collecting the associated DNA.

    Techniques: Activation Assay, Reverse Transcription Polymerase Chain Reaction, Expressing, Over Expression, Transformation Assay, Binding Assay, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction, Construct, Transfection, Activity Assay, Luciferase, Reporter Assay, Western Blot, Generated

    Impaired IL-6-induced STAT3 phosphorylation in Cd4(Δlepr) T cells

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Leptin receptor signaling in T cells is required for Th17 differentiation

    doi: 10.4049/jimmunol.1402996

    Figure Lengend Snippet: Impaired IL-6-induced STAT3 phosphorylation in Cd4(Δlepr) T cells

    Article Snippet: The membrane was blocked for 1 hour with TBS-T 5% milk, incubated overnight with anti-phospho-STAT3 antibody (Cell Signaling Y705) and developed using secondary antibody conjugated to HRP.

    Techniques:

    Kinetics of signal transducer and activator of transcription 3 (STAT3)-regulated genes in anaplastic large cell lymphomas (ALCL). ( A ) RT-qPCR analysis shows progressive decrease of STAT3 mRNA levels in the anaplastic lymphoma kinase (ALK) positive cell line TS-SUP-M2 S3S after doxycycline treatment (1 µg/mL). Pellet were collected at 72, 96, 120, 144 h. Error bars represent the standard deviation (s.d.) of triplicate measurements. ( B ) Heatmap representation of gene expression profile analysis after STAT3 inducible knockdown in the ALK positive cell line TS-SUP-M2 S3S. Biological triplicate were used for each experimental condition. Hybridization was carried out on HumanHT-12 v4.0 Expression BeadChip (Illumina Inc., San Diego, CA, USA). STAT3 modulated genes were grouped in 12 clusters. Upregulated RNAs are shown in red, downregulated RNA are shown in green. The colour bar represents relative gene expression changes. In brackets are shown genes selected for functional validation.

    Journal: Cancers

    Article Title: IRF4 Mediates the Oncogenic Effects of STAT3 in Anaplastic Large Cell Lymphomas

    doi: 10.3390/cancers10010021

    Figure Lengend Snippet: Kinetics of signal transducer and activator of transcription 3 (STAT3)-regulated genes in anaplastic large cell lymphomas (ALCL). ( A ) RT-qPCR analysis shows progressive decrease of STAT3 mRNA levels in the anaplastic lymphoma kinase (ALK) positive cell line TS-SUP-M2 S3S after doxycycline treatment (1 µg/mL). Pellet were collected at 72, 96, 120, 144 h. Error bars represent the standard deviation (s.d.) of triplicate measurements. ( B ) Heatmap representation of gene expression profile analysis after STAT3 inducible knockdown in the ALK positive cell line TS-SUP-M2 S3S. Biological triplicate were used for each experimental condition. Hybridization was carried out on HumanHT-12 v4.0 Expression BeadChip (Illumina Inc., San Diego, CA, USA). STAT3 modulated genes were grouped in 12 clusters. Upregulated RNAs are shown in red, downregulated RNA are shown in green. The colour bar represents relative gene expression changes. In brackets are shown genes selected for functional validation.

    Article Snippet: 5 µg of antibodies anti-STAT3 #4904 (Cell Signaling), H3K4me3 (ab8580, Abcam, Cambridge, UK) H3K27Ac (ab177178, Abcam), H3K27me3 (ab6002, Abcam), or control IgG #2729 (Cell Signaling) were added to the precleared sample and incubated overnight at 4 °C.

    Techniques: Quantitative RT-PCR, Standard Deviation, Expressing, Hybridization, Functional Assay

    IRF4 partially mediates STAT3 oncogenic properties in ALCL cells. ( A ) TS-SUP-M2 S3S cells were transduced with lentiviral particles expressing human IRF4 open reading frame (ORF), an empty vector (EV), or left untransduced (UTR) as negative controls. Cells were cultured in the presence of 1 µg/mL doxycycline to induce STAT3 KD. Kinetics of cell death induced by conditional STAT3 KD revealed that cells expressing IRF4 displayed lower apoptotic rates compared to controls. Apoptosis analysis was performed by TMRM staining-flow cytometry at the indicated time points after doxycycline treatment. Error bars represent the s.d. of triplicate measurements (*** p

    Journal: Cancers

    Article Title: IRF4 Mediates the Oncogenic Effects of STAT3 in Anaplastic Large Cell Lymphomas

    doi: 10.3390/cancers10010021

    Figure Lengend Snippet: IRF4 partially mediates STAT3 oncogenic properties in ALCL cells. ( A ) TS-SUP-M2 S3S cells were transduced with lentiviral particles expressing human IRF4 open reading frame (ORF), an empty vector (EV), or left untransduced (UTR) as negative controls. Cells were cultured in the presence of 1 µg/mL doxycycline to induce STAT3 KD. Kinetics of cell death induced by conditional STAT3 KD revealed that cells expressing IRF4 displayed lower apoptotic rates compared to controls. Apoptosis analysis was performed by TMRM staining-flow cytometry at the indicated time points after doxycycline treatment. Error bars represent the s.d. of triplicate measurements (*** p

    Article Snippet: 5 µg of antibodies anti-STAT3 #4904 (Cell Signaling), H3K4me3 (ab8580, Abcam, Cambridge, UK) H3K27Ac (ab177178, Abcam), H3K27me3 (ab6002, Abcam), or control IgG #2729 (Cell Signaling) were added to the precleared sample and incubated overnight at 4 °C.

    Techniques: Transduction, Expressing, Plasmid Preparation, Cell Culture, Staining, Flow Cytometry, Cytometry

    STAT3 binds to IRF4 regulatory regions in ALK-positive ALCL cells. STAT3 (blue), H3K4me (green), H3K27Ac (purple) and H3K27me3 (orange) bindings to IRF4 in TS-SUP-M2 cells. Loss of STAT3 binding (light blue) was achieved after crizotinib treatment (6 h, 200 nM). y -axis values represent read densities normalized to total number of reads.

    Journal: Cancers

    Article Title: IRF4 Mediates the Oncogenic Effects of STAT3 in Anaplastic Large Cell Lymphomas

    doi: 10.3390/cancers10010021

    Figure Lengend Snippet: STAT3 binds to IRF4 regulatory regions in ALK-positive ALCL cells. STAT3 (blue), H3K4me (green), H3K27Ac (purple) and H3K27me3 (orange) bindings to IRF4 in TS-SUP-M2 cells. Loss of STAT3 binding (light blue) was achieved after crizotinib treatment (6 h, 200 nM). y -axis values represent read densities normalized to total number of reads.

    Article Snippet: 5 µg of antibodies anti-STAT3 #4904 (Cell Signaling), H3K4me3 (ab8580, Abcam, Cambridge, UK) H3K27Ac (ab177178, Abcam), H3K27me3 (ab6002, Abcam), or control IgG #2729 (Cell Signaling) were added to the precleared sample and incubated overnight at 4 °C.

    Techniques: Binding Assay

    MCP-1 is not required for STAT3 activation during liver regeneration. Western blot analysis of STAT3 and phosphorylated- STAT3 proteins in the regenerating liver of wild type and MCP-1 knockout mice at the indicated times after PH (20 μg protein/lane)

    Journal: Journal of Inflammation (London, England)

    Article Title: Monocyte chemoattractant protein-1 is not required for liver regeneration after partial hepatectomy

    doi: 10.1186/s12950-016-0136-1

    Figure Lengend Snippet: MCP-1 is not required for STAT3 activation during liver regeneration. Western blot analysis of STAT3 and phosphorylated- STAT3 proteins in the regenerating liver of wild type and MCP-1 knockout mice at the indicated times after PH (20 μg protein/lane)

    Article Snippet: Homogenates (25–50 μg protein/lane) were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to polyvinylidene difluoride membranes for western blot analysis with anti-STAT3 and anti-phosphorylated STAT3 antibodies (Cell Signaling Technology, Danvers, MA).

    Techniques: Activation Assay, Western Blot, Knock-Out, Mouse Assay

    LncRNA PTCSC3 regulated INO80 through STAT3. (A) The expression levels of INO80 mRNA and protein in FTC238 cells were examined by qRT-PCR and western blot, respectively. ** P

    Journal: Cancer Biology & Therapy

    Article Title: LncRNA PTCSC3 affects drug resistance of anaplastic thyroid cancer through STAT3/INO80 pathway

    doi: 10.1080/15384047.2018.1449610

    Figure Lengend Snippet: LncRNA PTCSC3 regulated INO80 through STAT3. (A) The expression levels of INO80 mRNA and protein in FTC238 cells were examined by qRT-PCR and western blot, respectively. ** P

    Article Snippet: The membrane was then blocked with 5% nonfat milk for 1 hour at RT, and then incubated with the following primary antibodies: anti-STAT3 antibody (Abcam, 1:3000), anti-INO80 antibody (1:1000), anti-ALDH antibody (1:500), anti-MDR1 antibody (1:2000), anti-β-actin antibody (Abcam, 1:2000) at 4°C for overnight.

    Techniques: Expressing, Quantitative RT-PCR, Western Blot

    LncRNA PTCSC3 negatively regulated STAT3. (A) Combination condition between PTCSC3 and STAT3 was determined by RIP assay. (B) The interaction between PTCSC3 and STAT3 was detected by RNA pull-down assay. ** P

    Journal: Cancer Biology & Therapy

    Article Title: LncRNA PTCSC3 affects drug resistance of anaplastic thyroid cancer through STAT3/INO80 pathway

    doi: 10.1080/15384047.2018.1449610

    Figure Lengend Snippet: LncRNA PTCSC3 negatively regulated STAT3. (A) Combination condition between PTCSC3 and STAT3 was determined by RIP assay. (B) The interaction between PTCSC3 and STAT3 was detected by RNA pull-down assay. ** P

    Article Snippet: The membrane was then blocked with 5% nonfat milk for 1 hour at RT, and then incubated with the following primary antibodies: anti-STAT3 antibody (Abcam, 1:3000), anti-INO80 antibody (1:1000), anti-ALDH antibody (1:500), anti-MDR1 antibody (1:2000), anti-β-actin antibody (Abcam, 1:2000) at 4°C for overnight.

    Techniques: Pull Down Assay

    STAT3 promoted expression of INO80. (A) The chromatin immune-precipitation was used to verify the binding between PTCSC3 and the promoter of STAT3. (B) The expression levels of INO80 mRNA and protein in FTC238 cells were examined by qRT-PCR and western blot, respectively. ** P

    Journal: Cancer Biology & Therapy

    Article Title: LncRNA PTCSC3 affects drug resistance of anaplastic thyroid cancer through STAT3/INO80 pathway

    doi: 10.1080/15384047.2018.1449610

    Figure Lengend Snippet: STAT3 promoted expression of INO80. (A) The chromatin immune-precipitation was used to verify the binding between PTCSC3 and the promoter of STAT3. (B) The expression levels of INO80 mRNA and protein in FTC238 cells were examined by qRT-PCR and western blot, respectively. ** P

    Article Snippet: The membrane was then blocked with 5% nonfat milk for 1 hour at RT, and then incubated with the following primary antibodies: anti-STAT3 antibody (Abcam, 1:3000), anti-INO80 antibody (1:1000), anti-ALDH antibody (1:500), anti-MDR1 antibody (1:2000), anti-β-actin antibody (Abcam, 1:2000) at 4°C for overnight.

    Techniques: Expressing, Binding Assay, Quantitative RT-PCR, Western Blot

    Expression of Smad3, NFAT2, and Stat3 in the duodenum . (a) The results of Smad3, NFAT2, and Stat3 western blot analysis. (b) The average optical density (AOD) of Smad3, NFAT2, and Stat3 in the duodenum was analysed using immunohistochemistry. The sections are represented as a percentage of the total duodenum (200×). Results represent 1 experiment repeated 3 times. Six mice per group were used in the study. ∗ P

    Journal: BioMed Research International

    Article Title: Adoptive Transfers of CD4+CD25+ Tregs Raise Foxp3 Expression and Alleviate Mouse Enteritis

    doi: 10.1155/2018/9064073

    Figure Lengend Snippet: Expression of Smad3, NFAT2, and Stat3 in the duodenum . (a) The results of Smad3, NFAT2, and Stat3 western blot analysis. (b) The average optical density (AOD) of Smad3, NFAT2, and Stat3 in the duodenum was analysed using immunohistochemistry. The sections are represented as a percentage of the total duodenum (200×). Results represent 1 experiment repeated 3 times. Six mice per group were used in the study. ∗ P

    Article Snippet: The appropriate amounts of rat anti-Smad3, NFAT2, and Stat3 mAb (Abcam, USK) were added and blocked in the shaker for 2.5 hours at 37°C.

    Techniques: Expressing, Western Blot, Immunohistochemistry, Mouse Assay

    Effect of vitamin C on cell proliferation in the GES-1 and AGS cell lines. Cells were treated with vitamin C at concentrations of 10 −9 , 10 −8 , 10 −7 and 10 −6 mol/l and (A) GES-1 and (C) AGS cell viability was assessed by the Cell Counting Kit-8 method at 0, 24, 48 and 72 h. In addition, (B) GES-1 and (D) AGS cells were treated with vitamin C at concentrations of 10 −7 and 10 −6 mol/l for 48 h, and the expression levels of p-STAT3 and PCNA were quantified via western blot analysis. **P

    Journal: Oncology Letters

    Article Title: Upregulation of TMEFF2 is involved in the antiproliferative effects of vitamin C and tyrphostin AG490 on GES-1 and AGS cells

    doi: 10.3892/ol.2018.9619

    Figure Lengend Snippet: Effect of vitamin C on cell proliferation in the GES-1 and AGS cell lines. Cells were treated with vitamin C at concentrations of 10 −9 , 10 −8 , 10 −7 and 10 −6 mol/l and (A) GES-1 and (C) AGS cell viability was assessed by the Cell Counting Kit-8 method at 0, 24, 48 and 72 h. In addition, (B) GES-1 and (D) AGS cells were treated with vitamin C at concentrations of 10 −7 and 10 −6 mol/l for 48 h, and the expression levels of p-STAT3 and PCNA were quantified via western blot analysis. **P

    Article Snippet: The following antibodies were adopted: A TMEFF2 antibody (1 µg/ml, Ab50002; Abcam), a PCNA antibody (1:1,000 dilution, cat. no: 13110, CST), a STAT3 antibody (1:100 dilution, Ab50761; Abcam), a p-STAT3 antibody (1:200,000 dilution, cat. no: Ab76315, Abcam), and a GAPDH antibody (1:2,000 dilution, cat. no: 5174; Cell Signaling Technology, Inc., Danvers, MA, USA).

    Techniques: Cell Counting, Expressing, Western Blot

    Schematic representation indicates that gemcitabine-erlotinib combination inhibits recurrent pancreatic tumor growth via JAK/STAT signaling. The gemcitabine-erlotinib combination significantly suppressed the phosphorylation levels of JAK1, JAK2, JAK3 as well as downstream STAT3 and STAT1 and eventually inhibited the growth of recurrent pancreatic tumors.

    Journal: Oncology Reports

    Article Title: Combination of gemcitabine and erlotinib inhibits recurrent pancreatic cancer growth in mice via the JAK-STAT pathway

    doi: 10.3892/or.2018.6198

    Figure Lengend Snippet: Schematic representation indicates that gemcitabine-erlotinib combination inhibits recurrent pancreatic tumor growth via JAK/STAT signaling. The gemcitabine-erlotinib combination significantly suppressed the phosphorylation levels of JAK1, JAK2, JAK3 as well as downstream STAT3 and STAT1 and eventually inhibited the growth of recurrent pancreatic tumors.

    Article Snippet: The following primary antibodies were used: anti-JAK1 (rabbit polyclonal; cat. no. AF5012), phospho-JAK1 (Tyr1022 ) (rabbit polyclonal; cat. no. AF2012), anti-JAK2 (rabbit polyclonal; cat. no. AF6022), phospho-JAK2 (Tyr221 ) (rabbit polyclonal; cat. no. AF3023), anti-JAK3 (mouse monoclonal; cat. no. BF0256), phospho-JAK3 (Tyr981 ) (rabbit polyclonal; cat. no. AF8160), phospho-STAT1 (Tyr701 ) (rabbit polyclonal; cat. no. AF3300) and anti-STAT1 (rabbit polyclonal; cat. no. AF6300) were all purchased from Affinity Biosciences (Cambridge, UK); anti-STAT3 (rabbit monoclonal; cat. no. ab76315), and anti-pSTAT3 Try705 (rabbit monoclonal; cat. no. ab68153) were obtained from Abcam (Cambridge, MA, USA); anti-HIF-1α (rabbit polyclonal; cat. no. BS3514) and anti-cyclin D1 (rabbit polyclonal; cat. no. BS6532) were purchased from Bioworld Technology Co., Ltd. (Nanjing, China); anti-p53 (rabbit, monoclonal; cat. no. 2527) was acquired from Cell Signaling Technology, Inc. (Danvers, MA, USA); while GAPDH was purchased from EarthOx Life Sciences (Millbrae, CA, USA).

    Techniques:

    The gemcitabine-erlotinib (E+G) combination group inhibits the activity of the JAK-STAT pathway, as well as the expression of downstream HIF-1α, cyclin D1 and p53. (A and B) The protein levels of phosphorylated STAT3 Tyr 705 (p-STAT3 Tyr 705 ), HIF-1α, p53, cyclin D1 in BxPC-3 and PANC-1 cells were analyzed by western blotting, respectively. (C and D) The protein expression of p-STAT3 Tyr 705 , HIF-1α, p53, cyclin D1 in BxPC-3 and PANC-1 cells was calculated using one-way ANOVA. *P

    Journal: Oncology Reports

    Article Title: Combination of gemcitabine and erlotinib inhibits recurrent pancreatic cancer growth in mice via the JAK-STAT pathway

    doi: 10.3892/or.2018.6198

    Figure Lengend Snippet: The gemcitabine-erlotinib (E+G) combination group inhibits the activity of the JAK-STAT pathway, as well as the expression of downstream HIF-1α, cyclin D1 and p53. (A and B) The protein levels of phosphorylated STAT3 Tyr 705 (p-STAT3 Tyr 705 ), HIF-1α, p53, cyclin D1 in BxPC-3 and PANC-1 cells were analyzed by western blotting, respectively. (C and D) The protein expression of p-STAT3 Tyr 705 , HIF-1α, p53, cyclin D1 in BxPC-3 and PANC-1 cells was calculated using one-way ANOVA. *P

    Article Snippet: The following primary antibodies were used: anti-JAK1 (rabbit polyclonal; cat. no. AF5012), phospho-JAK1 (Tyr1022 ) (rabbit polyclonal; cat. no. AF2012), anti-JAK2 (rabbit polyclonal; cat. no. AF6022), phospho-JAK2 (Tyr221 ) (rabbit polyclonal; cat. no. AF3023), anti-JAK3 (mouse monoclonal; cat. no. BF0256), phospho-JAK3 (Tyr981 ) (rabbit polyclonal; cat. no. AF8160), phospho-STAT1 (Tyr701 ) (rabbit polyclonal; cat. no. AF3300) and anti-STAT1 (rabbit polyclonal; cat. no. AF6300) were all purchased from Affinity Biosciences (Cambridge, UK); anti-STAT3 (rabbit monoclonal; cat. no. ab76315), and anti-pSTAT3 Try705 (rabbit monoclonal; cat. no. ab68153) were obtained from Abcam (Cambridge, MA, USA); anti-HIF-1α (rabbit polyclonal; cat. no. BS3514) and anti-cyclin D1 (rabbit polyclonal; cat. no. BS6532) were purchased from Bioworld Technology Co., Ltd. (Nanjing, China); anti-p53 (rabbit, monoclonal; cat. no. 2527) was acquired from Cell Signaling Technology, Inc. (Danvers, MA, USA); while GAPDH was purchased from EarthOx Life Sciences (Millbrae, CA, USA).

    Techniques: Activity Assay, Expressing, Western Blot