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rabbit monoclonal anti pstat3 s727 antibody  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit monoclonal anti pstat3 s727 antibody
    Sialin interacts with <t>pSTAT3</t> <t>S727</t> and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1
    Rabbit Monoclonal Anti Pstat3 S727 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+monoclonal+antibody+phospho+stat3/Phospho-Stat3+(Ser727)+Rabbit+mAb/pmc12887030-275-33-39
    Average 95 stars, based on 78 article reviews
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    Images

    1) Product Images from "Sialin-STAT3 axis regulates bone homeostasis in mice"

    Article Title: Sialin-STAT3 axis regulates bone homeostasis in mice

    Journal: Bone Research

    doi: 10.1038/s41413-025-00504-2

    Sialin interacts with pSTAT3 S727 and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1
    Figure Legend Snippet: Sialin interacts with pSTAT3 S727 and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1

    Techniques Used: Translocation Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, SPR Assay, Binding Assay, Staining, Quantitation Assay, Control

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    Article Snippet: Rabbit monoclonal antibody Phospho-Stat3 (Tyr705, batch number 91455) was purchased from Cell Signaling Technology.



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    Cell Signaling Technology Inc rabbit monoclonal anti pstat3 s727 antibody
    Sialin interacts with <t>pSTAT3</t> <t>S727</t> and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1
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    Sialin interacts with <t>pSTAT3</t> <t>S727</t> and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1
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    Src kinase regulates Ndrg1 transcription via the <t>Stat3-Hif1α</t> signaling pathway . A , silencing Hif1α decreases Ndrg1 expression. B , stabilization of Hif1α by CoCl 2 upregulates Ndrg1 expression. Huh-7.5 cells were treated with CoCl 2 (150 μM, 24 h). Right: quantification of Ndrg1 protein levels relative to control. C , Hif1α expression is not reduced in Src-KO cells. Huh-7.5, Src-KO#1, and Src-KO#2 cells were either infected or left uninfected with HCV (MOI = 5) for 72 h, followed by immunoblot analysis. Hif1α levels remained comparable across all cell lines. CoCl 2 treatment (150 μM) served as a positive control for Hif1α stabilization. D , Src knockout reduces Stat3 <t>Tyr705</t> phosphorylation. Densitometric ratios normalized to Huh-7.5 control are indicated below each blot. E . Loss of Src kinase disrupts the interaction between Hif1α and Stat3. The Stat3-Hif1α interaction was markedly reduced in both Src-KO clones. F . Ndrg1 expression is decreased in Stat3-KO cells. Loss of Stat3 significantly reduced Ndrg1 levels without altering Hif1α abundance. G , Stat3 is required for CoCl 2 -induced upregulation of Ndrg1. Stat3-KO#1, and Stat3-KO#2 cells were treated with or without CoCl 2 (150 μM, 24 h). CoCl 2 -mediated induction of Ndrg1 was abolished in Stat3-KO cells. Data represent the mean ± SD of three independent biological replicates. Statistical significance was analyzed using Welch’s t test. ∗ p < 0.05, ns, not significant.
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    Src kinase regulates Ndrg1 transcription via the <t>Stat3-Hif1α</t> signaling pathway . A , silencing Hif1α decreases Ndrg1 expression. B , stabilization of Hif1α by CoCl 2 upregulates Ndrg1 expression. Huh-7.5 cells were treated with CoCl 2 (150 μM, 24 h). Right: quantification of Ndrg1 protein levels relative to control. C , Hif1α expression is not reduced in Src-KO cells. Huh-7.5, Src-KO#1, and Src-KO#2 cells were either infected or left uninfected with HCV (MOI = 5) for 72 h, followed by immunoblot analysis. Hif1α levels remained comparable across all cell lines. CoCl 2 treatment (150 μM) served as a positive control for Hif1α stabilization. D , Src knockout reduces Stat3 <t>Tyr705</t> phosphorylation. Densitometric ratios normalized to Huh-7.5 control are indicated below each blot. E . Loss of Src kinase disrupts the interaction between Hif1α and Stat3. The Stat3-Hif1α interaction was markedly reduced in both Src-KO clones. F . Ndrg1 expression is decreased in Stat3-KO cells. Loss of Stat3 significantly reduced Ndrg1 levels without altering Hif1α abundance. G , Stat3 is required for CoCl 2 -induced upregulation of Ndrg1. Stat3-KO#1, and Stat3-KO#2 cells were treated with or without CoCl 2 (150 μM, 24 h). CoCl 2 -mediated induction of Ndrg1 was abolished in Stat3-KO cells. Data represent the mean ± SD of three independent biological replicates. Statistical significance was analyzed using Welch’s t test. ∗ p < 0.05, ns, not significant.
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    Cell Signaling Technology Inc rabbit monoclonal phospho stat3 tyr705 antibody
    Src kinase regulates Ndrg1 transcription via the <t>Stat3-Hif1α</t> signaling pathway . A , silencing Hif1α decreases Ndrg1 expression. B , stabilization of Hif1α by CoCl 2 upregulates Ndrg1 expression. Huh-7.5 cells were treated with CoCl 2 (150 μM, 24 h). Right: quantification of Ndrg1 protein levels relative to control. C , Hif1α expression is not reduced in Src-KO cells. Huh-7.5, Src-KO#1, and Src-KO#2 cells were either infected or left uninfected with HCV (MOI = 5) for 72 h, followed by immunoblot analysis. Hif1α levels remained comparable across all cell lines. CoCl 2 treatment (150 μM) served as a positive control for Hif1α stabilization. D , Src knockout reduces Stat3 <t>Tyr705</t> phosphorylation. Densitometric ratios normalized to Huh-7.5 control are indicated below each blot. E . Loss of Src kinase disrupts the interaction between Hif1α and Stat3. The Stat3-Hif1α interaction was markedly reduced in both Src-KO clones. F . Ndrg1 expression is decreased in Stat3-KO cells. Loss of Stat3 significantly reduced Ndrg1 levels without altering Hif1α abundance. G , Stat3 is required for CoCl 2 -induced upregulation of Ndrg1. Stat3-KO#1, and Stat3-KO#2 cells were treated with or without CoCl 2 (150 μM, 24 h). CoCl 2 -mediated induction of Ndrg1 was abolished in Stat3-KO cells. Data represent the mean ± SD of three independent biological replicates. Statistical significance was analyzed using Welch’s t test. ∗ p < 0.05, ns, not significant.
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    Cell Signaling Technology Inc anti pstat3 mouse monoclonal antibody
    Immunohistochemical analysis of SOX7, SOX17, SOX18, SOX30, MEF2C, VCAM1, and p-STAT3 expression in non-malignant lung tissue (NMLT; n = 55) and non-small-cell lung cancer (NSCLC) samples, including squamous cell carcinoma (LSCC; n = 400) and adenocarcinoma (LUAD; n = 400). All analyzed markers demonstrated nuclear, cytoplasmic, and endothelial localization ( A1 – G4 ). With the exception of SOX30, all markers showed significantly increased expression in the nuclear and endothelial compartments of both LSCC and LUAD samples compared with NMLT ( p < 0.0001). Subfigures ( A5 – G5 ) present the quantitative immunoreactivity scores (IRS ± SD) for the corresponding markers: ( A5 ) SOX7, ( B5 ) SOX17, ( C5 ) SOX18, ( D5 ) SOX30, ( E5 ) MEF2C, ( F5 ) VCAM1, and ( G5 ) <t>phosphorylated</t> <t>STAT3</t> (p-STAT3) in NMLT, LSCC, and LUAD. Statistical significance is indicated as p < 0.05 (*), p < 0.01 (**), and p < 0.0001 (****). Arrows indicate representative positively stained endothelial cells. Original magnification: ×200.
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    Image Search Results


    Sialin interacts with pSTAT3 S727 and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1

    Journal: Bone Research

    Article Title: Sialin-STAT3 axis regulates bone homeostasis in mice

    doi: 10.1038/s41413-025-00504-2

    Figure Lengend Snippet: Sialin interacts with pSTAT3 S727 and promotes its mitochondrial translocation in MSCs. a Gene Ontology biological process (GO-BP) enrichment analysis of the differentially phosphorylated proteins. b Dual-view hierarchical graph learning model predicts the interaction between Sialin and candidate proteins. c Co-immunoprecipitation (Co-IP) showing the interaction between Sialin and pSTAT3 S727 in hMSCs. d Surface plasmon resonance (SPR) analysis confirming the direct binding between Sialin and pSTAT3 S727 in hMSCs (KD = 683 nmol/L). e IF staining images and quantitation of pSTAT3 S727 colocalization with mitochondria by Pearson’s correlation coefficient in control, Sialin-overexpressing (HA- SLC17A5 ), and mitochondria-targeted Sialin-overexpressing (HA-Mito- SLC17A5 ) hMSCs. Scale bars, 10 μm. f A schematic model: Sialin binds pSTAT3 S727 , promotes its translocation to mitochondria, and thereby activates mitochondrial function in hMSCs. Data are presented as the mean ± SD, n = 3, except for f ( n = 30). **** P < 0.000 1

    Article Snippet: Proteins were incubated with IgG (control), Sialin, or pSTAT3 S727 conjugated Dynabeads (Life Technologies) at room temperature for 4 h. Following several antibody tests, the rabbit polyclonal anti-Sialin antibody from Thermo and the rabbit monoclonal anti-pSTAT3 S727 antibody from CST yielded efficient immunoprecipitation results.

    Techniques: Translocation Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, SPR Assay, Binding Assay, Staining, Quantitation Assay, Control

    Src kinase regulates Ndrg1 transcription via the Stat3-Hif1α signaling pathway . A , silencing Hif1α decreases Ndrg1 expression. B , stabilization of Hif1α by CoCl 2 upregulates Ndrg1 expression. Huh-7.5 cells were treated with CoCl 2 (150 μM, 24 h). Right: quantification of Ndrg1 protein levels relative to control. C , Hif1α expression is not reduced in Src-KO cells. Huh-7.5, Src-KO#1, and Src-KO#2 cells were either infected or left uninfected with HCV (MOI = 5) for 72 h, followed by immunoblot analysis. Hif1α levels remained comparable across all cell lines. CoCl 2 treatment (150 μM) served as a positive control for Hif1α stabilization. D , Src knockout reduces Stat3 Tyr705 phosphorylation. Densitometric ratios normalized to Huh-7.5 control are indicated below each blot. E . Loss of Src kinase disrupts the interaction between Hif1α and Stat3. The Stat3-Hif1α interaction was markedly reduced in both Src-KO clones. F . Ndrg1 expression is decreased in Stat3-KO cells. Loss of Stat3 significantly reduced Ndrg1 levels without altering Hif1α abundance. G , Stat3 is required for CoCl 2 -induced upregulation of Ndrg1. Stat3-KO#1, and Stat3-KO#2 cells were treated with or without CoCl 2 (150 μM, 24 h). CoCl 2 -mediated induction of Ndrg1 was abolished in Stat3-KO cells. Data represent the mean ± SD of three independent biological replicates. Statistical significance was analyzed using Welch’s t test. ∗ p < 0.05, ns, not significant.

    Journal: The Journal of Biological Chemistry

    Article Title: Protein tyrosine kinase Src suppresses hepatitis C virus particle release through regulation of Ndrg1

    doi: 10.1016/j.jbc.2025.111125

    Figure Lengend Snippet: Src kinase regulates Ndrg1 transcription via the Stat3-Hif1α signaling pathway . A , silencing Hif1α decreases Ndrg1 expression. B , stabilization of Hif1α by CoCl 2 upregulates Ndrg1 expression. Huh-7.5 cells were treated with CoCl 2 (150 μM, 24 h). Right: quantification of Ndrg1 protein levels relative to control. C , Hif1α expression is not reduced in Src-KO cells. Huh-7.5, Src-KO#1, and Src-KO#2 cells were either infected or left uninfected with HCV (MOI = 5) for 72 h, followed by immunoblot analysis. Hif1α levels remained comparable across all cell lines. CoCl 2 treatment (150 μM) served as a positive control for Hif1α stabilization. D , Src knockout reduces Stat3 Tyr705 phosphorylation. Densitometric ratios normalized to Huh-7.5 control are indicated below each blot. E . Loss of Src kinase disrupts the interaction between Hif1α and Stat3. The Stat3-Hif1α interaction was markedly reduced in both Src-KO clones. F . Ndrg1 expression is decreased in Stat3-KO cells. Loss of Stat3 significantly reduced Ndrg1 levels without altering Hif1α abundance. G , Stat3 is required for CoCl 2 -induced upregulation of Ndrg1. Stat3-KO#1, and Stat3-KO#2 cells were treated with or without CoCl 2 (150 μM, 24 h). CoCl 2 -mediated induction of Ndrg1 was abolished in Stat3-KO cells. Data represent the mean ± SD of three independent biological replicates. Statistical significance was analyzed using Welch’s t test. ∗ p < 0.05, ns, not significant.

    Article Snippet: Anti-HCV core monoclonal antibody (Abcam, catalog number: ab2740, lot number: 1076091–2), anti-NS3 polyclonal antibody (GeneTex, catalog number: GTX131276, lot number: 41,836), anti-Src monoclonal antibody (Cell signaling, catalog number: 2123, lot number: 5), anti-Ndrg1 polyclonal antibody (Proteintech, catalog number: 26902-1-AP, lot number: 00050845), anti-Hif1α polyclonal antibody (Proteintech, catalog number: 20960-1-AP, lot number: 00149455), anti-Stat3 polyclonal antibody (Santa Cruz, catalog number: sc-7179, lot number: A069), anti-Stat3 monoclonal antibody (Cell signaling, catalog number: 4904P, lot number: 7), anti-phospho-Stat3 (Tyr705) monoclonal antibody (Cell signaling, catalog number: 9145, lot number: 43), anti-β-actin monoclonal antibody (Santa Cruz, catalog number: sc-47778, lot number: l2822), and anti-mouse IgG(H + L), F(ab’) 2 fragment (Cell signaling, Alexa Fluor 488 conjugate, catalog number: 4408, lot number: 24) were used in this study.

    Techniques: Expressing, Control, Infection, Western Blot, Positive Control, Knock-Out, Phospho-proteomics, Clone Assay

    Immunohistochemical analysis of SOX7, SOX17, SOX18, SOX30, MEF2C, VCAM1, and p-STAT3 expression in non-malignant lung tissue (NMLT; n = 55) and non-small-cell lung cancer (NSCLC) samples, including squamous cell carcinoma (LSCC; n = 400) and adenocarcinoma (LUAD; n = 400). All analyzed markers demonstrated nuclear, cytoplasmic, and endothelial localization ( A1 – G4 ). With the exception of SOX30, all markers showed significantly increased expression in the nuclear and endothelial compartments of both LSCC and LUAD samples compared with NMLT ( p < 0.0001). Subfigures ( A5 – G5 ) present the quantitative immunoreactivity scores (IRS ± SD) for the corresponding markers: ( A5 ) SOX7, ( B5 ) SOX17, ( C5 ) SOX18, ( D5 ) SOX30, ( E5 ) MEF2C, ( F5 ) VCAM1, and ( G5 ) phosphorylated STAT3 (p-STAT3) in NMLT, LSCC, and LUAD. Statistical significance is indicated as p < 0.05 (*), p < 0.01 (**), and p < 0.0001 (****). Arrows indicate representative positively stained endothelial cells. Original magnification: ×200.

    Journal: International Journal of Molecular Sciences

    Article Title: SOX18 and SOX30 in NSCLC: The Epigenetic Landscape of Methylation, miRNA Regulation, and Network Crosstalk in Tumor Progression

    doi: 10.3390/ijms262311669

    Figure Lengend Snippet: Immunohistochemical analysis of SOX7, SOX17, SOX18, SOX30, MEF2C, VCAM1, and p-STAT3 expression in non-malignant lung tissue (NMLT; n = 55) and non-small-cell lung cancer (NSCLC) samples, including squamous cell carcinoma (LSCC; n = 400) and adenocarcinoma (LUAD; n = 400). All analyzed markers demonstrated nuclear, cytoplasmic, and endothelial localization ( A1 – G4 ). With the exception of SOX30, all markers showed significantly increased expression in the nuclear and endothelial compartments of both LSCC and LUAD samples compared with NMLT ( p < 0.0001). Subfigures ( A5 – G5 ) present the quantitative immunoreactivity scores (IRS ± SD) for the corresponding markers: ( A5 ) SOX7, ( B5 ) SOX17, ( C5 ) SOX18, ( D5 ) SOX30, ( E5 ) MEF2C, ( F5 ) VCAM1, and ( G5 ) phosphorylated STAT3 (p-STAT3) in NMLT, LSCC, and LUAD. Statistical significance is indicated as p < 0.05 (*), p < 0.01 (**), and p < 0.0001 (****). Arrows indicate representative positively stained endothelial cells. Original magnification: ×200.

    Article Snippet: The following antibodies were used for the immunohistochemical examination of the markers: rabbit polyclonal antibody against SOX7 (1:500; ab94397, Abcam, Cambridge, UK), rabbit monoclonal antibody against SOX17 (1:400, ab224637, Abcam, Cambridge, UK), mouse monoclonal antibody against SOX18 (1:500, sc-166025, SantaCruz, Dallas, TX, USA), anti-SOX30 rabbit polyclonal antibody (1:200, NBP1-86503, NovusBio, Centennial, CO, USA), anti-MEF2C rabbit polyclonal antibody (1:200, HPA005533, SigmaAldrich, Louis, MO, USA), anti-VCAM1 rabbit polyclonal antibody (1:200, 11444-1-AP, ProteinTech, Rosemont, IL, USA) and anti-pSTAT3 mouse monoclonal antibody (1:200, #9145, Cell Signaling, Danvers, MA, USA).

    Techniques: Immunohistochemical staining, Expressing, Staining