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anti beta actin antibody  (Proteintech)


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    Structured Review

    Proteintech anti beta actin antibody
    Anti Beta Actin Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 2606 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hrp+conjugated+beta+actin/HRP-conjugated+beta+Actin+Antibody/pmc13669683-464-19-21
    Average 96 stars, based on 2606 article reviews
    anti beta actin antibody - by Bioz Stars, 2026-11
    96/100 stars

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    Related Articles

    Western Blot:

    Article Title: Microbial metabolite restricts 5-fluorouracil-resistant colonic tumor progression by sensitizing drug transporters via regulation of FOXO3-FOXM1 axis
    Article Snippet: HRP-Conjugated GAPDH , ProteinTech , HRP-60004 , WB , . .. HRP-Conjugated Beta Actin , ProteinTech , HRP-60008 , WB , 1:5000. .. Goat anti-mouse IgG (H+L), HRP conjugate , ProteinTech , SA00001-1 , WB , 1:5000.

    Article Title: Membrane-bound O -acyltransferase 7 (MBOAT7) shapes lysosomal lipid homeostasis and function to control alcohol-associated liver injury
    Article Snippet: Antibody , Lamin A/C (4C11) (Mouse monoclonal) , Cell Signaling , Cat#: 4777 , WB (1:1000). .. Antibody , HRP-conjugated Beta Actin (Mouse monoclonal) , Proteintech , Cat#: HRP-60008 RRID: AB_2289225 , WB (1:10,000). .. Commercial assay or kit , Alanine Aminotransaminase (ALT) kit , Sekisui Diagnostics , 318-30 , .

    Article Title: AARS2 ameliorates myocardial ischemia via fine-tuning PKM2-mediated metabolism
    Article Snippet: Antibody , HRP-conjugated GAPDH , Proteintech , HRP-60004 RRID: AB_2737588 , WB (1:10000). .. Antibody , HRP-conjugated Beta Actin , Proteintech , HRP-60008 RRID: AB_2819183 , WB (1:10000). .. Antibody , HRP-conjugated Alpha Tubulin , Proteintech , HRP-66031 RRID: AB_2687491 , WB (1:10000).

    other:

    Article Title: Unveiling the STAT3-ACC1 axis: a key driver of lipid metabolism and tumor progression in non-small cell lung cancer
    Article Snippet: The subsequent antibodies were commercially obtained as follows: mouse anti-STAT3 (9139S, CST), rabbit anti-ACC1 (A19627, ABclonal), goat anti-rabbit IgG (H+L), HRP conjugated (SA00001-2, Proteintech), goat anti-mouse IgG (H+L), HRP conjugated (SA00001-1, Proteintech), and HRP-conjugated beta actin (HRP-60008, Proteintech).

    Article Title: Unveiling the STAT3-ACC1 axis: a key driver of lipid metabolism and tumor progression in non-small cell lung cancer.
    Article Snippet: The subsequent antibodies were commercially obtained as follows: mouse anti-STAT3 (9139S, CST), rabbit anti-ACC1 (A19627, ABclonal), goat anti-rabbit IgG (H+L), HRP conjugated (SA00001-2, Proteintech), goat anti-mouse IgG (H+L), HRP conjugated (SA00001-1, Proteintech), and HRP-conjugated beta actin (HRP-60008, Proteintech).

    Article Title: Targeting pancreatic cancer glutamine dependency confers vulnerability to GPX4-dependent ferroptosis
    Article Snippet: HRP-conjugated Beta Actin , Proteintech , Cat# HRP-60008; RRID: AB_2819183.



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    ABclonal Biotechnology β actin
    sgp130Fc treatment attenuates benzalkonium chloride (BAC)-mediated oxidative imbalance in human telomerase-immortalized corneal epithelial (hTCEpi) cells. a BAC-induced increases in total reactive oxygen species (ROS) levels were partially reduced by sgp130Fc treatment. 100 µM pyocyanin was used as a positive control. b Similarly, increased levels of hydrogen peroxide (H 2 O 2 ) in BAC-treated hTCEpi cells were mitigated by sgp130Fc treatment. c – f sgp130Fc prevented the BAC-induced decrease in gene expression of several antioxidant enzymes ( SOD1 , PRDX1 , and PRDX2 ) and reduction of total peroxiredoxin (PRDX) protein levels. <t>β-actin</t> is used as loading control. g – j A similar trend was observed for GPX1 , GPX4 , and TXN gene expression and catalase protein levels under these treatment conditions. β-actin was used as a loading control. k sgp130Fc treatment also restored total antioxidant capacity, measured in mM TE (Trolox equivalents), in BAC-treated hTCEpi cells. Data are represented as mean ± standard error of the mean, n = 3–23/group; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001
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    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
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    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
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    Proteintech anti beta actin antibody
    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
    Anti Beta Actin Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Proteintech anti β actin
    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
    Anti β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology hrp conjugated anti beta actin antibody
    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
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    ABclonal Biotechnology anti β actin
    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
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    Proteintech hrp conjugated anti mouse
    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
    Hrp Conjugated Anti Mouse, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ABclonal Biotechnology hrp conjugated β actin
    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to <t>β-actin).</t> ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
    Hrp Conjugated β Actin, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    sgp130Fc treatment attenuates benzalkonium chloride (BAC)-mediated oxidative imbalance in human telomerase-immortalized corneal epithelial (hTCEpi) cells. a BAC-induced increases in total reactive oxygen species (ROS) levels were partially reduced by sgp130Fc treatment. 100 µM pyocyanin was used as a positive control. b Similarly, increased levels of hydrogen peroxide (H 2 O 2 ) in BAC-treated hTCEpi cells were mitigated by sgp130Fc treatment. c – f sgp130Fc prevented the BAC-induced decrease in gene expression of several antioxidant enzymes ( SOD1 , PRDX1 , and PRDX2 ) and reduction of total peroxiredoxin (PRDX) protein levels. β-actin is used as loading control. g – j A similar trend was observed for GPX1 , GPX4 , and TXN gene expression and catalase protein levels under these treatment conditions. β-actin was used as a loading control. k sgp130Fc treatment also restored total antioxidant capacity, measured in mM TE (Trolox equivalents), in BAC-treated hTCEpi cells. Data are represented as mean ± standard error of the mean, n = 3–23/group; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001

    Journal: Eye and Vision

    Article Title: Blocking IL-6 trans-signaling mitigates benzalkonium chloride-induced inflammation, oxidative imbalance, ER stress, and barrier disruption in human corneal epithelial cells

    doi: 10.1186/s40662-026-00513-0

    Figure Lengend Snippet: sgp130Fc treatment attenuates benzalkonium chloride (BAC)-mediated oxidative imbalance in human telomerase-immortalized corneal epithelial (hTCEpi) cells. a BAC-induced increases in total reactive oxygen species (ROS) levels were partially reduced by sgp130Fc treatment. 100 µM pyocyanin was used as a positive control. b Similarly, increased levels of hydrogen peroxide (H 2 O 2 ) in BAC-treated hTCEpi cells were mitigated by sgp130Fc treatment. c – f sgp130Fc prevented the BAC-induced decrease in gene expression of several antioxidant enzymes ( SOD1 , PRDX1 , and PRDX2 ) and reduction of total peroxiredoxin (PRDX) protein levels. β-actin is used as loading control. g – j A similar trend was observed for GPX1 , GPX4 , and TXN gene expression and catalase protein levels under these treatment conditions. β-actin was used as a loading control. k sgp130Fc treatment also restored total antioxidant capacity, measured in mM TE (Trolox equivalents), in BAC-treated hTCEpi cells. Data are represented as mean ± standard error of the mean, n = 3–23/group; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001

    Article Snippet: The following primary antibodies were used: PRDX (1:100, #sc-137222, Santa Cruz Biotechnology), Catalase (1:250, #sc-271803, Santa Cruz Biotechnology), BiP (1:1000, #A0241, ABclonal), PERK (1:1000, #5683, Cell Signaling), Ero1α (1:1000, #3264, Cell Signaling), β-catenin (1:500, #8480S, Cell Signaling), Occludin (1:200, #40–4700, Invitrogen), Claudin-1 (1:1000, #A2196, ABclonal), IL-6R (1:1000, #A1570, ABclonal), gp130 (1:100, #sc-655, Santa Cruz Biotechnology), and β-actin (1:10,000, #AC028, ABclonal).

    Techniques: Positive Control, Gene Expression, Control

    Interleukin-6 (IL-6) trans-signaling elevates intracellular calcium levels and endoplasmic reticulum (ER) stress in benzalkonium chloride (BAC)-treated human telomerase-immortalized corneal epithelial (hTCEpi) cells. a Intracellular Ca 2+ levels were significantly elevated after BAC exposure, while sgp130Fc treatment had a protective effect against BAC-mediated Ca 2+ flux. b , c Expression of cytosolic chaperone HSP72 and levels of ER chaperone binding immunoglobulin protein (BiP) were significantly increased by BAC but attenuated with sgp130Fc treatment. d , e BAC exposure led to elevated levels of protein kinase RNA-like endoplasmic reticulum kinase (PERK), a sensor of ER stress, and Ero1α, a downstream target of PERK; however, blocking IL-6 trans-signaling with sgp130Fc mitigated BAC-induced upregulation of these ER stress mediators. β-actin was used as a loading control. Data are represented as mean ± standard error of the mean, n = 3–14/group; * P < 0.05, ** P < 0.01, *** P < 0.001

    Journal: Eye and Vision

    Article Title: Blocking IL-6 trans-signaling mitigates benzalkonium chloride-induced inflammation, oxidative imbalance, ER stress, and barrier disruption in human corneal epithelial cells

    doi: 10.1186/s40662-026-00513-0

    Figure Lengend Snippet: Interleukin-6 (IL-6) trans-signaling elevates intracellular calcium levels and endoplasmic reticulum (ER) stress in benzalkonium chloride (BAC)-treated human telomerase-immortalized corneal epithelial (hTCEpi) cells. a Intracellular Ca 2+ levels were significantly elevated after BAC exposure, while sgp130Fc treatment had a protective effect against BAC-mediated Ca 2+ flux. b , c Expression of cytosolic chaperone HSP72 and levels of ER chaperone binding immunoglobulin protein (BiP) were significantly increased by BAC but attenuated with sgp130Fc treatment. d , e BAC exposure led to elevated levels of protein kinase RNA-like endoplasmic reticulum kinase (PERK), a sensor of ER stress, and Ero1α, a downstream target of PERK; however, blocking IL-6 trans-signaling with sgp130Fc mitigated BAC-induced upregulation of these ER stress mediators. β-actin was used as a loading control. Data are represented as mean ± standard error of the mean, n = 3–14/group; * P < 0.05, ** P < 0.01, *** P < 0.001

    Article Snippet: The following primary antibodies were used: PRDX (1:100, #sc-137222, Santa Cruz Biotechnology), Catalase (1:250, #sc-271803, Santa Cruz Biotechnology), BiP (1:1000, #A0241, ABclonal), PERK (1:1000, #5683, Cell Signaling), Ero1α (1:1000, #3264, Cell Signaling), β-catenin (1:500, #8480S, Cell Signaling), Occludin (1:200, #40–4700, Invitrogen), Claudin-1 (1:1000, #A2196, ABclonal), IL-6R (1:1000, #A1570, ABclonal), gp130 (1:100, #sc-655, Santa Cruz Biotechnology), and β-actin (1:10,000, #AC028, ABclonal).

    Techniques: Expressing, Binding Assay, Blocking Assay, Control, Gene Expression

    Benzalkonium chloride (BAC)-induced corneal epithelial barrier dysfunction is partially restored by sgp130Fc. a Trans-epithelial electrical resistance (TER) of human telomerase-immortalized corneal epithelial (hTCEpi) cell monolayers was monitored every 4 min for 60 min. BAC induced a progressive decline in TER reaching a 29% reduction at 60 min, whereas sgp130Fc partially prevented BAC-induced loss of barrier integrity. b Representative western blots of junctional proteins in hTCEpi cells. β-actin was used as a loading control. c Levels of β-catenin were significantly decreased with BAC treatment. d , e Levels of tight junction proteins, occludin and claudin-1, exhibited a similar decrease after BAC exposure. Inhibiting interleukin-6 trans-signaling with sgp130Fc showed partial protection against loss of these junctional proteins. Data are represented as mean ± standard error of the mean, n = 8–19/group; * P < 0.05, **** P < 0.0001

    Journal: Eye and Vision

    Article Title: Blocking IL-6 trans-signaling mitigates benzalkonium chloride-induced inflammation, oxidative imbalance, ER stress, and barrier disruption in human corneal epithelial cells

    doi: 10.1186/s40662-026-00513-0

    Figure Lengend Snippet: Benzalkonium chloride (BAC)-induced corneal epithelial barrier dysfunction is partially restored by sgp130Fc. a Trans-epithelial electrical resistance (TER) of human telomerase-immortalized corneal epithelial (hTCEpi) cell monolayers was monitored every 4 min for 60 min. BAC induced a progressive decline in TER reaching a 29% reduction at 60 min, whereas sgp130Fc partially prevented BAC-induced loss of barrier integrity. b Representative western blots of junctional proteins in hTCEpi cells. β-actin was used as a loading control. c Levels of β-catenin were significantly decreased with BAC treatment. d , e Levels of tight junction proteins, occludin and claudin-1, exhibited a similar decrease after BAC exposure. Inhibiting interleukin-6 trans-signaling with sgp130Fc showed partial protection against loss of these junctional proteins. Data are represented as mean ± standard error of the mean, n = 8–19/group; * P < 0.05, **** P < 0.0001

    Article Snippet: The following primary antibodies were used: PRDX (1:100, #sc-137222, Santa Cruz Biotechnology), Catalase (1:250, #sc-271803, Santa Cruz Biotechnology), BiP (1:1000, #A0241, ABclonal), PERK (1:1000, #5683, Cell Signaling), Ero1α (1:1000, #3264, Cell Signaling), β-catenin (1:500, #8480S, Cell Signaling), Occludin (1:200, #40–4700, Invitrogen), Claudin-1 (1:1000, #A2196, ABclonal), IL-6R (1:1000, #A1570, ABclonal), gp130 (1:100, #sc-655, Santa Cruz Biotechnology), and β-actin (1:10,000, #AC028, ABclonal).

    Techniques: Western Blot, Control

    KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to β-actin). ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

    Journal: Gut Microbes

    Article Title: Targeted intestinal ROS scavenging alleviated rheumatoid arthritis by microbial metabolite kynurenic acid mediated Treg/Th17 balance through AhR pathway activation

    doi: 10.1080/19490976.2026.2739669

    Figure Lengend Snippet: KYNA promoted Treg cell differentiation by suppressing mTORC1 activation through the AhR pathway. (A) Predicted binding mode of KYNA within the ligand-binding pocket of AhR. (B) The expression of FOXP3 in naïve CD4⁺ T cells cultured under TGF-β-induced conditions with different concentrations of KYNA, in the presence or absence of CH-223191, was detected by flow cytometry. (C) GSEA of the PI3K/AKT signaling pathway between the control and KYNA-treated groups. (D) Representative Western blot images of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 in the presence or absence of KYNA. (E) Western blot quantification of AKT, p-AKT, mTOR, p-mTOR, p70 S6K, p-p70 S6K, 4E-BP1, p-4E-BP1, and FOXP3 protein levels (normalized to β-actin). ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

    Article Snippet: HRP-conjugated β-actin antibody (ABclonal, Cat. no. AC028, 1:100,000) was used as a loading control.

    Techniques: Cell Differentiation, Activation Assay, Binding Assay, Ligand Binding Assay, Expressing, Cell Culture, Flow Cytometry, Control, Western Blot

    KYNA exerted anti-rheumatic arthritis effects in vivo through the AhR pathway. (A) Detailed schematic of the animal experimental procedures of CIA PBS , CIA KYNA and CIA KYNA+CH-223191 groups. (B) Arthritis scores in CIA mice. (C) Representative photographs and micro-CT images of paws. (D) Quantitative analyses of bone histomorphometry indexes including BMD, BV/TV, Tb.Th, Tb.Sp, and Tb.N in CIA mice. (E) Representative HE staining images of joints. Scale bar, 100 μm. (F) Histological scores of the joints. (G) Representative TRAP staining images of joints. Scale bar, 100 μm. (H) Quantitative analyses of TRAP staining. (I–L) Flow cytometric analysis and quantification of IL-17A⁺ Th17 cells and FOXP3⁺ Treg cells among CD4⁺ T cells, as well as the Treg/Th17 ratio, in the spleen and MLN. (M–P) (M and O), Representative immunofluorescence staining of ZO-1 and Occludin in colon tissue. Scale bar, 100 μm. (N and P) Quantification of the MFI of ZO-1 and Occludin after normalization. (Q) Representative Western blot images of ZO-1 and Occludin in the presence of KYNA or KYNA + CH-223191 in IEC-6 cells. (R and S) Western blot quantification of ZO-1 and Occludin protein levels (normalized to β-actin). ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

    Journal: Gut Microbes

    Article Title: Targeted intestinal ROS scavenging alleviated rheumatoid arthritis by microbial metabolite kynurenic acid mediated Treg/Th17 balance through AhR pathway activation

    doi: 10.1080/19490976.2026.2739669

    Figure Lengend Snippet: KYNA exerted anti-rheumatic arthritis effects in vivo through the AhR pathway. (A) Detailed schematic of the animal experimental procedures of CIA PBS , CIA KYNA and CIA KYNA+CH-223191 groups. (B) Arthritis scores in CIA mice. (C) Representative photographs and micro-CT images of paws. (D) Quantitative analyses of bone histomorphometry indexes including BMD, BV/TV, Tb.Th, Tb.Sp, and Tb.N in CIA mice. (E) Representative HE staining images of joints. Scale bar, 100 μm. (F) Histological scores of the joints. (G) Representative TRAP staining images of joints. Scale bar, 100 μm. (H) Quantitative analyses of TRAP staining. (I–L) Flow cytometric analysis and quantification of IL-17A⁺ Th17 cells and FOXP3⁺ Treg cells among CD4⁺ T cells, as well as the Treg/Th17 ratio, in the spleen and MLN. (M–P) (M and O), Representative immunofluorescence staining of ZO-1 and Occludin in colon tissue. Scale bar, 100 μm. (N and P) Quantification of the MFI of ZO-1 and Occludin after normalization. (Q) Representative Western blot images of ZO-1 and Occludin in the presence of KYNA or KYNA + CH-223191 in IEC-6 cells. (R and S) Western blot quantification of ZO-1 and Occludin protein levels (normalized to β-actin). ns, p ≥ 0.05; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

    Article Snippet: HRP-conjugated β-actin antibody (ABclonal, Cat. no. AC028, 1:100,000) was used as a loading control.

    Techniques: In Vivo, Micro-CT, H&E Stain, Staining, Analysis, Immunofluorescence, Tissue, Western Blot