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human il 1β  (R&D Systems)


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    R&D Systems human il 1β
    TMH inhibits activation of the NLRP3 inflammasome. (A) Schematic workflow of in vitro NLRP3 inflammasome activation. (B,C) Cell viability was assessed in J774A.1 cells (B) and PMA (500 nM)-differentiated THP-1 cells (C) treated with TMH for 2 or 18 h using the EZ-Cytox assay. (D) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with ATP (5 mM) for 30 min in the presence or absence of <t>MCC950.</t> <t>IL-1β</t> (p17) levels in supernatants were measured by ELISA. (E,F) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with ATP (5 mM) (E) or nigericin (10 μM) (F) for 1 h, with or without MCC950. IL-1β (p17) levels in supernatants were determined by ELISA. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001; n.s., not significant.
    Human Il 1β, supplied by R&D Systems, used in various techniques. Bioz Stars score: 97/100, based on 954 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+anti+human+mouse+il+1%CE%B2/Mouse+IL-1+beta%2FIL-1F2+Antibody/pmc13125143-61-3-13
    Average 97 stars, based on 954 article reviews
    human il 1β - by Bioz Stars, 2026-09
    97/100 stars

    Images

    1) Product Images from "Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity"

    Article Title: Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2026.1781860

    TMH inhibits activation of the NLRP3 inflammasome. (A) Schematic workflow of in vitro NLRP3 inflammasome activation. (B,C) Cell viability was assessed in J774A.1 cells (B) and PMA (500 nM)-differentiated THP-1 cells (C) treated with TMH for 2 or 18 h using the EZ-Cytox assay. (D) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with ATP (5 mM) for 30 min in the presence or absence of MCC950. IL-1β (p17) levels in supernatants were measured by ELISA. (E,F) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with ATP (5 mM) (E) or nigericin (10 μM) (F) for 1 h, with or without MCC950. IL-1β (p17) levels in supernatants were determined by ELISA. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001; n.s., not significant.
    Figure Legend Snippet: TMH inhibits activation of the NLRP3 inflammasome. (A) Schematic workflow of in vitro NLRP3 inflammasome activation. (B,C) Cell viability was assessed in J774A.1 cells (B) and PMA (500 nM)-differentiated THP-1 cells (C) treated with TMH for 2 or 18 h using the EZ-Cytox assay. (D) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with ATP (5 mM) for 30 min in the presence or absence of MCC950. IL-1β (p17) levels in supernatants were measured by ELISA. (E,F) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with ATP (5 mM) (E) or nigericin (10 μM) (F) for 1 h, with or without MCC950. IL-1β (p17) levels in supernatants were determined by ELISA. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001; n.s., not significant.

    Techniques Used: Activation Assay, In Vitro, Enzyme-linked Immunosorbent Assay

    TMH does not affect other inflammasome or inflammatory pathways. (A,B) LPS-primed J774A.1 cells were treated with TMH for 2 h, followed by stimulation with either dsDNA (1 μg/mL) (A) or flagellin (B) transfected using Lipofectamine 2000 for 3 h. (C) Following TMH treatment (2 h), nuclear and cytosolic fractions of LPS-primed J774A.1 cells were separated and assessed for NF-κB p65 translocation by immunoblotting. (D) HEK293FT cells transfected with the pGL4.32 luciferase reporter vector were treated with TNF-α (20 ng/mL) for 5 h, with or without TMH pre-treatment (2 h). Luciferase activity was measured using the Bright-Glo™ luciferase assay system (Promega). Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test n.s., not significant.
    Figure Legend Snippet: TMH does not affect other inflammasome or inflammatory pathways. (A,B) LPS-primed J774A.1 cells were treated with TMH for 2 h, followed by stimulation with either dsDNA (1 μg/mL) (A) or flagellin (B) transfected using Lipofectamine 2000 for 3 h. (C) Following TMH treatment (2 h), nuclear and cytosolic fractions of LPS-primed J774A.1 cells were separated and assessed for NF-κB p65 translocation by immunoblotting. (D) HEK293FT cells transfected with the pGL4.32 luciferase reporter vector were treated with TNF-α (20 ng/mL) for 5 h, with or without TMH pre-treatment (2 h). Luciferase activity was measured using the Bright-Glo™ luciferase assay system (Promega). Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test n.s., not significant.

    Techniques Used: Transfection, Translocation Assay, Western Blot, Luciferase, Plasmid Preparation, Activity Assay

    TMH inhibits NLRP3 inflammasome activation by suppressing ASC oligomerization and ATPase activity. (A) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with imiquimod (200 μM) for 1 h. (B) Cells were treated with TMH (2 h), stained with MitoSOX (5 μM, 10 min), and stimulated with ATP (5 mM, 5 min). Intracellular ROS were visualized by confocal microscopy. (C,D) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with nigericin (10 μM, 1 h). ASC speck formation was examined by confocal microscopy (C) , and representative images from five fields are shown (D) . (E) Cells were stimulated with or without MCC950 and cross-linked with DSS (2.5 mM, 30 min) before immunoblotting for ASC oligomerization. (F) NLRP3 ATPase activity was measured using the ADP-Glo™ assay to quantify ATP-to-ADP conversion following TMH treatment. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. **P < 0.01, ***P < 0.001.
    Figure Legend Snippet: TMH inhibits NLRP3 inflammasome activation by suppressing ASC oligomerization and ATPase activity. (A) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with imiquimod (200 μM) for 1 h. (B) Cells were treated with TMH (2 h), stained with MitoSOX (5 μM, 10 min), and stimulated with ATP (5 mM, 5 min). Intracellular ROS were visualized by confocal microscopy. (C,D) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with nigericin (10 μM, 1 h). ASC speck formation was examined by confocal microscopy (C) , and representative images from five fields are shown (D) . (E) Cells were stimulated with or without MCC950 and cross-linked with DSS (2.5 mM, 30 min) before immunoblotting for ASC oligomerization. (F) NLRP3 ATPase activity was measured using the ADP-Glo™ assay to quantify ATP-to-ADP conversion following TMH treatment. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. **P < 0.01, ***P < 0.001.

    Techniques Used: Activation Assay, Activity Assay, Staining, Confocal Microscopy, Western Blot, Glo Assay

    Toxicity assessment of TMH in zebrafish embryos. (A) Survival curves of zebrafish embryos treated with TMH at concentrations of 1, 10, or 100 μg/mL. Sixty embryos were used per condition and maintained in E3 medium. The control group was treated with DMSO (0.25%, v/v), corresponding to the highest TMH concentration. (B) Survival and phenotype distribution of 5 dpf embryos treated with TMH at distinct concentrations from 1 to 5 dpf. (C) Representative images showing developmental abnormalities observed in embryos treated with 10 μg/mL TMH at 5 dpf. (D) Representative images of Sudan Black B staining in 3 dpf embryos treated with vehicle control (0.0025% DMSO with PTU; upper panel) or TMH (1 μg/mL; lower panel). (E) Quantification of neutrophil counts in the CHT (red dashed outline) following treatment with TMH (1 μg/mL). Data are presented as mean ± SEM of individual embryos. Statistical significance was determined using an unpaired two-tailed Student’s t-test; n.s., not significant (p = 0.9997). Scale bars, 300 µm.
    Figure Legend Snippet: Toxicity assessment of TMH in zebrafish embryos. (A) Survival curves of zebrafish embryos treated with TMH at concentrations of 1, 10, or 100 μg/mL. Sixty embryos were used per condition and maintained in E3 medium. The control group was treated with DMSO (0.25%, v/v), corresponding to the highest TMH concentration. (B) Survival and phenotype distribution of 5 dpf embryos treated with TMH at distinct concentrations from 1 to 5 dpf. (C) Representative images showing developmental abnormalities observed in embryos treated with 10 μg/mL TMH at 5 dpf. (D) Representative images of Sudan Black B staining in 3 dpf embryos treated with vehicle control (0.0025% DMSO with PTU; upper panel) or TMH (1 μg/mL; lower panel). (E) Quantification of neutrophil counts in the CHT (red dashed outline) following treatment with TMH (1 μg/mL). Data are presented as mean ± SEM of individual embryos. Statistical significance was determined using an unpaired two-tailed Student’s t-test; n.s., not significant (p = 0.9997). Scale bars, 300 µm.

    Techniques Used: Control, Concentration Assay, Staining, Two Tailed Test

    TMH suppresses LPS-induced inflammatory cell recruitment in zebrafish embryos. (A) Representative images of neutrophil recruitment in the CHT in 3 dpf zebrafish embryos following LPS stimulation, assessed by Sudan Black B staining. Top panel: control embryos treated with 0.0025% DMSO (n = 29); middle panel: LPS-treated embryos (10 μg/mL; n = 32); bottom panel: embryos co-treated with LPS (10 μg/mL) and TMH (1 μg/mL; n = 33). (B) Quantification of neutrophil accumulation in the CHT following LPS stimulation with or without TMH treatment using Sudan Black B staining from (A) . (C) Representative images of whole-mount in situ hybridization showing mpx -positive neutrophils in 3 dpf embryos under LPS and TMH treatment conditions. Top panel (DMSO 0.0025%; n = 34); middle panel (LPS 10 μg/mL; n = 35); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 39). (D) Quantification of mpx -positive cells within the CHT from (C) . (E) Representative confocal images of macrophages in 3 dpf Tg ( mpeg1 :EGFP) zebrafish embryos following LPS and TMH treatment. Top panel (DMSO 0.0025%; n = 8); middle panel (LPS 10 μg/mL; n = 11); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 13). (F) Quantification of mpeg1 :EGFP-positive macrophages in the CHT region shown in (E) . Red dashed outline indicates the CHT. All data are presented as mean ± SEM. Statistical significance was determined using an unpaired two-tailed Student’s t-test. *P < 0.05; **P < 0.01; ***P < 0.05; ****P < 0.0001. Scale bars, 300 µm.
    Figure Legend Snippet: TMH suppresses LPS-induced inflammatory cell recruitment in zebrafish embryos. (A) Representative images of neutrophil recruitment in the CHT in 3 dpf zebrafish embryos following LPS stimulation, assessed by Sudan Black B staining. Top panel: control embryos treated with 0.0025% DMSO (n = 29); middle panel: LPS-treated embryos (10 μg/mL; n = 32); bottom panel: embryos co-treated with LPS (10 μg/mL) and TMH (1 μg/mL; n = 33). (B) Quantification of neutrophil accumulation in the CHT following LPS stimulation with or without TMH treatment using Sudan Black B staining from (A) . (C) Representative images of whole-mount in situ hybridization showing mpx -positive neutrophils in 3 dpf embryos under LPS and TMH treatment conditions. Top panel (DMSO 0.0025%; n = 34); middle panel (LPS 10 μg/mL; n = 35); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 39). (D) Quantification of mpx -positive cells within the CHT from (C) . (E) Representative confocal images of macrophages in 3 dpf Tg ( mpeg1 :EGFP) zebrafish embryos following LPS and TMH treatment. Top panel (DMSO 0.0025%; n = 8); middle panel (LPS 10 μg/mL; n = 11); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 13). (F) Quantification of mpeg1 :EGFP-positive macrophages in the CHT region shown in (E) . Red dashed outline indicates the CHT. All data are presented as mean ± SEM. Statistical significance was determined using an unpaired two-tailed Student’s t-test. *P < 0.05; **P < 0.01; ***P < 0.05; ****P < 0.0001. Scale bars, 300 µm.

    Techniques Used: Staining, Control, In Situ Hybridization, Two Tailed Test

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    Article Title: Identification of Human NK17/NK1 Cells
    Article Snippet: Mouse anti-CCR4, mouse anti-CCR6, mouse anti-CCR7, mouse anti-CXCR3, FITC-conjugated mouse anti-CCR4, FITC-conjugated mouse anti-CCR6, FITC-conjugated mouse anti-CCR7, FITC-conjugated mouse anti-CCR9, FITC-conjugated mouse anti-CXCR1, FITC-conjugated mouse anti-CXCR3, FITC-conjugated anti-mouse CXCR4, PE-conjugated mouse anti-CD158, PE-conjugated mouse anti-CD127 (IL-7Rα), PE-conjugated mouse anti-CD132 (common γ chain), PE-conjugated mouse anti-IL-2Rβ, PE-conjugated mouse anti-IL-17, PE-conjugated mouse anti-IFN-γ, PE-conjugated mouse anti-IL-23R, PE-conjugated mouse anti-CCL22 (MDC), mouse anti-human mouse IL-1β, mouse anti-human IL-6, goat anti-human anti-TGF-β1, mouse IgG 1 , mouse IgG 2B, mouse IgG 2A , rat and goat IgG were all purchased from R&D Systems (R&D Systems Europe Ltd., Abingdon, UK).



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    TMH inhibits activation of the NLRP3 inflammasome. (A) Schematic workflow of in vitro NLRP3 inflammasome activation. (B,C) Cell viability was assessed in J774A.1 cells (B) and PMA (500 nM)-differentiated THP-1 cells (C) treated with TMH for 2 or 18 h using the EZ-Cytox assay. (D) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with ATP (5 mM) for 30 min in the presence or absence of MCC950. IL-1β (p17) levels in supernatants were measured by ELISA. (E,F) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with ATP (5 mM) (E) or nigericin (10 μM) (F) for 1 h, with or without MCC950. IL-1β (p17) levels in supernatants were determined by ELISA. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001; n.s., not significant.

    Journal: Frontiers in Pharmacology

    Article Title: Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity

    doi: 10.3389/fphar.2026.1781860

    Figure Lengend Snippet: TMH inhibits activation of the NLRP3 inflammasome. (A) Schematic workflow of in vitro NLRP3 inflammasome activation. (B,C) Cell viability was assessed in J774A.1 cells (B) and PMA (500 nM)-differentiated THP-1 cells (C) treated with TMH for 2 or 18 h using the EZ-Cytox assay. (D) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with ATP (5 mM) for 30 min in the presence or absence of MCC950. IL-1β (p17) levels in supernatants were measured by ELISA. (E,F) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with ATP (5 mM) (E) or nigericin (10 μM) (F) for 1 h, with or without MCC950. IL-1β (p17) levels in supernatants were determined by ELISA. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001; n.s., not significant.

    Article Snippet: Antibodies specific for human IL-1β (AF-401-NA) and mouse IL-1β (AF-201-NA) were purchased from R&D Systems (United States).

    Techniques: Activation Assay, In Vitro, Enzyme-linked Immunosorbent Assay

    TMH does not affect other inflammasome or inflammatory pathways. (A,B) LPS-primed J774A.1 cells were treated with TMH for 2 h, followed by stimulation with either dsDNA (1 μg/mL) (A) or flagellin (B) transfected using Lipofectamine 2000 for 3 h. (C) Following TMH treatment (2 h), nuclear and cytosolic fractions of LPS-primed J774A.1 cells were separated and assessed for NF-κB p65 translocation by immunoblotting. (D) HEK293FT cells transfected with the pGL4.32 luciferase reporter vector were treated with TNF-α (20 ng/mL) for 5 h, with or without TMH pre-treatment (2 h). Luciferase activity was measured using the Bright-Glo™ luciferase assay system (Promega). Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test n.s., not significant.

    Journal: Frontiers in Pharmacology

    Article Title: Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity

    doi: 10.3389/fphar.2026.1781860

    Figure Lengend Snippet: TMH does not affect other inflammasome or inflammatory pathways. (A,B) LPS-primed J774A.1 cells were treated with TMH for 2 h, followed by stimulation with either dsDNA (1 μg/mL) (A) or flagellin (B) transfected using Lipofectamine 2000 for 3 h. (C) Following TMH treatment (2 h), nuclear and cytosolic fractions of LPS-primed J774A.1 cells were separated and assessed for NF-κB p65 translocation by immunoblotting. (D) HEK293FT cells transfected with the pGL4.32 luciferase reporter vector were treated with TNF-α (20 ng/mL) for 5 h, with or without TMH pre-treatment (2 h). Luciferase activity was measured using the Bright-Glo™ luciferase assay system (Promega). Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test n.s., not significant.

    Article Snippet: Antibodies specific for human IL-1β (AF-401-NA) and mouse IL-1β (AF-201-NA) were purchased from R&D Systems (United States).

    Techniques: Transfection, Translocation Assay, Western Blot, Luciferase, Plasmid Preparation, Activity Assay

    TMH inhibits NLRP3 inflammasome activation by suppressing ASC oligomerization and ATPase activity. (A) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with imiquimod (200 μM) for 1 h. (B) Cells were treated with TMH (2 h), stained with MitoSOX (5 μM, 10 min), and stimulated with ATP (5 mM, 5 min). Intracellular ROS were visualized by confocal microscopy. (C,D) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with nigericin (10 μM, 1 h). ASC speck formation was examined by confocal microscopy (C) , and representative images from five fields are shown (D) . (E) Cells were stimulated with or without MCC950 and cross-linked with DSS (2.5 mM, 30 min) before immunoblotting for ASC oligomerization. (F) NLRP3 ATPase activity was measured using the ADP-Glo™ assay to quantify ATP-to-ADP conversion following TMH treatment. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. **P < 0.01, ***P < 0.001.

    Journal: Frontiers in Pharmacology

    Article Title: Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity

    doi: 10.3389/fphar.2026.1781860

    Figure Lengend Snippet: TMH inhibits NLRP3 inflammasome activation by suppressing ASC oligomerization and ATPase activity. (A) LPS-primed J774A.1 cells were treated with TMH for 2 h, then stimulated with imiquimod (200 μM) for 1 h. (B) Cells were treated with TMH (2 h), stained with MitoSOX (5 μM, 10 min), and stimulated with ATP (5 mM, 5 min). Intracellular ROS were visualized by confocal microscopy. (C,D) PMA-differentiated THP-1 cells were primed with LPS, treated with TMH for 2 h, then stimulated with nigericin (10 μM, 1 h). ASC speck formation was examined by confocal microscopy (C) , and representative images from five fields are shown (D) . (E) Cells were stimulated with or without MCC950 and cross-linked with DSS (2.5 mM, 30 min) before immunoblotting for ASC oligomerization. (F) NLRP3 ATPase activity was measured using the ADP-Glo™ assay to quantify ATP-to-ADP conversion following TMH treatment. Data are presented as the mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparisons test. **P < 0.01, ***P < 0.001.

    Article Snippet: Antibodies specific for human IL-1β (AF-401-NA) and mouse IL-1β (AF-201-NA) were purchased from R&D Systems (United States).

    Techniques: Activation Assay, Activity Assay, Staining, Confocal Microscopy, Western Blot, Glo Assay

    Toxicity assessment of TMH in zebrafish embryos. (A) Survival curves of zebrafish embryos treated with TMH at concentrations of 1, 10, or 100 μg/mL. Sixty embryos were used per condition and maintained in E3 medium. The control group was treated with DMSO (0.25%, v/v), corresponding to the highest TMH concentration. (B) Survival and phenotype distribution of 5 dpf embryos treated with TMH at distinct concentrations from 1 to 5 dpf. (C) Representative images showing developmental abnormalities observed in embryos treated with 10 μg/mL TMH at 5 dpf. (D) Representative images of Sudan Black B staining in 3 dpf embryos treated with vehicle control (0.0025% DMSO with PTU; upper panel) or TMH (1 μg/mL; lower panel). (E) Quantification of neutrophil counts in the CHT (red dashed outline) following treatment with TMH (1 μg/mL). Data are presented as mean ± SEM of individual embryos. Statistical significance was determined using an unpaired two-tailed Student’s t-test; n.s., not significant (p = 0.9997). Scale bars, 300 µm.

    Journal: Frontiers in Pharmacology

    Article Title: Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity

    doi: 10.3389/fphar.2026.1781860

    Figure Lengend Snippet: Toxicity assessment of TMH in zebrafish embryos. (A) Survival curves of zebrafish embryos treated with TMH at concentrations of 1, 10, or 100 μg/mL. Sixty embryos were used per condition and maintained in E3 medium. The control group was treated with DMSO (0.25%, v/v), corresponding to the highest TMH concentration. (B) Survival and phenotype distribution of 5 dpf embryos treated with TMH at distinct concentrations from 1 to 5 dpf. (C) Representative images showing developmental abnormalities observed in embryos treated with 10 μg/mL TMH at 5 dpf. (D) Representative images of Sudan Black B staining in 3 dpf embryos treated with vehicle control (0.0025% DMSO with PTU; upper panel) or TMH (1 μg/mL; lower panel). (E) Quantification of neutrophil counts in the CHT (red dashed outline) following treatment with TMH (1 μg/mL). Data are presented as mean ± SEM of individual embryos. Statistical significance was determined using an unpaired two-tailed Student’s t-test; n.s., not significant (p = 0.9997). Scale bars, 300 µm.

    Article Snippet: Antibodies specific for human IL-1β (AF-401-NA) and mouse IL-1β (AF-201-NA) were purchased from R&D Systems (United States).

    Techniques: Control, Concentration Assay, Staining, Two Tailed Test

    TMH suppresses LPS-induced inflammatory cell recruitment in zebrafish embryos. (A) Representative images of neutrophil recruitment in the CHT in 3 dpf zebrafish embryos following LPS stimulation, assessed by Sudan Black B staining. Top panel: control embryos treated with 0.0025% DMSO (n = 29); middle panel: LPS-treated embryos (10 μg/mL; n = 32); bottom panel: embryos co-treated with LPS (10 μg/mL) and TMH (1 μg/mL; n = 33). (B) Quantification of neutrophil accumulation in the CHT following LPS stimulation with or without TMH treatment using Sudan Black B staining from (A) . (C) Representative images of whole-mount in situ hybridization showing mpx -positive neutrophils in 3 dpf embryos under LPS and TMH treatment conditions. Top panel (DMSO 0.0025%; n = 34); middle panel (LPS 10 μg/mL; n = 35); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 39). (D) Quantification of mpx -positive cells within the CHT from (C) . (E) Representative confocal images of macrophages in 3 dpf Tg ( mpeg1 :EGFP) zebrafish embryos following LPS and TMH treatment. Top panel (DMSO 0.0025%; n = 8); middle panel (LPS 10 μg/mL; n = 11); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 13). (F) Quantification of mpeg1 :EGFP-positive macrophages in the CHT region shown in (E) . Red dashed outline indicates the CHT. All data are presented as mean ± SEM. Statistical significance was determined using an unpaired two-tailed Student’s t-test. *P < 0.05; **P < 0.01; ***P < 0.05; ****P < 0.0001. Scale bars, 300 µm.

    Journal: Frontiers in Pharmacology

    Article Title: Thymelaea hirsuta (L.) Endl . extract attenuates NLRP3 inflammasome activation via modulation of ATPase activity

    doi: 10.3389/fphar.2026.1781860

    Figure Lengend Snippet: TMH suppresses LPS-induced inflammatory cell recruitment in zebrafish embryos. (A) Representative images of neutrophil recruitment in the CHT in 3 dpf zebrafish embryos following LPS stimulation, assessed by Sudan Black B staining. Top panel: control embryos treated with 0.0025% DMSO (n = 29); middle panel: LPS-treated embryos (10 μg/mL; n = 32); bottom panel: embryos co-treated with LPS (10 μg/mL) and TMH (1 μg/mL; n = 33). (B) Quantification of neutrophil accumulation in the CHT following LPS stimulation with or without TMH treatment using Sudan Black B staining from (A) . (C) Representative images of whole-mount in situ hybridization showing mpx -positive neutrophils in 3 dpf embryos under LPS and TMH treatment conditions. Top panel (DMSO 0.0025%; n = 34); middle panel (LPS 10 μg/mL; n = 35); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 39). (D) Quantification of mpx -positive cells within the CHT from (C) . (E) Representative confocal images of macrophages in 3 dpf Tg ( mpeg1 :EGFP) zebrafish embryos following LPS and TMH treatment. Top panel (DMSO 0.0025%; n = 8); middle panel (LPS 10 μg/mL; n = 11); bottom panel (LPS 10 μg/mL with TMH 1 μg/mL; n = 13). (F) Quantification of mpeg1 :EGFP-positive macrophages in the CHT region shown in (E) . Red dashed outline indicates the CHT. All data are presented as mean ± SEM. Statistical significance was determined using an unpaired two-tailed Student’s t-test. *P < 0.05; **P < 0.01; ***P < 0.05; ****P < 0.0001. Scale bars, 300 µm.

    Article Snippet: Antibodies specific for human IL-1β (AF-401-NA) and mouse IL-1β (AF-201-NA) were purchased from R&D Systems (United States).

    Techniques: Staining, Control, In Situ Hybridization, Two Tailed Test

    CTG12 inhibits NLRP3 inflammasome activation in mouse BMDMs and human THP1. A The structure of CTG12. B , C Cell viability of BMDMs ( B ) and THP1 cells ( C ) treated with CTG12. (D-H) Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), NLRP3, ASC in whole cell lysates (WCL) of LPS-primed BMDMs treated with CTG12 and then stimulated with Nigericin (25 min) ( D ), supernatants were collected for the measurement of caspase-1( E ), IL-1β ( F ), LDH ( G ) and TNF-α ( H ). (I-M) THP-1 cells primed with PMA for 12 h were treated with CTG12 for 1 h and then stimulated with nigericin for 55 min. Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), ASC in whole cell lysates (WCL) of THP-1 ( I ), supernatants were collected for the measurement of caspase-1( J ), IL-1β ( K ), LDH ( L ) and TNF-α ( M ). Coomassie blue-stained gels was used as loading control and Lamin B was used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). Compared to con, ** p < 0.01, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

    Journal: Cell Communication and Signaling : CCS

    Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

    doi: 10.1186/s12964-026-02741-2

    Figure Lengend Snippet: CTG12 inhibits NLRP3 inflammasome activation in mouse BMDMs and human THP1. A The structure of CTG12. B , C Cell viability of BMDMs ( B ) and THP1 cells ( C ) treated with CTG12. (D-H) Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), NLRP3, ASC in whole cell lysates (WCL) of LPS-primed BMDMs treated with CTG12 and then stimulated with Nigericin (25 min) ( D ), supernatants were collected for the measurement of caspase-1( E ), IL-1β ( F ), LDH ( G ) and TNF-α ( H ). (I-M) THP-1 cells primed with PMA for 12 h were treated with CTG12 for 1 h and then stimulated with nigericin for 55 min. Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), ASC in whole cell lysates (WCL) of THP-1 ( I ), supernatants were collected for the measurement of caspase-1( J ), IL-1β ( K ), LDH ( L ) and TNF-α ( M ). Coomassie blue-stained gels was used as loading control and Lamin B was used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). Compared to con, ** p < 0.01, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

    Article Snippet: Anti-human IL-1β (p17, 12242S), anti-Phospho-IRF3 (Ser396) (4947), caspase-1 antibody (4199S) and anti-ASC antibody (sc-22, 514-R) were obtained from Cell Signaling Technology (Germany).

    Techniques: Activation Assay, Western Blot, Staining, Control, Concentration Assay

    CTG12 specifically inhibits canonical and noncanonical NLRP3 inflammasome activation. A - C BMDMs were primed with LPS and then treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly (I:C), or SiO₂. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs (A), supernatants were collected for the measurement of caspase-1 ( B ) and IL-1β ( C ). D - F BMDMs primed with Pam3CSK4 treated with CTG12 (5 μM), followed by cytosolic LPS. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( D ), supernatants were collected for the measurement of caspase-1 ( E ) and IL-1β ( F ). ( G - I ) BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, Salmonella, poly (dA:dT). Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( G ), supernatants were collected for the measurement of caspase-1 ( H ) and IL-1β ( I ). Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

    Journal: Cell Communication and Signaling : CCS

    Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

    doi: 10.1186/s12964-026-02741-2

    Figure Lengend Snippet: CTG12 specifically inhibits canonical and noncanonical NLRP3 inflammasome activation. A - C BMDMs were primed with LPS and then treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly (I:C), or SiO₂. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs (A), supernatants were collected for the measurement of caspase-1 ( B ) and IL-1β ( C ). D - F BMDMs primed with Pam3CSK4 treated with CTG12 (5 μM), followed by cytosolic LPS. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( D ), supernatants were collected for the measurement of caspase-1 ( E ) and IL-1β ( F ). ( G - I ) BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, Salmonella, poly (dA:dT). Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( G ), supernatants were collected for the measurement of caspase-1 ( H ) and IL-1β ( I ). Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

    Article Snippet: Anti-human IL-1β (p17, 12242S), anti-Phospho-IRF3 (Ser396) (4947), caspase-1 antibody (4199S) and anti-ASC antibody (sc-22, 514-R) were obtained from Cell Signaling Technology (Germany).

    Techniques: Activation Assay, Western Blot, Staining, Control

    CTG12 inhibits LPS-induced priming step of inflammasome activation and specifically inhibits canonical and noncanonical NLRP3 inflammasome activation by blocking NLRP3-dependent ASC oligomerization. A BMDMs were cultured with LPS for 4 h, then incubated with CTG12 for 1 h, or BMDMs were first treated with CTG12 for 1 h, followed by stimulation with LPS for 4 h, western blot analysis of protein levels of NLRP3, ASC, pro-IL-1β, Cas-1 p45, Lamin B. B BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. C BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly(I:C), SiO 2 , western blot analysis of in Triton X insoluble microparticle cross-linked ASC. D BMDMs were primed with Pam3CSK4 treated with CTG12 (5 μM), followed by stimulation with ultra-LPS, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. E BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, salmonella or poly (dA:dT), western blot analysis of in Triton X insoluble microparticle cross-linked ASC. Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples

    Journal: Cell Communication and Signaling : CCS

    Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

    doi: 10.1186/s12964-026-02741-2

    Figure Lengend Snippet: CTG12 inhibits LPS-induced priming step of inflammasome activation and specifically inhibits canonical and noncanonical NLRP3 inflammasome activation by blocking NLRP3-dependent ASC oligomerization. A BMDMs were cultured with LPS for 4 h, then incubated with CTG12 for 1 h, or BMDMs were first treated with CTG12 for 1 h, followed by stimulation with LPS for 4 h, western blot analysis of protein levels of NLRP3, ASC, pro-IL-1β, Cas-1 p45, Lamin B. B BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. C BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly(I:C), SiO 2 , western blot analysis of in Triton X insoluble microparticle cross-linked ASC. D BMDMs were primed with Pam3CSK4 treated with CTG12 (5 μM), followed by stimulation with ultra-LPS, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. E BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, salmonella or poly (dA:dT), western blot analysis of in Triton X insoluble microparticle cross-linked ASC. Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples

    Article Snippet: Anti-human IL-1β (p17, 12242S), anti-Phospho-IRF3 (Ser396) (4947), caspase-1 antibody (4199S) and anti-ASC antibody (sc-22, 514-R) were obtained from Cell Signaling Technology (Germany).

    Techniques: Activation Assay, Blocking Assay, Cell Culture, Incubation, Western Blot, Staining, Control

    CTG12 alleviates LPS-induced acute systemic inflammation in mice. A - J Female mice (8 weeks) were injected intraperitoneally with CTG12 (0 mg/kg, 15 mg/kg, 30 mg/kg), MCC950 (40 mg/kg) or CTG12 (30 mg/kg) + MCC950 (40 mg/kg) for 1 h, followed by an injection of 20 mg/kg LPS for 5 h ( n = 6). The levels of IL-1β (A, B), IL-18 ( C , D ), IL-6 ( E , F ), TNF-α ( G , H ) and CXCL1/KC ( I , J ) in peritoneal lavage fluid and serum were analyzed by ELISA ( n = 6). Data represent as mean ± SD. Compared to con, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

    Journal: Cell Communication and Signaling : CCS

    Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

    doi: 10.1186/s12964-026-02741-2

    Figure Lengend Snippet: CTG12 alleviates LPS-induced acute systemic inflammation in mice. A - J Female mice (8 weeks) were injected intraperitoneally with CTG12 (0 mg/kg, 15 mg/kg, 30 mg/kg), MCC950 (40 mg/kg) or CTG12 (30 mg/kg) + MCC950 (40 mg/kg) for 1 h, followed by an injection of 20 mg/kg LPS for 5 h ( n = 6). The levels of IL-1β (A, B), IL-18 ( C , D ), IL-6 ( E , F ), TNF-α ( G , H ) and CXCL1/KC ( I , J ) in peritoneal lavage fluid and serum were analyzed by ELISA ( n = 6). Data represent as mean ± SD. Compared to con, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

    Article Snippet: Anti-human IL-1β (p17, 12242S), anti-Phospho-IRF3 (Ser396) (4947), caspase-1 antibody (4199S) and anti-ASC antibody (sc-22, 514-R) were obtained from Cell Signaling Technology (Germany).

    Techniques: Injection, Enzyme-linked Immunosorbent Assay, Concentration Assay

    TRAF1 V203A mutation in THP-1 cells reduces secretion of caspase-1 and IL-1β by reducing K63-linked polyubiquitination of caspase-1. TRAF1 WT and TRAF1 V203A THP-1 cells were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). The culture supernatants were collected, and the proteins were precipitated using 100% TCA. (A) Supernatants were immunoblotted for immature caspase-1 (pro-caspase-1) and active caspase-1 (p20 subunit). (B) Supernatants were immunoblotted for inactive IL-1β (pro-IL-1β) and processed IL-1β (bioactive IL-1β). The blots shown in (A) and (B) are representative of five independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation. (C) TRAF1 WT cells and TRAF1 V203A THP-1 clones (C1 and C2) were primed with or without 100 ng/mL LPS for 24 hours. Cells were stimulated with 10 µM nigericin for 2, 10, and 25 minutes. Whole-cell lysates were immunoblotted for K63-linked polyubiquitin (Ub) chains. (D) The whole-cell lysates from (C) were immunoprecipitated with endogenous caspase-1 and then immunoblotted for K63-linked polyubiquitin (Ub) chains. The blots shown in (C) and (D) are representative of two independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation.

    Journal: ImmunoHorizons

    Article Title: Disrupting the TRAF1/cIAP2 interaction attenuates inflammasome activation and protects against monosodium urate crystal–induced arthritis

    doi: 10.1093/immhor/vlaf065

    Figure Lengend Snippet: TRAF1 V203A mutation in THP-1 cells reduces secretion of caspase-1 and IL-1β by reducing K63-linked polyubiquitination of caspase-1. TRAF1 WT and TRAF1 V203A THP-1 cells were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). The culture supernatants were collected, and the proteins were precipitated using 100% TCA. (A) Supernatants were immunoblotted for immature caspase-1 (pro-caspase-1) and active caspase-1 (p20 subunit). (B) Supernatants were immunoblotted for inactive IL-1β (pro-IL-1β) and processed IL-1β (bioactive IL-1β). The blots shown in (A) and (B) are representative of five independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation. (C) TRAF1 WT cells and TRAF1 V203A THP-1 clones (C1 and C2) were primed with or without 100 ng/mL LPS for 24 hours. Cells were stimulated with 10 µM nigericin for 2, 10, and 25 minutes. Whole-cell lysates were immunoblotted for K63-linked polyubiquitin (Ub) chains. (D) The whole-cell lysates from (C) were immunoprecipitated with endogenous caspase-1 and then immunoblotted for K63-linked polyubiquitin (Ub) chains. The blots shown in (C) and (D) are representative of two independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation.

    Article Snippet: Proteins in the culture supernatants collected from inflammasome-stimulated THP-1 cells were precipitated with 100% trichloroacetic acid (TCA) and then immunoblotted with antibodies to detect human/mouse IL-1β ELISA (R&D Systems, Minneapolis, MN, USA) and mouse caspase-1 (BioLegend).

    Techniques: Mutagenesis, Clone Assay, Immunoprecipitation

    TRAF1 V196A mice exhibit reduced inflammasome-driven IL-1β secretion in vivo and in vitro. TRAF1 WT and TRAF1 V196A BMDMs were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). IL-1β was quantified from the collected supernatant by ELISA. A total of six independent experiments were performed, three in female mice (A) and three in male mice (B). Ordinary 2-way ANOVA was performed with Tukey multiple comparisons test to determine statistical significance. (C) TRAF1 WT ( n = 4) and TRAF1 V196A ( n = 4) female littermate mice were injected intraperitoneally with a sublethal LPS dose of 10 mg/kg. Blood was collected at the 1- and 6-hour timepoints by saphenous vein and the serum was collected to perform the multiplex cytokine assay by flow cytometry. Each symbol represents one mouse. Ordinary 2-way ANOVA was performed with Sidak multiple comparisons test to determine statistical significance. The error bars represent mean ± SEM. * P < 0.05, ** P < 0.01.

    Journal: ImmunoHorizons

    Article Title: Disrupting the TRAF1/cIAP2 interaction attenuates inflammasome activation and protects against monosodium urate crystal–induced arthritis

    doi: 10.1093/immhor/vlaf065

    Figure Lengend Snippet: TRAF1 V196A mice exhibit reduced inflammasome-driven IL-1β secretion in vivo and in vitro. TRAF1 WT and TRAF1 V196A BMDMs were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). IL-1β was quantified from the collected supernatant by ELISA. A total of six independent experiments were performed, three in female mice (A) and three in male mice (B). Ordinary 2-way ANOVA was performed with Tukey multiple comparisons test to determine statistical significance. (C) TRAF1 WT ( n = 4) and TRAF1 V196A ( n = 4) female littermate mice were injected intraperitoneally with a sublethal LPS dose of 10 mg/kg. Blood was collected at the 1- and 6-hour timepoints by saphenous vein and the serum was collected to perform the multiplex cytokine assay by flow cytometry. Each symbol represents one mouse. Ordinary 2-way ANOVA was performed with Sidak multiple comparisons test to determine statistical significance. The error bars represent mean ± SEM. * P < 0.05, ** P < 0.01.

    Article Snippet: Proteins in the culture supernatants collected from inflammasome-stimulated THP-1 cells were precipitated with 100% trichloroacetic acid (TCA) and then immunoblotted with antibodies to detect human/mouse IL-1β ELISA (R&D Systems, Minneapolis, MN, USA) and mouse caspase-1 (BioLegend).

    Techniques: In Vivo, In Vitro, Enzyme-linked Immunosorbent Assay, Injection, Multiplex Assay, Cytokine Assay, Flow Cytometry

    Figure 1. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in plasma samples from patients with brain gliomas of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

    Journal: International journal of molecular sciences

    Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

    doi: 10.3390/ijms26104802

    Figure Lengend Snippet: Figure 1. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in plasma samples from patients with brain gliomas of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

    Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

    Techniques: Clinical Proteomics

    Figure 2. Graphs of the changes of HIF-1α, ANG-2, and IL-1β concentrations in plasma samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann–Whitney-U test p-value results table.

    Journal: International journal of molecular sciences

    Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

    doi: 10.3390/ijms26104802

    Figure Lengend Snippet: Figure 2. Graphs of the changes of HIF-1α, ANG-2, and IL-1β concentrations in plasma samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann–Whitney-U test p-value results table.

    Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

    Techniques: Clinical Proteomics, MANN-WHITNEY

    Figure 3. ROC curves for (A) HIF-1α; (B) ANG-2; and (C) IL-1β.

    Journal: International journal of molecular sciences

    Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

    doi: 10.3390/ijms26104802

    Figure Lengend Snippet: Figure 3. ROC curves for (A) HIF-1α; (B) ANG-2; and (C) IL-1β.

    Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

    Techniques:

    Figure 4. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenate samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

    Journal: International journal of molecular sciences

    Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

    doi: 10.3390/ijms26104802

    Figure Lengend Snippet: Figure 4. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenate samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

    Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

    Techniques:

    Figure 5. Graphs of changes in HIF-1α, ANG-2, and IL-1β concentrations in tissue homogenate samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann– Whitney U test p-value results table.

    Journal: International journal of molecular sciences

    Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

    doi: 10.3390/ijms26104802

    Figure Lengend Snippet: Figure 5. Graphs of changes in HIF-1α, ANG-2, and IL-1β concentrations in tissue homogenate samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann– Whitney U test p-value results table.

    Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

    Techniques: MANN-WHITNEY

    Figure 6. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenates and plasma samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots.

    Journal: International journal of molecular sciences

    Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

    doi: 10.3390/ijms26104802

    Figure Lengend Snippet: Figure 6. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenates and plasma samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots.

    Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

    Techniques: Clinical Proteomics