monoclonal mouse antibody against il 1β  (R&D Systems)

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

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

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:

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:

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

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

Journal: Frontiers in Immunology

Article Title: The endoplasmic reticulum stress sensor IRE1α modulates macrophage metabolic function during Brucella abortus infection

doi: 10.3389/fimmu.2022.1063221

Figure Lengend Snippet: IRE1α is necessary for full induction of HIF-1α-dependent inflammatory responses during infection. (A) IL-6, (B) IL-12, (C) IL-1β and (D) TNF-α produced by macrophages derived from HIF-1α WT and HIF-1α KO mice non-infected (NI), infected with B abortus (Ba) or pre-treated with 4μ8c (50 μM) and infected with B abortus (Ba+4μ8c), detected in cell supernatants using ELISA. The data are representative of three independent experiments. The data are presented as mean ± SD, * p < 0.05 (compared between WT and KO), # p < 0.05 (compared to Ba from WT), & p < 0.05 (compared to Ba from KO), two-way ANOVA.

Article Snippet: Primary antibodies used are the following: a monoclonal antibody against IL-1β (clone 3A6, Cell Signaling Technology), a monoclonal antibody against HIF-1α (clone D1S7W, Cell Signaling Technology, Danvers, MA), a monoclonal antibody against caspase-11 (clone Flamy-1, Adipogen, San Diego, CA), a monoclonal antibody against gasdermin D (clone EPR19828, Abcam, Cambridge, U.K.), and a monoclonal antibody against the p20 subunit of caspase-1 (clone Casper-1, Adipogen), all at a 1:1000 dilution.

Techniques: Infection, Produced, Derivative Assay, Enzyme-linked Immunosorbent Assay

Journal: Frontiers in Immunology

Article Title: The endoplasmic reticulum stress sensor IRE1α modulates macrophage metabolic function during Brucella abortus infection

doi: 10.3389/fimmu.2022.1063221

Figure Lengend Snippet: IRE1α induces inflammasome activation and IL-1β release in infected macrophages. (A) IL-1β released by macrophages derived from C57BL/6 mice non-infected (NI), infected with B abortus (Ba) or pre-treated with 4μ8c (50 μM) and infected with B abortus (Ba+4μ8c), detected in cell supernatants using ELISA. (B) IL-1β released by macrophages derived from C57BL/6 mice subjected to specific XBP1 gene knockdown and then infected with B abortus . (C) Western blot analysis of pro-IL-1β, pro-caspase-1, caspase-11 and p30 fragment of GSDMD in cell lysates and caspase-1 (p20 subunit) in supernatants from macrophages derived from C57BL/6 mice, non-infected (NI), infected with B abortus (Ba) or pre-treated with 4μ8c (50 μM) and infected with B abortus (Ba+4μ8c). Equal loading was controlled by measuring β-actin in the corresponding cell lysates. (D) LDH release in macrophages derived from C57BL/6 mice non-infected (NI), infected with B abortus (Ba) or pre-treated with 4μ8c (50 μM) and infected with B abortus (Ba+4μ8c). Values represent the percentage of LDH release compared with lysed cells. The data are representative of three independent experiments. The data (A, D) are presented as mean ± SD, * p < 0.05, one-way ANOVA. The data (B) are presented as mean ± SD, * p < 0.05, Student’s t test.

Article Snippet: Primary antibodies used are the following: a monoclonal antibody against IL-1β (clone 3A6, Cell Signaling Technology), a monoclonal antibody against HIF-1α (clone D1S7W, Cell Signaling Technology, Danvers, MA), a monoclonal antibody against caspase-11 (clone Flamy-1, Adipogen, San Diego, CA), a monoclonal antibody against gasdermin D (clone EPR19828, Abcam, Cambridge, U.K.), and a monoclonal antibody against the p20 subunit of caspase-1 (clone Casper-1, Adipogen), all at a 1:1000 dilution.

Techniques: Activation Assay, Infection, Derivative Assay, Enzyme-linked Immunosorbent Assay, Knockdown, Western Blot

Journal: Frontiers in Immunology

Article Title: The endoplasmic reticulum stress sensor IRE1α modulates macrophage metabolic function during Brucella abortus infection

doi: 10.3389/fimmu.2022.1063221

Figure Lengend Snippet: Regulation of macrophage metabolic function by IRE1α in Brucella abortus infection. IRE1α activation by Brucella abortus triggers mROS generation that induces HIF-1α stabilization in infected macrophages. IRE1α drives the metabolic reprogramming in macrophages, contributing to the enhanced glycolysis and reduced OXPHOS observed in Brucella -infected macrophages possibly via HIF-1α. This IRE1α-dependent HIF-1α stabilization is crucial for inducing inflammatory responses during infection. IRE1α induces inflammasome assembly, IL-1β release and NO production, supporting the inflammatory profile in macrophages infected with B abortus . Figure created using BioRender ( https://biorender.com ).

Article Snippet: Primary antibodies used are the following: a monoclonal antibody against IL-1β (clone 3A6, Cell Signaling Technology), a monoclonal antibody against HIF-1α (clone D1S7W, Cell Signaling Technology, Danvers, MA), a monoclonal antibody against caspase-11 (clone Flamy-1, Adipogen, San Diego, CA), a monoclonal antibody against gasdermin D (clone EPR19828, Abcam, Cambridge, U.K.), and a monoclonal antibody against the p20 subunit of caspase-1 (clone Casper-1, Adipogen), all at a 1:1000 dilution.

Techniques: Infection, Activation Assay