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Figure 1. Prevention of Inflammasome Priming and Activation in L. am-Infected Macrophages BMDMs were infected with amastigotes at a MOI of 4:1. (A) Western blot analysis of mature IL-1b and caspase-1 p20 in culture supernatants (SN) and pro-caspase-1 and pro-IL-1b in macrophage lysates (day 3 PI). (B) Western blot analysis of ASC in cell lysates and pellets (day 3 PI). (C) Western blot analysis of NLRP3, <t>NLRC4,</t> AIM2, and RIG-1 inflammasomes in BMDM lysates (day 3 PI). Beta-actin was used as a control protein. (D) Transcriptional modulation of inflammasome components as assessed by qRT-PCR. BMDMs were loaded with live (L. am) or heat-killed (HK L. am) amastigotes or latex beads and cultured for 3 days. As positive control, NLRP3 activation was induced after LPS and ATP stimulation. The expression fold changes (FCs) are indicated using uninfected and unstimulated macrophages as a calibrator. Histograms display mean FC values ± SEM for L. am-infected and LPS + ATP-treated uninfected BMDMs (n = 4–13 independent experiments) and for HK L. am and latex bead-loaded BMDMs (technical duplicates; one representative experiment is shown). (E and F) Biparametric dot plots displaying transcript modulation (fold changes [FCs]) of IL-1b (E) and IL-18 (F) and parasite load (mean number of amastigotes per macrophage) at different time points PI (indicated by the numeric label of the data points). The F-test p value is indicated for the corresponding linear regression. (G) Western blot analyses of inflammasome components at day 3 PI in culture supernatants (SN) and lysates from LPS-stimulated and non-stimulated samples. (H and I) Detection by ELISA of secreted IL-1b (H) and IL-18 (I). Cytokines were quantified in supernatants following sequential LPS/ATP stimulation of mac- rophages at day 1 and day 3 PI. Blue and red bars represent cytokine levels for uninfected and infected BMDMs, respectively (mean ± SEM, n = 3-6). nd, not detected; *p < 0.06; **p < 0.05.
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Figure 1. Prevention of Inflammasome Priming and Activation in L. am-Infected Macrophages BMDMs were infected with amastigotes at a MOI of 4:1. (A) Western blot analysis of mature IL-1b and caspase-1 p20 in culture supernatants (SN) and pro-caspase-1 and pro-IL-1b in macrophage lysates (day 3 PI). (B) Western blot analysis of ASC in cell lysates and pellets (day 3 PI). (C) Western blot analysis of NLRP3, NLRC4, AIM2, and RIG-1 inflammasomes in BMDM lysates (day 3 PI). Beta-actin was used as a control protein. (D) Transcriptional modulation of inflammasome components as assessed by qRT-PCR. BMDMs were loaded with live (L. am) or heat-killed (HK L. am) amastigotes or latex beads and cultured for 3 days. As positive control, NLRP3 activation was induced after LPS and ATP stimulation. The expression fold changes (FCs) are indicated using uninfected and unstimulated macrophages as a calibrator. Histograms display mean FC values ± SEM for L. am-infected and LPS + ATP-treated uninfected BMDMs (n = 4–13 independent experiments) and for HK L. am and latex bead-loaded BMDMs (technical duplicates; one representative experiment is shown). (E and F) Biparametric dot plots displaying transcript modulation (fold changes [FCs]) of IL-1b (E) and IL-18 (F) and parasite load (mean number of amastigotes per macrophage) at different time points PI (indicated by the numeric label of the data points). The F-test p value is indicated for the corresponding linear regression. (G) Western blot analyses of inflammasome components at day 3 PI in culture supernatants (SN) and lysates from LPS-stimulated and non-stimulated samples. (H and I) Detection by ELISA of secreted IL-1b (H) and IL-18 (I). Cytokines were quantified in supernatants following sequential LPS/ATP stimulation of mac- rophages at day 1 and day 3 PI. Blue and red bars represent cytokine levels for uninfected and infected BMDMs, respectively (mean ± SEM, n = 3-6). nd, not detected; *p < 0.06; **p < 0.05.

Journal: Cell reports

Article Title: Targeting Macrophage Histone H3 Modification as a Leishmania Strategy to Dampen the NF-κB/NLRP3-Mediated Inflammatory Response.

doi: 10.1016/j.celrep.2020.01.030

Figure Lengend Snippet: Figure 1. Prevention of Inflammasome Priming and Activation in L. am-Infected Macrophages BMDMs were infected with amastigotes at a MOI of 4:1. (A) Western blot analysis of mature IL-1b and caspase-1 p20 in culture supernatants (SN) and pro-caspase-1 and pro-IL-1b in macrophage lysates (day 3 PI). (B) Western blot analysis of ASC in cell lysates and pellets (day 3 PI). (C) Western blot analysis of NLRP3, NLRC4, AIM2, and RIG-1 inflammasomes in BMDM lysates (day 3 PI). Beta-actin was used as a control protein. (D) Transcriptional modulation of inflammasome components as assessed by qRT-PCR. BMDMs were loaded with live (L. am) or heat-killed (HK L. am) amastigotes or latex beads and cultured for 3 days. As positive control, NLRP3 activation was induced after LPS and ATP stimulation. The expression fold changes (FCs) are indicated using uninfected and unstimulated macrophages as a calibrator. Histograms display mean FC values ± SEM for L. am-infected and LPS + ATP-treated uninfected BMDMs (n = 4–13 independent experiments) and for HK L. am and latex bead-loaded BMDMs (technical duplicates; one representative experiment is shown). (E and F) Biparametric dot plots displaying transcript modulation (fold changes [FCs]) of IL-1b (E) and IL-18 (F) and parasite load (mean number of amastigotes per macrophage) at different time points PI (indicated by the numeric label of the data points). The F-test p value is indicated for the corresponding linear regression. (G) Western blot analyses of inflammasome components at day 3 PI in culture supernatants (SN) and lysates from LPS-stimulated and non-stimulated samples. (H and I) Detection by ELISA of secreted IL-1b (H) and IL-18 (I). Cytokines were quantified in supernatants following sequential LPS/ATP stimulation of mac- rophages at day 1 and day 3 PI. Blue and red bars represent cytokine levels for uninfected and infected BMDMs, respectively (mean ± SEM, n = 3-6). nd, not detected; *p < 0.06; **p < 0.05.

Article Snippet: Proteins were resolved by SDS–PAGE (4%–12% Bis-Tris NuPAGE gels, MOPS buffer), electroblotted (polyvinylidene difluoride membranes), blocked (5% fat-free milk, Tris-buffered saline, 0.25% Tween 20) and probed overnight at 4 C with anti- NLRP3 (MAB7578, R&D Systems), NLRC4 (NB100-56142, Novus Biologicals), AIM2 (ab93015, abcam), RIG-I (3743, D14G6 clone, Cell Signaling), caspase-1 p20 (AG-20B-0042, Adipogen Life Sciences), IkBa (ab32518, abcam), phospho IkBa (MA5-14857, clone e2 Cell Reports 30, 1870–1882.e1–e4, February 11, 2020 J10.3,ThermoFischer scientific), IKKb (AM8109a, 62AT216 clone, Abgent), IKKg (sc-8330, Santa Cruz Biotechnology) and b-actin (4970, Cell Signaling) antibodies.

Techniques: Activation Assay, Infection, Western Blot, Control, Quantitative RT-PCR, Cell Culture, Positive Control, Expressing, Enzyme-linked Immunosorbent Assay