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    Cell Signaling Technology Inc p38
    Giardia duodenalis trophozoites–induced cytokine production was disrupted by <t>p38</t> and ERK inhibitor treatment. (A) A total of 3 × 10 6 wild-type (WT) mouse peritoneal macrophages were pretreated for 30 min with the p38 inhibitor SB203580 (30 μM) or the ERK inhibitor PD98059 (40 μM) before stimulation with 1 × 10 6 Giardia lamblia virus (GLV)–free Giardia trophozoites or 1 × 10 6 GLV-containing Giardia trophozoites. The phosphorylation levels of p38 and ERK were subsequently analyzed by Western blot. Relative protein expression was quantified by densitometric analysis using β-actin as an internal reference. (B) The production of IL-6, TNF-α, and IL-12 p40 in cell supernatants was measured by ELISA. Data are expressed as means ± SD from three separate experiments. * p
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    Giardia duodenalis trophozoites–induced cytokine production was disrupted by p38 and ERK inhibitor treatment. (A) A total of 3 × 10 6 wild-type (WT) mouse peritoneal macrophages were pretreated for 30 min with the p38 inhibitor SB203580 (30 μM) or the ERK inhibitor PD98059 (40 μM) before stimulation with 1 × 10 6 Giardia lamblia virus (GLV)–free Giardia trophozoites or 1 × 10 6 GLV-containing Giardia trophozoites. The phosphorylation levels of p38 and ERK were subsequently analyzed by Western blot. Relative protein expression was quantified by densitometric analysis using β-actin as an internal reference. (B) The production of IL-6, TNF-α, and IL-12 p40 in cell supernatants was measured by ELISA. Data are expressed as means ± SD from three separate experiments. * p

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: Giardia duodenalis Induces Proinflammatory Cytokine Production in Mouse Macrophages via TLR9-Mediated p38 and ERK Signaling Pathways

    doi: 10.3389/fcell.2021.694675

    Figure Lengend Snippet: Giardia duodenalis trophozoites–induced cytokine production was disrupted by p38 and ERK inhibitor treatment. (A) A total of 3 × 10 6 wild-type (WT) mouse peritoneal macrophages were pretreated for 30 min with the p38 inhibitor SB203580 (30 μM) or the ERK inhibitor PD98059 (40 μM) before stimulation with 1 × 10 6 Giardia lamblia virus (GLV)–free Giardia trophozoites or 1 × 10 6 GLV-containing Giardia trophozoites. The phosphorylation levels of p38 and ERK were subsequently analyzed by Western blot. Relative protein expression was quantified by densitometric analysis using β-actin as an internal reference. (B) The production of IL-6, TNF-α, and IL-12 p40 in cell supernatants was measured by ELISA. Data are expressed as means ± SD from three separate experiments. * p

    Article Snippet: After blocking with 5% bovine serum albumin (BSA) in Tris-buffered saline 0.1 Tween 20 (TBST) for 2 h at room temperature, the membranes were incubated overnight at 4°C with primary antibodies targeting TLR9, p38, ERK, AKT, NF-κB p65, phospho-p38, phospho-ERK, phospho-AKT, phospho-p65, phospho-IκBα, β-actin (all rabbit), and IκBα (mouse) (all from Cell Signaling Technology, Danvers, MA, United States) diluted 1/1,000 in 5% BSA.

    Techniques: Western Blot, Expressing, Enzyme-linked Immunosorbent Assay

    Giardia duodenalis trophozoites activated the p38 and ERK/MAPK signaling pathways via TLR9. (A) A total of 3 × 10 6 wild-type (WT) mouse peritoneal macrophages were stimulated with 1 × 10 6 G . duodenalis trophozoites for various periods (0–6 h) following which the phosphorylation levels of p38 and ERK were analyzed by Western blot. (B) The secretion levels of IL-6, TNF-α, and IL-12 p40 in cell culture supernatants were measured by ELISA. (C) Macrophages treated or not with small-interfering RNA (siRNA) targeting TLR9 (siTLR9) were stimulated with Giardia lamblia virus (GLV)–free or GLV-containing Giardia trophozoites for 3 h. (D) A total of 3 × 10 6 WT macrophages pretreated or not with siTLR9 were incubated for 3 h with 1 × 10 6 GLV-free Giardia trophozoites or 1 × 10 6 GLV-containing Giardia trophozoites, following which TLR9 expression levels were analyzed by Western blot. Relative protein expression was quantified by densitometric analysis using β-actin as an internal reference. Data are expressed as means ± SD from three separate experiments. ns, no significant difference, * p

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: Giardia duodenalis Induces Proinflammatory Cytokine Production in Mouse Macrophages via TLR9-Mediated p38 and ERK Signaling Pathways

    doi: 10.3389/fcell.2021.694675

    Figure Lengend Snippet: Giardia duodenalis trophozoites activated the p38 and ERK/MAPK signaling pathways via TLR9. (A) A total of 3 × 10 6 wild-type (WT) mouse peritoneal macrophages were stimulated with 1 × 10 6 G . duodenalis trophozoites for various periods (0–6 h) following which the phosphorylation levels of p38 and ERK were analyzed by Western blot. (B) The secretion levels of IL-6, TNF-α, and IL-12 p40 in cell culture supernatants were measured by ELISA. (C) Macrophages treated or not with small-interfering RNA (siRNA) targeting TLR9 (siTLR9) were stimulated with Giardia lamblia virus (GLV)–free or GLV-containing Giardia trophozoites for 3 h. (D) A total of 3 × 10 6 WT macrophages pretreated or not with siTLR9 were incubated for 3 h with 1 × 10 6 GLV-free Giardia trophozoites or 1 × 10 6 GLV-containing Giardia trophozoites, following which TLR9 expression levels were analyzed by Western blot. Relative protein expression was quantified by densitometric analysis using β-actin as an internal reference. Data are expressed as means ± SD from three separate experiments. ns, no significant difference, * p

    Article Snippet: After blocking with 5% bovine serum albumin (BSA) in Tris-buffered saline 0.1 Tween 20 (TBST) for 2 h at room temperature, the membranes were incubated overnight at 4°C with primary antibodies targeting TLR9, p38, ERK, AKT, NF-κB p65, phospho-p38, phospho-ERK, phospho-AKT, phospho-p65, phospho-IκBα, β-actin (all rabbit), and IκBα (mouse) (all from Cell Signaling Technology, Danvers, MA, United States) diluted 1/1,000 in 5% BSA.

    Techniques: Western Blot, Cell Culture, Enzyme-linked Immunosorbent Assay, Small Interfering RNA, Incubation, Expressing

    The effects of nobiletin on the intracellular phosphorylation of p38 MAPK, ERK, and JNK in IL-1β-stimulated HPDLCs. HPDLCs were treated with nobiletin (0, 50, or 100 μM) for 24 h, followed by stimulation with or without IL-1β (1 ng/mL) for 15, 30, or 60 min. Western blot analysis was conducted to assess the expression of phospho-p38 MAPK, p38 MAPK, phospho-ERK, ERK, phospho-JNK, JNK and, GAPDH. Each photograph is representative of data of 3 separate experiments.

    Journal: Pharmaceutics

    Article Title: Nobiletin Inhibits Inflammatory Reaction in Interleukin-1β-Stimulated Human Periodontal Ligament Cells

    doi: 10.3390/pharmaceutics13050667

    Figure Lengend Snippet: The effects of nobiletin on the intracellular phosphorylation of p38 MAPK, ERK, and JNK in IL-1β-stimulated HPDLCs. HPDLCs were treated with nobiletin (0, 50, or 100 μM) for 24 h, followed by stimulation with or without IL-1β (1 ng/mL) for 15, 30, or 60 min. Western blot analysis was conducted to assess the expression of phospho-p38 MAPK, p38 MAPK, phospho-ERK, ERK, phospho-JNK, JNK and, GAPDH. Each photograph is representative of data of 3 separate experiments.

    Article Snippet: Antibodies against phospho-p38 MAPK, phospho-extracellular signal-regulated kinase (ERK), phospho-c-Jun N-terminal kinase (JNK), phospho-IkappaB kinase (IKK)-α/β, phospho-NF-κB p65, phospho-Akt, p38 MAPK, ERK, JNK, IKK-α, NF-κB p65, Akt, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were purchased from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Western Blot, Expressing