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Cell Signaling Technology Inc iκb kinase
Model of proposed signaling pathway. In mature osteoclasts, TGF-β rapidly activates both SMAD and <t>TAK1.</t> TAK1 activation leads to sequential activation of MEK1/2, AKT, NIK, and IKKα/β, leading to phosphorylation of <t>IκB.</t> This causes targeted degradation of IκB, allowing subsequent NFκB nuclear localization to promote osteoclast survival. TGF-β-dependent SMAD2/3 activation and nuclear localization also occurs in parallel. NFκB activates transcription of BCLX L and Mcl-1 whereas SMAD2/3 activate transcription of Mcl-1.
Iκb Kinase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Article Title: TGF-? Coordinately Activates TAK1/MEK/AKT/NFkB and Smad Pathways to Promote Osteoclast Survival

Journal: Experimental cell research

doi: 10.1016/j.yexcr.2008.06.006

Model of proposed signaling pathway. In mature osteoclasts, TGF-β rapidly activates both SMAD and TAK1. TAK1 activation leads to sequential activation of MEK1/2, AKT, NIK, and IKKα/β, leading to phosphorylation of IκB. This causes targeted degradation of IκB, allowing subsequent NFκB nuclear localization to promote osteoclast survival. TGF-β-dependent SMAD2/3 activation and nuclear localization also occurs in parallel. NFκB activates transcription of BCLX L and Mcl-1 whereas SMAD2/3 activate transcription of Mcl-1.
Figure Legend Snippet: Model of proposed signaling pathway. In mature osteoclasts, TGF-β rapidly activates both SMAD and TAK1. TAK1 activation leads to sequential activation of MEK1/2, AKT, NIK, and IKKα/β, leading to phosphorylation of IκB. This causes targeted degradation of IκB, allowing subsequent NFκB nuclear localization to promote osteoclast survival. TGF-β-dependent SMAD2/3 activation and nuclear localization also occurs in parallel. NFκB activates transcription of BCLX L and Mcl-1 whereas SMAD2/3 activate transcription of Mcl-1.

Techniques Used: Activation Assay

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Article Title: TGF-? Coordinately Activates TAK1/MEK/AKT/NFkB and Smad Pathways to Promote Osteoclast Survival
Article Snippet: .. Anti phospho- and total antibodies directed toward Tak1 (Thr184/187), MEK 1/2 (Ser217/221), AKT (Ser473), Inhibitor of IκB Kinase (IKK)α/β (Ser176/180), Inhibitor of NFκB (IκB) (Ser32), and NFκB (Ser536) (Cell Signaling, Beverly, MA) were used at a 1:1,000 dilution for Western blotting according to the product directions as we have reported [ ]. .. Anti-tubulin hybridoma supernatant (E7) from The Developmental Studies Hybridoma Bank at the University of Iowa was also used at a 1:1,000 dilution.

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    Cell Signaling Technology Inc phosphorylated iκb kinase α β
    Curcumin modulated the nuclear factor-κB (NF-κB) pathway to alleviate inflammation. Liver tissues were prepared from the mice fed ND, MCD diet, or MCD/curcumin (100 mg/kg) diet. ( A ) The mRNA levels of hepatic Toll-like receptor 4 ( TLR4 ), Tumor necrosis factor-alpha ( TNF-α ) and Interleukin 6 ( IL-6 ) were measured by quantitative real-time polymerase chain reaction (qRT-PCR). ( B ) Representative immunoblot analyses of phosphorylated <t>IκB</t> kinase <t>α/β</t> (p-IKKα/β), p-IκBα, and p-NF-κB p65. ( C ) Liver sections were subjected to immunoblot and IHC analyses (original magnification 200×) for α-smooth muscle actin (α-SMA). Data are mean ± SD ( n = 7/group). * p
    Phosphorylated Iκb Kinase α β, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc iκb kinase α
    Effects of GMP hydrolysate obtained with papain for 1 h hydrolysis (GHP) on LPS-induced Nuclear factor-κB (NF-κB) activation in RAW264.7 macrophages. RAW264.7 macrophages were pretreated with/without the indicated concentrations of GHP and then stimulated with LPS (1 μg mL −1 ) for 30 min. Cell lysates were analyzed by Western blotting using specific antibodies against inhibitor of κB-α (IκBα), phosphorylated inhibitor of κB-α (pIκBα), Nuclear factor-κB p65 subunit (NF-κB p65) and phosphorylated <t>IκB</t> <t>kinase-α/β</t> (pIKKα/β).
    Iκb Kinase α, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/iκb kinase α/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc iκb kinase p ikk α β
    Troglitazone inhibits 12- O -tetradecanoylphorbol-13-acetate (TPA)-induced nuclear factor κB (NF-κB) activation in MCF-7 cells. (A) Cells were treated with troglitazone with TPA and nuclear extracts were prepared after 3 hours. Translocation of p65 and p50 into the nucleus and phosphorylation of <t>IκB</t> kinase (IKK) <t>α/β</t> and nuclear factor of κ light polypeptide gene enhancer in B cells inhibitor (IκB) α in cytosol was determined by western blots. Proliferating cell nuclear antigen (PCNA) was the loading control for nuclear proteins. (B) NF-κB-luc reporters and a Renilla luciferase thymidine kinase reporter vector were co-transfected into MCF-7 cells. Cells were treated with troglitazone with TPA and NF-κB promoter activity was measured with dual-luciferase reporter assays. (C) Cells were treated with troglitazone with TPA and nuclear extracts made after 3 hours. NF-κB DNA binding was analyzed by electrophoretic mobility shift assay. Values are mean±standard error of the mean of three independent experiments. * p
    Iκb Kinase P Ikk α β, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phosphorylated iκb kinase ikk α β
    HMFO-induced nuclear factor kappa B (NF-κB) activation by the phosphorylation of inhibitor of kappa B <t>(IκB)-α</t> and IκB kinase <t>(IKK)-α/β</t> in RAW 264.7 macrophages. Cells were stimulated with HMFO (50, 100, or 200 μg/mL) or LPS (1 μg/mL). ( A ) Nuclear extracts (N) were isolated from cells stimulated with HMFO or LPS. Level of p65 in the nuclear fractions was determined by immunoblotting analysis; ( B , C ) Phosphorylated IκB-α and IKKα/β isolated from cell lysates were determined by immunoblotting analysis. β-actin was used as an internal control. Values with the different letters are significantly different ( p
    Phosphorylated Iκb Kinase Ikk α β, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylated iκb kinase ikk α β/product/Cell Signaling Technology Inc
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylated iκb kinase ikk α β - by Bioz Stars, 2020-09
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    Curcumin modulated the nuclear factor-κB (NF-κB) pathway to alleviate inflammation. Liver tissues were prepared from the mice fed ND, MCD diet, or MCD/curcumin (100 mg/kg) diet. ( A ) The mRNA levels of hepatic Toll-like receptor 4 ( TLR4 ), Tumor necrosis factor-alpha ( TNF-α ) and Interleukin 6 ( IL-6 ) were measured by quantitative real-time polymerase chain reaction (qRT-PCR). ( B ) Representative immunoblot analyses of phosphorylated IκB kinase α/β (p-IKKα/β), p-IκBα, and p-NF-κB p65. ( C ) Liver sections were subjected to immunoblot and IHC analyses (original magnification 200×) for α-smooth muscle actin (α-SMA). Data are mean ± SD ( n = 7/group). * p

    Journal: Nutrients

    Article Title: Curcumin Ameliorates Nonalcoholic Fatty Liver Disease through Inhibition of O-GlcNAcylation

    doi: 10.3390/nu11112702

    Figure Lengend Snippet: Curcumin modulated the nuclear factor-κB (NF-κB) pathway to alleviate inflammation. Liver tissues were prepared from the mice fed ND, MCD diet, or MCD/curcumin (100 mg/kg) diet. ( A ) The mRNA levels of hepatic Toll-like receptor 4 ( TLR4 ), Tumor necrosis factor-alpha ( TNF-α ) and Interleukin 6 ( IL-6 ) were measured by quantitative real-time polymerase chain reaction (qRT-PCR). ( B ) Representative immunoblot analyses of phosphorylated IκB kinase α/β (p-IKKα/β), p-IκBα, and p-NF-κB p65. ( C ) Liver sections were subjected to immunoblot and IHC analyses (original magnification 200×) for α-smooth muscle actin (α-SMA). Data are mean ± SD ( n = 7/group). * p

    Article Snippet: After further washing in TBS-T, immunoprobed proteins were visualized using an enhanced chemiluminescence method (Visual Protein Co., Taipei, Taiwan) Antibodies against α-smooth muscle actin (α-SMA), O -GlcNAc (Sigma Aldrich, St. Louis, MO, USA), p-AMPKα, AMPKα, phosphorylated liver kinase B1 (p-LKB1), LKB1, phosphorylated Acetyl-CoA carboxylase (p-ACC), ACC, phosphorylated IκB kinase α/β (p-IKKα/β), IKKα, p-IκBα, p-NF-κB p65, IRE1α, OGT, SIRT1 (Cell signaling), Sterol regulatory element-binding protein (SREBP), fatty acid synthase (FAS), AnnexinA5 (ANXA5), peroxiredoxin 6 (Prx6), ChREBP, SOD1 (Santa Cruz, Dallas, TX, USA), Cytokeratin 8 (CK8), Cytokeratin 18 (CK18), and OGA (Abcam, Cambridge, MA, USA) were used as probes.

    Techniques: Mouse Assay, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Immunohistochemistry

    Effects of GMP hydrolysate obtained with papain for 1 h hydrolysis (GHP) on LPS-induced Nuclear factor-κB (NF-κB) activation in RAW264.7 macrophages. RAW264.7 macrophages were pretreated with/without the indicated concentrations of GHP and then stimulated with LPS (1 μg mL −1 ) for 30 min. Cell lysates were analyzed by Western blotting using specific antibodies against inhibitor of κB-α (IκBα), phosphorylated inhibitor of κB-α (pIκBα), Nuclear factor-κB p65 subunit (NF-κB p65) and phosphorylated IκB kinase-α/β (pIKKα/β).

    Journal: Nutrients

    Article Title: Endotoxin-Binding Peptides Derived from Casein Glycomacropeptide Inhibit Lipopolysaccharide-Stimulated Inflammatory Responses via Blockade of NF-κB activation in macrophages

    doi: 10.3390/nu7053119

    Figure Lengend Snippet: Effects of GMP hydrolysate obtained with papain for 1 h hydrolysis (GHP) on LPS-induced Nuclear factor-κB (NF-κB) activation in RAW264.7 macrophages. RAW264.7 macrophages were pretreated with/without the indicated concentrations of GHP and then stimulated with LPS (1 μg mL −1 ) for 30 min. Cell lysates were analyzed by Western blotting using specific antibodies against inhibitor of κB-α (IκBα), phosphorylated inhibitor of κB-α (pIκBα), Nuclear factor-κB p65 subunit (NF-κB p65) and phosphorylated IκB kinase-α/β (pIKKα/β).

    Article Snippet: Mouse monoclonal inhibitor of κB-α (IκBα, No. 4814) antibody and rabbit monoclonal Nuclear factor-κB p65 subunit (NF-κB p65, No. 8242), phosphorylated inhibitor of κB-α (pIκBα, No. 2859), IκB kinase-α (IKKα, No. 2682), IKKβ (No. 2370) and phosphorylated IKKα/β (pIKKα/β, No. 2697) antibodies were purchased from Cell Signaling Technology (CST, Beverly, MA, USA). β-actin, histone H4 and horseradish peroxidase-conjugated anti-species (mouse and rabbit) secondary antibodies were purchased from Beyotime Biotech (Haimen, Jiangsu, China).

    Techniques: Activation Assay, Western Blot

    Troglitazone inhibits 12- O -tetradecanoylphorbol-13-acetate (TPA)-induced nuclear factor κB (NF-κB) activation in MCF-7 cells. (A) Cells were treated with troglitazone with TPA and nuclear extracts were prepared after 3 hours. Translocation of p65 and p50 into the nucleus and phosphorylation of IκB kinase (IKK) α/β and nuclear factor of κ light polypeptide gene enhancer in B cells inhibitor (IκB) α in cytosol was determined by western blots. Proliferating cell nuclear antigen (PCNA) was the loading control for nuclear proteins. (B) NF-κB-luc reporters and a Renilla luciferase thymidine kinase reporter vector were co-transfected into MCF-7 cells. Cells were treated with troglitazone with TPA and NF-κB promoter activity was measured with dual-luciferase reporter assays. (C) Cells were treated with troglitazone with TPA and nuclear extracts made after 3 hours. NF-κB DNA binding was analyzed by electrophoretic mobility shift assay. Values are mean±standard error of the mean of three independent experiments. * p

    Journal: Journal of Breast Cancer

    Article Title: Troglitazone Inhibits Matrix Metalloproteinase-9 Expression and Invasion of Breast Cancer Cell through a Peroxisome Proliferator-Activated Receptor γ-Dependent Mechanism

    doi: 10.4048/jbc.2018.21.1.28

    Figure Lengend Snippet: Troglitazone inhibits 12- O -tetradecanoylphorbol-13-acetate (TPA)-induced nuclear factor κB (NF-κB) activation in MCF-7 cells. (A) Cells were treated with troglitazone with TPA and nuclear extracts were prepared after 3 hours. Translocation of p65 and p50 into the nucleus and phosphorylation of IκB kinase (IKK) α/β and nuclear factor of κ light polypeptide gene enhancer in B cells inhibitor (IκB) α in cytosol was determined by western blots. Proliferating cell nuclear antigen (PCNA) was the loading control for nuclear proteins. (B) NF-κB-luc reporters and a Renilla luciferase thymidine kinase reporter vector were co-transfected into MCF-7 cells. Cells were treated with troglitazone with TPA and NF-κB promoter activity was measured with dual-luciferase reporter assays. (C) Cells were treated with troglitazone with TPA and nuclear extracts made after 3 hours. NF-κB DNA binding was analyzed by electrophoretic mobility shift assay. Values are mean±standard error of the mean of three independent experiments. * p

    Article Snippet: Phosphorylated (p)-c-Jun, nuclear factor of κ light polypeptide gene enhancer in B cells inhibitor (p-IκB) α, IκB kinase (p-IKK) α/β, c-Jun N-terminal kinases (JNK), p-JNK, extracellular signal-regulated kinases (ERK), p-ERK, and p-protein kinase B (AKT) antibodies were purchased from Cell Signaling Technology (Danvers, USA).

    Techniques: Activation Assay, Translocation Assay, Western Blot, Luciferase, Plasmid Preparation, Transfection, Activity Assay, Binding Assay, Electrophoretic Mobility Shift Assay

    HMFO-induced nuclear factor kappa B (NF-κB) activation by the phosphorylation of inhibitor of kappa B (IκB)-α and IκB kinase (IKK)-α/β in RAW 264.7 macrophages. Cells were stimulated with HMFO (50, 100, or 200 μg/mL) or LPS (1 μg/mL). ( A ) Nuclear extracts (N) were isolated from cells stimulated with HMFO or LPS. Level of p65 in the nuclear fractions was determined by immunoblotting analysis; ( B , C ) Phosphorylated IκB-α and IKKα/β isolated from cell lysates were determined by immunoblotting analysis. β-actin was used as an internal control. Values with the different letters are significantly different ( p

    Journal: Nutrients

    Article Title: Immune-Enhancing Effects of a High Molecular Weight Fraction of Cynanchum wilfordii Hemsley in Macrophages and Immunosuppressed Mice

    doi: 10.3390/nu8100600

    Figure Lengend Snippet: HMFO-induced nuclear factor kappa B (NF-κB) activation by the phosphorylation of inhibitor of kappa B (IκB)-α and IκB kinase (IKK)-α/β in RAW 264.7 macrophages. Cells were stimulated with HMFO (50, 100, or 200 μg/mL) or LPS (1 μg/mL). ( A ) Nuclear extracts (N) were isolated from cells stimulated with HMFO or LPS. Level of p65 in the nuclear fractions was determined by immunoblotting analysis; ( B , C ) Phosphorylated IκB-α and IKKα/β isolated from cell lysates were determined by immunoblotting analysis. β-actin was used as an internal control. Values with the different letters are significantly different ( p

    Article Snippet: Antibodies against phosphorylated-inhibitor of kappa B (IκB)-α, phosphorylated-IκB kinase (IKK)-α/β, and phosphorylated-p38 were purchased from Cell Signaling Technology, Inc. (Beverly, MA, USA).

    Techniques: Activation Assay, Isolation