bay11 7082  (Millipore)

 
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    Name:
    Bay 11 7082
    Description:

    Catalog Number:
    B5556
    Price:
    None
    Applications:
    Bay 11-7082 has been used as:. a nuclear factor-kappa B (NF-kB) inhibitor to verify the action of the NF-kB signaling pathway in the production of interleukin (IL)-8. a nuclear factor-kappa B (NF-kB) inhibitor to study the role of NF-kB activation in Mycoplasma hyorhinis -induced epithelial-mesenchymal transition (EMT) and cell migration. a nod-like receptor family pyrin domain containing 3 (NLRP3) selective inhibitor to examine its effects on liver inflammation in mice after hematopoietic stem cell transplantation
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    Structured Review

    Millipore bay11 7082
    Bay 11 7082

    https://www.bioz.com/result/bay11 7082/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bay11 7082 - by Bioz Stars, 2021-09
    99/100 stars

    Images

    1) Product Images from "Aconine inhibits RANKL-induced osteoclast differentiation in RAW264.7 cells by suppressing NF-κB and NFATc1 activation and DC-STAMP expression"

    Article Title: Aconine inhibits RANKL-induced osteoclast differentiation in RAW264.7 cells by suppressing NF-κB and NFATc1 activation and DC-STAMP expression

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2015.85

    Aconine inhibits RANKL-induced NF-κB activation. (A) RAW264.7 cells that were stably transfected with a NF-κB luciferase reporter construct were pretreated with varying concentrations of aconine and the NF-κB inhibitor, BAY11-7082,
    Figure Legend Snippet: Aconine inhibits RANKL-induced NF-κB activation. (A) RAW264.7 cells that were stably transfected with a NF-κB luciferase reporter construct were pretreated with varying concentrations of aconine and the NF-κB inhibitor, BAY11-7082,

    Techniques Used: Activation Assay, Stable Transfection, Transfection, Luciferase, Construct

    2) Product Images from "Targeting xCT, a cystine-glutamate transporter induces apoptosis and tumor regression for KSHV/HIV-associated lymphoma"

    Article Title: Targeting xCT, a cystine-glutamate transporter induces apoptosis and tumor regression for KSHV/HIV-associated lymphoma

    Journal: Journal of Hematology & Oncology

    doi: 10.1186/1756-8722-7-30

    xCT inhibition induces intracellular ROS levels through upregulation of NADPH oxidases activities from KSHV-infected PEL cells. (A) BCP-1 and BCBL-1 were incubated with either MSG or SASP at the indicated concentrations for 24 h, then intracellular reactive oxygen species (ROS) were quantified using the ROS-specific dye CM-H2DCFDA and flow cytometry, and normalized to ROS levels for the vehicle-incubated cells. NF-κB inhibitor Bay11-7082 was used as a positive control. (B-C) BCP-1 and BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle for 24 h, then proteins expression were measured by immuoblots. NADPH oxidases activities were measured as described in Methods. (D) BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle in the presence or absence of the antioxidant N -acetylcysteine (NAC) 2.5 mM for 48 h, then cell apoptosis was assessed using Annexin V-PI staining and flow cytometry analysis (** vs MSG group; ## vs SASP group). Error bars represent the S.E.M. for 3 independent experiments. * = p
    Figure Legend Snippet: xCT inhibition induces intracellular ROS levels through upregulation of NADPH oxidases activities from KSHV-infected PEL cells. (A) BCP-1 and BCBL-1 were incubated with either MSG or SASP at the indicated concentrations for 24 h, then intracellular reactive oxygen species (ROS) were quantified using the ROS-specific dye CM-H2DCFDA and flow cytometry, and normalized to ROS levels for the vehicle-incubated cells. NF-κB inhibitor Bay11-7082 was used as a positive control. (B-C) BCP-1 and BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle for 24 h, then proteins expression were measured by immuoblots. NADPH oxidases activities were measured as described in Methods. (D) BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle in the presence or absence of the antioxidant N -acetylcysteine (NAC) 2.5 mM for 48 h, then cell apoptosis was assessed using Annexin V-PI staining and flow cytometry analysis (** vs MSG group; ## vs SASP group). Error bars represent the S.E.M. for 3 independent experiments. * = p

    Techniques Used: Inhibition, Infection, Incubation, Flow Cytometry, Cytometry, Positive Control, Expressing, Staining

    3) Product Images from "Monocytic microparticles activate endothelial cells in an IL-1?-dependent manner"

    Article Title: Monocytic microparticles activate endothelial cells in an IL-1?-dependent manner

    Journal: Blood

    doi: 10.1182/blood-2011-01-330878

    MPs released by LPS-treated THP-1 cells induce the expression of cell adhesion molecules by HUVECs. (A) HUVECs were incubated for 1 or 2 hours in serum-free conditions with MPs from untreated or LPS-treated THP-1 cells or 10 ng/mL TNF-α. ICAM-1 , VCAM-1 , and E-selectin mRNA expression was measured by real-time polymerase chain reaction. (B) HUVECs were incubated for 4 hours in serum-free conditions with MPs derived from LPS-treated or untreated THP-1 cells or 10 ng/mL TNF-α. Expression of VCAM-1, E-selectin, and ICAM-1 by HUVECs was detected by Western blot. (C) HUVECs were incubated for 4 hours in serum-free conditions with MPs from LPS-treated PBMCs or 10 ng/mL TNF-α. VCAM-1 was detected by Western blot. (D) HUVECs were treated with 5 or 10μM of the NF-κB pathway inhibitors MG-132, Bay11–7082, or vehicle control (dimethyl sulfoxide [DMSO]) and then stimulated with MPs from LPS-treated THP-1 cells. VCAM-1 was detected by Western blot. GAPDH served as a loading control. Results are representative of 3 independent experiments.
    Figure Legend Snippet: MPs released by LPS-treated THP-1 cells induce the expression of cell adhesion molecules by HUVECs. (A) HUVECs were incubated for 1 or 2 hours in serum-free conditions with MPs from untreated or LPS-treated THP-1 cells or 10 ng/mL TNF-α. ICAM-1 , VCAM-1 , and E-selectin mRNA expression was measured by real-time polymerase chain reaction. (B) HUVECs were incubated for 4 hours in serum-free conditions with MPs derived from LPS-treated or untreated THP-1 cells or 10 ng/mL TNF-α. Expression of VCAM-1, E-selectin, and ICAM-1 by HUVECs was detected by Western blot. (C) HUVECs were incubated for 4 hours in serum-free conditions with MPs from LPS-treated PBMCs or 10 ng/mL TNF-α. VCAM-1 was detected by Western blot. (D) HUVECs were treated with 5 or 10μM of the NF-κB pathway inhibitors MG-132, Bay11–7082, or vehicle control (dimethyl sulfoxide [DMSO]) and then stimulated with MPs from LPS-treated THP-1 cells. VCAM-1 was detected by Western blot. GAPDH served as a loading control. Results are representative of 3 independent experiments.

    Techniques Used: Expressing, Incubation, Real-time Polymerase Chain Reaction, Derivative Assay, Western Blot

    4) Product Images from "The signal transduction pathway of PKC/NF-?B/c-fos may be involved in the influence of high glucose on the cardiomyocytes of neonatal rats"

    Article Title: The signal transduction pathway of PKC/NF-?B/c-fos may be involved in the influence of high glucose on the cardiomyocytes of neonatal rats

    Journal: Cardiovascular Diabetology

    doi: 10.1186/1475-2840-8-8

    Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on TNF-α expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher expression of TNF-α compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L) and NF-κB inhibitor BAY11-7082 (5 μmol/L), the expression of TNF-α decreased compared with the cardiomyocytes cultured in high glucose levels as shown in figure 5. Treatment with mannital, used as an osmotic control, had no significant effect on the expression of TNF-α in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P
    Figure Legend Snippet: Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on TNF-α expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher expression of TNF-α compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L) and NF-κB inhibitor BAY11-7082 (5 μmol/L), the expression of TNF-α decreased compared with the cardiomyocytes cultured in high glucose levels as shown in figure 5. Treatment with mannital, used as an osmotic control, had no significant effect on the expression of TNF-α in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P

    Techniques Used: Expressing, Cell Culture

    Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on total cellular NF-κB expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher expression and increased activity of NF-κB compared with control group. After adding PKC inhibitor Ro-31-8220(50 nmol/L) and NF-κB inhibitor BAY11-7082(5 μmol/L), the expression and activity of NF-κB decreased as shown in figure 3. Treatment with mannital, used as an osmotic control, had no significant effect on the expression of NF-κB in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P
    Figure Legend Snippet: Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on total cellular NF-κB expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher expression and increased activity of NF-κB compared with control group. After adding PKC inhibitor Ro-31-8220(50 nmol/L) and NF-κB inhibitor BAY11-7082(5 μmol/L), the expression and activity of NF-κB decreased as shown in figure 3. Treatment with mannital, used as an osmotic control, had no significant effect on the expression of NF-κB in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P

    Techniques Used: Expressing, Cell Culture, Activity Assay

    Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on nuclear NF-κB expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher nuclear protein expression and activity of NF-κB compared with control group. After adding PKC inhibitor Ro-31-8220(50 nmol/L) and NF-κB inhibitor BAY11-7082(5 μmol/L) the expression and activity of nuclear NF-κB decreased as shown in figure 4. Treatment with mannital, used as an osmotic control, had no significant effect on the nuclear expression of NF-κB in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P
    Figure Legend Snippet: Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on nuclear NF-κB expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher nuclear protein expression and activity of NF-κB compared with control group. After adding PKC inhibitor Ro-31-8220(50 nmol/L) and NF-κB inhibitor BAY11-7082(5 μmol/L) the expression and activity of nuclear NF-κB decreased as shown in figure 4. Treatment with mannital, used as an osmotic control, had no significant effect on the nuclear expression of NF-κB in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P

    Techniques Used: Expressing, Cell Culture, Activity Assay

    Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on c-fos expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher expression of c-fos compared with control group. After adding PKC inhibitor Ro-31-8220(50 nmol/L) and NF-κB inhibitor BAY11-7082(5 μmol/L) to the cardiomyocytes cultured in high glucose levels, the expression of c-fos decreased as shown in figure 6. Treatment with mannital, used as an osmotic control, had no significant effect on the expression of c-fos in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P
    Figure Legend Snippet: Effect of high glucose and PKC inhibitor Ro-31-8220, NF-κB inhibitor BAY11-7082 on c-fos expression in cardiomyocytes . Cardiomyocytes cultured in high glucose levels showed higher expression of c-fos compared with control group. After adding PKC inhibitor Ro-31-8220(50 nmol/L) and NF-κB inhibitor BAY11-7082(5 μmol/L) to the cardiomyocytes cultured in high glucose levels, the expression of c-fos decreased as shown in figure 6. Treatment with mannital, used as an osmotic control, had no significant effect on the expression of c-fos in cardiomyocytes. The results were expressed as means ± SE ( n = 4 or 5). * P

    Techniques Used: Expressing, Cell Culture

    5) Product Images from "Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an NF-?B-Dependent Manner ▿"

    Article Title: Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an NF-?B-Dependent Manner ▿

    Journal: Eukaryotic Cell

    doi: 10.1128/EC.00371-07

    B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. Iodoacetamide, a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P
    Figure Legend Snippet: B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. Iodoacetamide, a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P

    Techniques Used: Activation Assay, Western Blot, Protease Inhibitor, Binding Assay, Activity Assay, Mutagenesis, Incubation, Enzyme-linked Immunosorbent Assay

    B. ratti WR1 induces up-regulation of IL-8 mRNA levels in T84 cells. T84 cells were coincubated with live WR1 parasites or parasite lysate for 12 h. Total cellular RNA was isolated, and IL-8 and β-actin mRNA levels were measured by quantitative real-time RT-PCR as described in Materials and Methods. WR1 lysate caused a significant increase in IL-8 mRNA levels. A significant decrease in IL-8 mRNA levels was noticed after treatment with the NF-κB inhibitor BAY11-7082 and the cysteine protease inhibitor iodoacetamide. The increase in IL-8 mRNA relative to untreated T84 cells was calculated for each experiment based on internal β-actin controls. The values are means ± standard deviations ( n = 3). *, P
    Figure Legend Snippet: B. ratti WR1 induces up-regulation of IL-8 mRNA levels in T84 cells. T84 cells were coincubated with live WR1 parasites or parasite lysate for 12 h. Total cellular RNA was isolated, and IL-8 and β-actin mRNA levels were measured by quantitative real-time RT-PCR as described in Materials and Methods. WR1 lysate caused a significant increase in IL-8 mRNA levels. A significant decrease in IL-8 mRNA levels was noticed after treatment with the NF-κB inhibitor BAY11-7082 and the cysteine protease inhibitor iodoacetamide. The increase in IL-8 mRNA relative to untreated T84 cells was calculated for each experiment based on internal β-actin controls. The values are means ± standard deviations ( n = 3). *, P

    Techniques Used: Isolation, Quantitative RT-PCR, Protease Inhibitor

    6) Product Images from "Inflammation and hypoxia linked to renal injury by CCAAT/enhancer-binding protein δ"

    Article Title: Inflammation and hypoxia linked to renal injury by CCAAT/enhancer-binding protein δ

    Journal: Kidney International

    doi: 10.1038/ki.2015.21

    The nuclear factor (NF)-κB pathway regulates the CCAAT/enhancer-binding protein δ/hypoxia-inducible factor 1 (CEBPD/HIF-1) pathway under hypoxia or interleukin (IL)-1β treatment. ( a ) NF-κB reporter activity was measured under normoxia or hypoxia. The pRL-TK vector served as a control. Hypoxia (0.1% O 2 , 6 h) increased NF-κB activity in HK-2 cells. ( b ) Inhibition of the NF-κB pathway by p65 knockdown significantly decreased HREluc activity under hypoxia in HK-2 cells. ( c ) (Upper panel) HK-2 cells were pretreated with BAY11-7082 (IKK inhibitor, 10 μ M ) or dimethyl sulfoxide (for control) for 30 min and then treated with hypoxia (upper left panel) or IL-1β (1 ng/ml; upper right panel) for 6 h. CEBPD and HIF-1α protein induction under both conditions were inhibited. The same phenomena were observed using small interfering RNA (siRNA) against p65-mediated NF-κB inhibition (lower left panel for hypoxia and lower right panel for IL-1β). ( d ) Human CEBPD stable overexpression HK-2 clones were generated using a retroviral system. Upon NF-κB inhibition by BAY11-7082 (10 μ M ), HIF-1α protein induction under hypoxia (left panel) or IL-1β (1 ng/ml; right panel) was reduced in control HK-2 cells. In stable CEBPD-expressed HK-2 cells, the HIF-1α protein induction was restored under both conditions, indicating the necessity for HIF-1α protein regulation by CEBPD. The endogenous CEBPD protein is hardly detected, because exposure time was optimized for the overexpressed protein. Bar graph (mean±s.e.m. or representative of at least three independent experiments) statistics performed using two-way analysis of variance with Bonferroni's post-hoc tests. ** P
    Figure Legend Snippet: The nuclear factor (NF)-κB pathway regulates the CCAAT/enhancer-binding protein δ/hypoxia-inducible factor 1 (CEBPD/HIF-1) pathway under hypoxia or interleukin (IL)-1β treatment. ( a ) NF-κB reporter activity was measured under normoxia or hypoxia. The pRL-TK vector served as a control. Hypoxia (0.1% O 2 , 6 h) increased NF-κB activity in HK-2 cells. ( b ) Inhibition of the NF-κB pathway by p65 knockdown significantly decreased HREluc activity under hypoxia in HK-2 cells. ( c ) (Upper panel) HK-2 cells were pretreated with BAY11-7082 (IKK inhibitor, 10 μ M ) or dimethyl sulfoxide (for control) for 30 min and then treated with hypoxia (upper left panel) or IL-1β (1 ng/ml; upper right panel) for 6 h. CEBPD and HIF-1α protein induction under both conditions were inhibited. The same phenomena were observed using small interfering RNA (siRNA) against p65-mediated NF-κB inhibition (lower left panel for hypoxia and lower right panel for IL-1β). ( d ) Human CEBPD stable overexpression HK-2 clones were generated using a retroviral system. Upon NF-κB inhibition by BAY11-7082 (10 μ M ), HIF-1α protein induction under hypoxia (left panel) or IL-1β (1 ng/ml; right panel) was reduced in control HK-2 cells. In stable CEBPD-expressed HK-2 cells, the HIF-1α protein induction was restored under both conditions, indicating the necessity for HIF-1α protein regulation by CEBPD. The endogenous CEBPD protein is hardly detected, because exposure time was optimized for the overexpressed protein. Bar graph (mean±s.e.m. or representative of at least three independent experiments) statistics performed using two-way analysis of variance with Bonferroni's post-hoc tests. ** P

    Techniques Used: Binding Assay, Activity Assay, Plasmid Preparation, Inhibition, Small Interfering RNA, Over Expression, Clone Assay, Generated

    7) Product Images from "Breviscapine ameliorates hypertrophy of cardiomyocytes induced by high glucose in diabetic rats via the PKC signaling pathway"

    Article Title: Breviscapine ameliorates hypertrophy of cardiomyocytes induced by high glucose in diabetic rats via the PKC signaling pathway

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2009.95

    Breviscapine decreased the expression of TNF-α in high glucose cultured cardiomyocytes. Cardiomyocytes cultured in high glucose levels showed higher expression of TNF-α compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L), NF-κB inhibitor BAY11-7082 (5 μmol/L) and breviscapine (10, 20, and 60 mmol/L), the expression of TNF-α decreased compared with the cardiomyocytes cultured in high glucose levels as shown in Figure 4 . The results were expressed as means±SEM. n =4 or 5. b P
    Figure Legend Snippet: Breviscapine decreased the expression of TNF-α in high glucose cultured cardiomyocytes. Cardiomyocytes cultured in high glucose levels showed higher expression of TNF-α compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L), NF-κB inhibitor BAY11-7082 (5 μmol/L) and breviscapine (10, 20, and 60 mmol/L), the expression of TNF-α decreased compared with the cardiomyocytes cultured in high glucose levels as shown in Figure 4 . The results were expressed as means±SEM. n =4 or 5. b P

    Techniques Used: Expressing, Cell Culture

    Breviscapine decreased the expression of c-fos in high glucose cultured cardiomyocytes. Cardiomyocytes cultured in high glucose levels showed higher expression of c-fos compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L), NF-κB inhibitor BAY11-7082 (5 μmol/L) and breviscapine (10, 20, and 60 mmol/L), the expression of c-fos decreased as shown in Figure 5 . The results were expressed as means±SEM. n =4 or 5. b P
    Figure Legend Snippet: Breviscapine decreased the expression of c-fos in high glucose cultured cardiomyocytes. Cardiomyocytes cultured in high glucose levels showed higher expression of c-fos compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L), NF-κB inhibitor BAY11-7082 (5 μmol/L) and breviscapine (10, 20, and 60 mmol/L), the expression of c-fos decreased as shown in Figure 5 . The results were expressed as means±SEM. n =4 or 5. b P

    Techniques Used: Expressing, Cell Culture

    Breviscapine decreased the expression of NF-κB in high glucose cultured cardiomyocytes. Cardiomyocytes cultured in high glucose levels showed higher expression and increased activity of NF-κB compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L), NF-κB inhibitor BAY11-7082 (5 μmol/L) and breviscapine (10, 20, and 60 mmol/L), the expression and activity of NF-κB decreased as shown in Figure 3 . The results were expressed as means±SEM. n =4 or 5. b P
    Figure Legend Snippet: Breviscapine decreased the expression of NF-κB in high glucose cultured cardiomyocytes. Cardiomyocytes cultured in high glucose levels showed higher expression and increased activity of NF-κB compared with control group. After adding PKC inhibitor Ro-31-8220 (50 nmol/L), NF-κB inhibitor BAY11-7082 (5 μmol/L) and breviscapine (10, 20, and 60 mmol/L), the expression and activity of NF-κB decreased as shown in Figure 3 . The results were expressed as means±SEM. n =4 or 5. b P

    Techniques Used: Expressing, Cell Culture, Activity Assay

    8) Product Images from "Aconine inhibits RANKL-induced osteoclast differentiation in RAW264.7 cells by suppressing NF-κB and NFATc1 activation and DC-STAMP expression"

    Article Title: Aconine inhibits RANKL-induced osteoclast differentiation in RAW264.7 cells by suppressing NF-κB and NFATc1 activation and DC-STAMP expression

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2015.85

    Aconine inhibits RANKL-induced NF-κB activation. (A) RAW264.7 cells that were stably transfected with a NF-κB luciferase reporter construct were pretreated with varying concentrations of aconine and the NF-κB inhibitor, BAY11-7082, for 30 min and then treated with RANKL (100 ng/mL) for 8 h. (B) RAW264.7 cells were pretreated with aconine for 30 min prior to RANKL (100 ng/mL) stimulation for 30 min. Then, whole cytoplasmic and nuclear proteins were extracted as described in the methods. The expression levels of IκB-α, NF-κB p65 in the cytoplasmic and NF-κB p65 in the nuclear extracts were determined using Western blot analysis. Subcellular fraction purity and the equality of sample loading were evaluated by analyzing the levels of β-actin and Lamin B1. Protein levels were quantified using densitometry. Mean±SEM. n =3. b P
    Figure Legend Snippet: Aconine inhibits RANKL-induced NF-κB activation. (A) RAW264.7 cells that were stably transfected with a NF-κB luciferase reporter construct were pretreated with varying concentrations of aconine and the NF-κB inhibitor, BAY11-7082, for 30 min and then treated with RANKL (100 ng/mL) for 8 h. (B) RAW264.7 cells were pretreated with aconine for 30 min prior to RANKL (100 ng/mL) stimulation for 30 min. Then, whole cytoplasmic and nuclear proteins were extracted as described in the methods. The expression levels of IκB-α, NF-κB p65 in the cytoplasmic and NF-κB p65 in the nuclear extracts were determined using Western blot analysis. Subcellular fraction purity and the equality of sample loading were evaluated by analyzing the levels of β-actin and Lamin B1. Protein levels were quantified using densitometry. Mean±SEM. n =3. b P

    Techniques Used: Activation Assay, Stable Transfection, Transfection, Luciferase, Construct, Expressing, Western Blot

    9) Product Images from "p53-mediated delayed NF-κB activity enhances etoposide-induced cell death in medulloblastoma"

    Article Title: p53-mediated delayed NF-κB activity enhances etoposide-induced cell death in medulloblastoma

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2010.16

    MB cell lines displayed different sensitivity to etoposide involving both caspase-dependent and -independent cell death. ( a ) Cell viability was analysed by MTS assay at indicated time points, upon 20 μ M etoposide treatment. ( b ) Viability of D283-MED cells treated with 20 μ M etoposide in the presence of 5 μ M Bay11-7082, 10 μ M Wedelolactone or 5 μ M JSH23 was assessed by MTS assay. ( c ) D283-Med cells were transfected with 100 nM of siRNA directed against p65 or a control scrambled siRNA. After 48 h, cells were treated with 20 μ M etoposide for 8 h and viability was assessed by MTS assay. The knockdown efficiency was controlled by western blot (insert). ( d ) Several MB cell lines were treated with 20 μ M etoposide for indicated times. Caspase 3/7 activity was measured with Caspase-Glo 3/7 assay kit. Results are expressed as fold-induction compared with control non-treated cells as a function of time. ( e ) D283-MED cells were treated with 20 μ M etoposide in presence or absence of 5 μ M Bay11-7082 for 8 h. Caspase 8 and 3/7 activities were assessed with Caspase-Glo assay kits. Results are relative to control non-treated cells. a – d results are the mean of three independent experiments±S.E.M. ‘ *** ' indicates statistical difference with P
    Figure Legend Snippet: MB cell lines displayed different sensitivity to etoposide involving both caspase-dependent and -independent cell death. ( a ) Cell viability was analysed by MTS assay at indicated time points, upon 20 μ M etoposide treatment. ( b ) Viability of D283-MED cells treated with 20 μ M etoposide in the presence of 5 μ M Bay11-7082, 10 μ M Wedelolactone or 5 μ M JSH23 was assessed by MTS assay. ( c ) D283-Med cells were transfected with 100 nM of siRNA directed against p65 or a control scrambled siRNA. After 48 h, cells were treated with 20 μ M etoposide for 8 h and viability was assessed by MTS assay. The knockdown efficiency was controlled by western blot (insert). ( d ) Several MB cell lines were treated with 20 μ M etoposide for indicated times. Caspase 3/7 activity was measured with Caspase-Glo 3/7 assay kit. Results are expressed as fold-induction compared with control non-treated cells as a function of time. ( e ) D283-MED cells were treated with 20 μ M etoposide in presence or absence of 5 μ M Bay11-7082 for 8 h. Caspase 8 and 3/7 activities were assessed with Caspase-Glo assay kits. Results are relative to control non-treated cells. a – d results are the mean of three independent experiments±S.E.M. ‘ *** ' indicates statistical difference with P

    Techniques Used: MTS Assay, Transfection, Western Blot, Activity Assay, Caspase-Glo Assay

    Etoposide induces a delayed p65 activation in some MB cells. ( a ) Four MB cell lines were treated with 20 μ M etoposide for 6 h. p65 and p65-Ser536 phosphorylation levels were assessed by western blot. The blot presented is representative of three independent experiments. Quantification of the bands was plotted as p65 phosphorylation fold increase compared with the control non-treated cells. ( b ) After 24 h transfection with NF-luc plasmid, cells were treated with 20 μ M etoposide for 8 h before assessment of the luciferase activity. Relative luminescence measurements to t0 are plotted for each cell line. ( c ) D283-MED cells were simultaneously treated for 6 h with 20 μ M etoposide and 5 μ M Bay11-7082 or 10 μ M BMS-345541. p65 phosphorylation was analysed by western blot. The blot presented is representative of three independent experiments and the plot represents the quantification of the blot shown. ( d ) D283-MED cells transfected with p65-RedXP and I κ B α -EGFP were treated with 20 μ M etoposide or 10 ng/ml TNF α . Time-lapse confocal microscopy was performed as described in Materials and Methods. Mean fluorescence intensities for individual cells were analysed. A typical cell for each treatment was plotted as the p65 nuclear/cytoplasmic ratio as a function of time. ( e ) D283-MED cells transfected with NF-Luc vector were treated with 20 μ M etoposide or 10 ng/ml TNF α . Real-time luminescence signal was captured as described in Materials and Methods. The graph represents mean luminescence intensities measured in whole field. ( f ) D283-MED cells were pretreated 30 min with 5 μ g/ml of the transcription inhibitor actinomycin-D, prior to a 10 min treatment with 10 ng/ml TNF α , or a 4 h treatment with 20 μ M etoposide. p65 phosphorylation levels were analysed by western blot. The blot presented is representative of three independent experiments and the plot represents the quantification of the blot shown
    Figure Legend Snippet: Etoposide induces a delayed p65 activation in some MB cells. ( a ) Four MB cell lines were treated with 20 μ M etoposide for 6 h. p65 and p65-Ser536 phosphorylation levels were assessed by western blot. The blot presented is representative of three independent experiments. Quantification of the bands was plotted as p65 phosphorylation fold increase compared with the control non-treated cells. ( b ) After 24 h transfection with NF-luc plasmid, cells were treated with 20 μ M etoposide for 8 h before assessment of the luciferase activity. Relative luminescence measurements to t0 are plotted for each cell line. ( c ) D283-MED cells were simultaneously treated for 6 h with 20 μ M etoposide and 5 μ M Bay11-7082 or 10 μ M BMS-345541. p65 phosphorylation was analysed by western blot. The blot presented is representative of three independent experiments and the plot represents the quantification of the blot shown. ( d ) D283-MED cells transfected with p65-RedXP and I κ B α -EGFP were treated with 20 μ M etoposide or 10 ng/ml TNF α . Time-lapse confocal microscopy was performed as described in Materials and Methods. Mean fluorescence intensities for individual cells were analysed. A typical cell for each treatment was plotted as the p65 nuclear/cytoplasmic ratio as a function of time. ( e ) D283-MED cells transfected with NF-Luc vector were treated with 20 μ M etoposide or 10 ng/ml TNF α . Real-time luminescence signal was captured as described in Materials and Methods. The graph represents mean luminescence intensities measured in whole field. ( f ) D283-MED cells were pretreated 30 min with 5 μ g/ml of the transcription inhibitor actinomycin-D, prior to a 10 min treatment with 10 ng/ml TNF α , or a 4 h treatment with 20 μ M etoposide. p65 phosphorylation levels were analysed by western blot. The blot presented is representative of three independent experiments and the plot represents the quantification of the blot shown

    Techniques Used: Activation Assay, Western Blot, Transfection, Plasmid Preparation, Luciferase, Activity Assay, Confocal Microscopy, Fluorescence

    10) Product Images from "Latent Membrane Protein 1 Regulates STAT1 through NF-?B-Dependent Interferon Secretion in Epstein-Barr Virus-Immortalized B Cells"

    Article Title: Latent Membrane Protein 1 Regulates STAT1 through NF-?B-Dependent Interferon Secretion in Epstein-Barr Virus-Immortalized B Cells

    Journal: Journal of Virology

    doi: 10.1128/JVI.79.8.4936-4943.2005

    Kinetics of the inhibition of the tyrosine phosphorylation of STAT1 in LCLs by the NF-κB specific inhibitor BAY11-7082. (A) Pri cells were treated with BAY11 (25 μM) for 30 min or 1, 2, 3, or 4 h (lanes 4 to 8). Control experiments were performed with DMSO (lanes 1 to 3). (B) LCL Pri cells were treated for 1 h with BAY11(40 μM) (lane 5). Cells were then resuspended in fresh medium without inhibitor for 2, 3, 4 or 5 h (lane 7 to 10). Control incubations were performed with DMSO (lanes 1 to 4). In lanes 2 and 6, cells were lysed immediately after resuspension in fresh medium to verify that the change of the medium in itself had no effect on the phosphorylation of STAT1. Similar results were obtained in three independent experiments.
    Figure Legend Snippet: Kinetics of the inhibition of the tyrosine phosphorylation of STAT1 in LCLs by the NF-κB specific inhibitor BAY11-7082. (A) Pri cells were treated with BAY11 (25 μM) for 30 min or 1, 2, 3, or 4 h (lanes 4 to 8). Control experiments were performed with DMSO (lanes 1 to 3). (B) LCL Pri cells were treated for 1 h with BAY11(40 μM) (lane 5). Cells were then resuspended in fresh medium without inhibitor for 2, 3, 4 or 5 h (lane 7 to 10). Control incubations were performed with DMSO (lanes 1 to 4). In lanes 2 and 6, cells were lysed immediately after resuspension in fresh medium to verify that the change of the medium in itself had no effect on the phosphorylation of STAT1. Similar results were obtained in three independent experiments.

    Techniques Used: Inhibition

    11) Product Images from "Lipocalin2 suppresses metastasis of colorectal cancer by attenuating NF-κB-dependent activation of snail and epithelial mesenchymal transition"

    Article Title: Lipocalin2 suppresses metastasis of colorectal cancer by attenuating NF-κB-dependent activation of snail and epithelial mesenchymal transition

    Journal: Molecular Cancer

    doi: 10.1186/s12943-016-0564-9

    LCN2 suppresses the NF-κB/snail signaling pathway and attenuates NF-κB promoter activity. a Western blots detection of p65 expression in LCN2-overexpressing and LCN2-knockdown cells. b Western blots detection, quantification of relative mRNA expression of snail expression in corresponding cells. c Immunofluorescence of snail expression and location in the indicated cells. d , e Western blots detection of EMT markers and snail changes ( d ) and quantification of relative mRNA expression of EMT markers ( e ) after treatment with LMB (20nM for 10 h) and Bay11-7082 (50 μM for 3 h) in corresponding cells. The grey value ratio of Vimentin/GAPDH was shown. f Survival analysis (Kaplan-Meier method, log-rank test) of combined LCN2 and NF-κB expression in CRC patients ( n = 126; group 1 ( n = 21, 3 died) vs group 2 ( n = 48, 17 died), P = .083; group 1 vs group 3 ( n = 27, 10 died), P = .088; group 1 vs group 4 ( n = 30, 13 died), P = .042). Values shown in real-time PCR assay are the mean ± SD from at least three independent experiments. (N, nuclear; P-phosphorylated). * P
    Figure Legend Snippet: LCN2 suppresses the NF-κB/snail signaling pathway and attenuates NF-κB promoter activity. a Western blots detection of p65 expression in LCN2-overexpressing and LCN2-knockdown cells. b Western blots detection, quantification of relative mRNA expression of snail expression in corresponding cells. c Immunofluorescence of snail expression and location in the indicated cells. d , e Western blots detection of EMT markers and snail changes ( d ) and quantification of relative mRNA expression of EMT markers ( e ) after treatment with LMB (20nM for 10 h) and Bay11-7082 (50 μM for 3 h) in corresponding cells. The grey value ratio of Vimentin/GAPDH was shown. f Survival analysis (Kaplan-Meier method, log-rank test) of combined LCN2 and NF-κB expression in CRC patients ( n = 126; group 1 ( n = 21, 3 died) vs group 2 ( n = 48, 17 died), P = .083; group 1 vs group 3 ( n = 27, 10 died), P = .088; group 1 vs group 4 ( n = 30, 13 died), P = .042). Values shown in real-time PCR assay are the mean ± SD from at least three independent experiments. (N, nuclear; P-phosphorylated). * P

    Techniques Used: Activity Assay, Western Blot, Expressing, Immunofluorescence, Real-time Polymerase Chain Reaction

    12) Product Images from "SARS-CoV-2 spike glycoprotein S1 induces neuroinflammation in BV-2 microglia"

    Article Title: SARS-CoV-2 spike glycoprotein S1 induces neuroinflammation in BV-2 microglia

    Journal: bioRxiv

    doi: 10.1101/2020.12.29.424619

    Pre-treatment with BAY11-7082 (1 µM) resulted in inhibition of SARS-CoV-2 spike S1 glycoprotein-induced increased production of NO (A), iNOS protein (B) in BV-2 microglia, following stimulation for 24 h. Culture supernatants were analysed using Griess assay, in-cell western (cytoblot) was used for iNOS detection. Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. *p
    Figure Legend Snippet: Pre-treatment with BAY11-7082 (1 µM) resulted in inhibition of SARS-CoV-2 spike S1 glycoprotein-induced increased production of NO (A), iNOS protein (B) in BV-2 microglia, following stimulation for 24 h. Culture supernatants were analysed using Griess assay, in-cell western (cytoblot) was used for iNOS detection. Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. *p

    Techniques Used: Inhibition, Griess Assay, In-Cell ELISA

    SARS-CoV-2 spike S1 glycoprotein activated NF-κB signalling in BV-2 microglia. Nuclear extracts were collected from cells stimulated with SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) in the absence or presence of BAY11-7082 (1 µM) for 60 min and subjected to DNA binding assays (A). Results of luciferase reporter gene assay showing increased NF-κB transcriptional activity by SARS-CoV-2 spike S1 glycoprotein and its inhibition by BAY11-7082 (1 µM) (B). In-cell western (cytoblot) analyses showing increased protein expressions of phospho-p65 sub-unit (C) and phospho-IκBα (D) following stimulation with SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) for 15 min and inhibition by BAY11-7082 (1 µM). Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. *p
    Figure Legend Snippet: SARS-CoV-2 spike S1 glycoprotein activated NF-κB signalling in BV-2 microglia. Nuclear extracts were collected from cells stimulated with SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) in the absence or presence of BAY11-7082 (1 µM) for 60 min and subjected to DNA binding assays (A). Results of luciferase reporter gene assay showing increased NF-κB transcriptional activity by SARS-CoV-2 spike S1 glycoprotein and its inhibition by BAY11-7082 (1 µM) (B). In-cell western (cytoblot) analyses showing increased protein expressions of phospho-p65 sub-unit (C) and phospho-IκBα (D) following stimulation with SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) for 15 min and inhibition by BAY11-7082 (1 µM). Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. *p

    Techniques Used: Binding Assay, Luciferase, Reporter Gene Assay, Activity Assay, Inhibition, In-Cell ELISA

    Pre-treatment with BAY11-7082 (1 µM) resulted in inhibition of SARS-CoV-2 spike S1 glycoprotein-induced increased production of TNFα (A), IL-6 (B) and IL-1β (C) in BV-2 microglia. Culture supernatants were analysed using ELISA following stimulation for 24 h. Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. **p□
    Figure Legend Snippet: Pre-treatment with BAY11-7082 (1 µM) resulted in inhibition of SARS-CoV-2 spike S1 glycoprotein-induced increased production of TNFα (A), IL-6 (B) and IL-1β (C) in BV-2 microglia. Culture supernatants were analysed using ELISA following stimulation for 24 h. Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. **p□

    Techniques Used: Inhibition, Enzyme-linked Immunosorbent Assay

    (A) Stimulation of BV-2 microglia with SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) increased protein expression of NLRP3 inflammasome, which was inhibited in the presence of CRID3 (1 µM) and BAY11-7082 (1 µM). (B) Increased caspase-1 activity by SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) BV-2 microglia was reduced in the presence of CRID3 (1 µM) and BAY11-7082 (1 µM). Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. *p
    Figure Legend Snippet: (A) Stimulation of BV-2 microglia with SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) increased protein expression of NLRP3 inflammasome, which was inhibited in the presence of CRID3 (1 µM) and BAY11-7082 (1 µM). (B) Increased caspase-1 activity by SARS-CoV-2 spike S1 glycoprotein (100 ng/mL) BV-2 microglia was reduced in the presence of CRID3 (1 µM) and BAY11-7082 (1 µM). Data were analysed using One-way ANOVA followed by a post hoc Tukey’s multiple comparison test. *p

    Techniques Used: Expressing, Activity Assay

    13) Product Images from "KSHV Manipulates Notch Signaling by DLL4 and JAG1 to Alter Cell Cycle Genes in Lymphatic Endothelia"

    Article Title: KSHV Manipulates Notch Signaling by DLL4 and JAG1 to Alter Cell Cycle Genes in Lymphatic Endothelia

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1000616

    vFLIP induces JAG1 expression in LEC through the NFκB pathway. (A) JAG1 mRNA levels in LEC and KLEC treated with BAY11-7082 (BAY11) or the equivalent volume of DMSO. Columns are the average fold change from two independent experiments. **, P
    Figure Legend Snippet: vFLIP induces JAG1 expression in LEC through the NFκB pathway. (A) JAG1 mRNA levels in LEC and KLEC treated with BAY11-7082 (BAY11) or the equivalent volume of DMSO. Columns are the average fold change from two independent experiments. **, P

    Techniques Used: Expressing

    14) Product Images from "NF-?B Inhibits Gammaherpesvirus Lytic Replication"

    Article Title: NF-?B Inhibits Gammaherpesvirus Lytic Replication

    Journal: Journal of Virology

    doi: 10.1128/JVI.77.15.8532-8540.2003

    NF-κB inhibitor Bay11-7082 induces lytic protein synthesis in latent KSHV- and EBV-infected cells. (A, C, and E) Western blots of HR-1 (A), KS-1 (B), and BCBL1 (C) whole-cell extracts. Cells were treated with sodium butyrate (A [Na.B]), TPA (C and E), or Bay11-7082. Blots were probed with nasopharyngeal carcinoma patient serum (A) or Kaposi's sarcoma patient serum recognizing several lytic antigens (C and E), polyclonal anti-RTA serum (E), and a MAb recognizing actin. DMSO, dimethyl sulfoxide. (B, D, and F) EMSA analysis of NF-κB activity in HR-1 (B), KS-1 (D), and BCBL1 (F) cells. Nuclear extracts were harvested directly after the 30-min treatment with Bay11-7082. Extracts were incubated with a consensus NF-κB binding site oligonucleotide. The specificity of the shifted complex was confirmed by using cold competitor oligonucleotides (comp.) and MAbs against p65 and FLAG (shift).
    Figure Legend Snippet: NF-κB inhibitor Bay11-7082 induces lytic protein synthesis in latent KSHV- and EBV-infected cells. (A, C, and E) Western blots of HR-1 (A), KS-1 (B), and BCBL1 (C) whole-cell extracts. Cells were treated with sodium butyrate (A [Na.B]), TPA (C and E), or Bay11-7082. Blots were probed with nasopharyngeal carcinoma patient serum (A) or Kaposi's sarcoma patient serum recognizing several lytic antigens (C and E), polyclonal anti-RTA serum (E), and a MAb recognizing actin. DMSO, dimethyl sulfoxide. (B, D, and F) EMSA analysis of NF-κB activity in HR-1 (B), KS-1 (D), and BCBL1 (F) cells. Nuclear extracts were harvested directly after the 30-min treatment with Bay11-7082. Extracts were incubated with a consensus NF-κB binding site oligonucleotide. The specificity of the shifted complex was confirmed by using cold competitor oligonucleotides (comp.) and MAbs against p65 and FLAG (shift).

    Techniques Used: Infection, Western Blot, Activity Assay, Incubation, Binding Assay

    15) Product Images from "Activation of neurokinin-1 receptors up-regulates substance P and neurokinin-1 receptor expression in murine pancreatic acinar cells"

    Article Title: Activation of neurokinin-1 receptors up-regulates substance P and neurokinin-1 receptor expression in murine pancreatic acinar cells

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/j.1582-4934.2011.01475.x

    PKC, MAPK and NF-κB are involved in SP-induced SP up-regulation in murine pancreatic acinar cells. Freshly prepared pancreatic acinar cells were pretreated with either Gö6976 (10 nM), rottlerin (5 μM), PD98059 (30 μM), SP600125 (30 μM) or Bay11-7082 (30μM) for 30 min. before stimulation with SP (10 −6 M) for 60 min. NK1R mRNA expression was determined with real time PCR. Whole cell lysates were prepared and 50 μg of protein were fractionated on 10% sodium dodecyl sulfate-polyacrylamide gels for Western blot analysis of NK1R and HPRT. NK1R mRNA expression was normalized with β-actin expression and NK1R protein expression was normalized with HPRT expression. (A) NK1R mRNA expression. (B) NK1R protein expression. Results are expressed as means ± S.E.M. from 4–6 independent experiments. * P
    Figure Legend Snippet: PKC, MAPK and NF-κB are involved in SP-induced SP up-regulation in murine pancreatic acinar cells. Freshly prepared pancreatic acinar cells were pretreated with either Gö6976 (10 nM), rottlerin (5 μM), PD98059 (30 μM), SP600125 (30 μM) or Bay11-7082 (30μM) for 30 min. before stimulation with SP (10 −6 M) for 60 min. NK1R mRNA expression was determined with real time PCR. Whole cell lysates were prepared and 50 μg of protein were fractionated on 10% sodium dodecyl sulfate-polyacrylamide gels for Western blot analysis of NK1R and HPRT. NK1R mRNA expression was normalized with β-actin expression and NK1R protein expression was normalized with HPRT expression. (A) NK1R mRNA expression. (B) NK1R protein expression. Results are expressed as means ± S.E.M. from 4–6 independent experiments. * P

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot

    16) Product Images from "Altering sphingolipid composition with aging induces contractile dysfunction of gastric smooth muscle via KCa1.1 upregulation"

    Article Title: Altering sphingolipid composition with aging induces contractile dysfunction of gastric smooth muscle via KCa1.1 upregulation

    Journal: Aging Cell

    doi: 10.1111/acel.12388

    The PI 3K/ PKC ζ / JNK / NF ‐κB pathway mediates K C a 1.1 upregulation due to aging or ceramide synthases 2 ( C er S 2) ablation. Protein levels of phosphorylated p85 (p‐p85), phosphorylated PKC ζ (p‐ PKC ζ ), K C a 1.1, and phosphorylated JNK (p‐ JNK ) were examined in gastric smooth muscle ( GSM ) or primary cultured gastric smooth muscle cells ( SMC s). (A) Levels of p‐p85 or p‐ PKC ζ in GSM of young C er S 2‐null and age‐matched WT mice. (B) p‐ PKC ζ levels in GSM of WT mice at different ages. (C) p‐ PKC ζ levels in WT gastric SMC s transfected with C er S 5 for 24 h. (D) K C a 1.1 levels in C er S 2‐null gastric SMC s treated with 10 μ m PKC ζ pseudosubstrate inhibitor ( PKI ) for 24 h (upper panels), or in C er S 2‐null gastric SMC s transfected with scrambled si RNA or si RNA against PKC ζ for 24 h (lower panels). (E) p‐ JNK levels in C er S 2‐null gastric SMC s transfected with scrambled si RNA or si RNA against PKC ζ for 24 h. (F) K C a 1.1 levels in C er S 2‐null gastric SMC s treated with the NF ‐κ B blockers, MG 132, Bay11‐7082, or SN 50, for 24 h. The blots are representative of 3–4 experiments. Results were normalized to GAPDH or α‐tubulin levels. *P
    Figure Legend Snippet: The PI 3K/ PKC ζ / JNK / NF ‐κB pathway mediates K C a 1.1 upregulation due to aging or ceramide synthases 2 ( C er S 2) ablation. Protein levels of phosphorylated p85 (p‐p85), phosphorylated PKC ζ (p‐ PKC ζ ), K C a 1.1, and phosphorylated JNK (p‐ JNK ) were examined in gastric smooth muscle ( GSM ) or primary cultured gastric smooth muscle cells ( SMC s). (A) Levels of p‐p85 or p‐ PKC ζ in GSM of young C er S 2‐null and age‐matched WT mice. (B) p‐ PKC ζ levels in GSM of WT mice at different ages. (C) p‐ PKC ζ levels in WT gastric SMC s transfected with C er S 5 for 24 h. (D) K C a 1.1 levels in C er S 2‐null gastric SMC s treated with 10 μ m PKC ζ pseudosubstrate inhibitor ( PKI ) for 24 h (upper panels), or in C er S 2‐null gastric SMC s transfected with scrambled si RNA or si RNA against PKC ζ for 24 h (lower panels). (E) p‐ JNK levels in C er S 2‐null gastric SMC s transfected with scrambled si RNA or si RNA against PKC ζ for 24 h. (F) K C a 1.1 levels in C er S 2‐null gastric SMC s treated with the NF ‐κ B blockers, MG 132, Bay11‐7082, or SN 50, for 24 h. The blots are representative of 3–4 experiments. Results were normalized to GAPDH or α‐tubulin levels. *P

    Techniques Used: Cell Culture, Mouse Assay, Transfection

    17) Product Images from "Ursolic Acid Attenuates Atherosclerosis in ApoE−/− Mice: Role of LOX-1 Mediated by ROS/NF-κB Pathway"

    Article Title: Ursolic Acid Attenuates Atherosclerosis in ApoE−/− Mice: Role of LOX-1 Mediated by ROS/NF-κB Pathway

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    doi: 10.3390/molecules23051101

    Cells were treated with LPS (5 mg/mL) for 4 h after pretreatment with UA (1 μM) or NAC (5 mM) for 1 h; ROS was determined by DCFH 2 -DA ( A ); Cells were treated with LPS (5 mg/mL) for 24 h with or without pretreatment with UA (1 μM), NAC (5 mM), or BAY (10 μM) for 1 h, and expression of p65 ( B ) and LOX-1 ( D ) was detected by western blotting; Cells were treated with LPS (5 mg/mL) with or without 1 h pretreatment with UA (1 μM) and NAC (5 mM), and p65 NF-κB localization was determined by immunofluorescence ( C ) (60×). UA, ursolic acid; BAY, BAY11-7082; NAC, N-acetyl cysteine.
    Figure Legend Snippet: Cells were treated with LPS (5 mg/mL) for 4 h after pretreatment with UA (1 μM) or NAC (5 mM) for 1 h; ROS was determined by DCFH 2 -DA ( A ); Cells were treated with LPS (5 mg/mL) for 24 h with or without pretreatment with UA (1 μM), NAC (5 mM), or BAY (10 μM) for 1 h, and expression of p65 ( B ) and LOX-1 ( D ) was detected by western blotting; Cells were treated with LPS (5 mg/mL) with or without 1 h pretreatment with UA (1 μM) and NAC (5 mM), and p65 NF-κB localization was determined by immunofluorescence ( C ) (60×). UA, ursolic acid; BAY, BAY11-7082; NAC, N-acetyl cysteine.

    Techniques Used: Expressing, Western Blot, Immunofluorescence

    18) Product Images from "Docosahexaenoic Acid Inhibits Tumor Promoter-Induced Urokinase-Type Plasminogen Activator Receptor by Suppressing PKCδ- and MAPKs-Mediated Pathways in ECV304 Human Endothelial Cells"

    Article Title: Docosahexaenoic Acid Inhibits Tumor Promoter-Induced Urokinase-Type Plasminogen Activator Receptor by Suppressing PKCδ- and MAPKs-Mediated Pathways in ECV304 Human Endothelial Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0163395

    DHA inhibits TPA-induced uPAR by suppressing the DNA-binding activities of NF-кB p65 in ECV304 cells. (A) Cells were treated with TPA for 0–90 min, and the cellular extracts were blotted using specific antibodies. (B) Cells were transiently transfected with the pNF-кB luciferase reporter construct. The transfected cells were incubated with TPA for 4 h and the luciferase activities were determined using a luminometer. (C) Cells were treated with 0–10 μM BAY11-7082 for 1 h prior to exposure to 100 nM TPA for 4 h. After incubation, the uPAR mRNA levels in the cell lysates were determined by RT-PCR. (D) Cells were treated with 0–10 μM BAY11-7082 for 1 h prior to exposure to 100 nM TPA for 16 h. After incubation, the uPAR protein levels were determined by western blotting. (E) The dominant negative mutant of I-κBα, I-κBβ, and NIK were co-transfected with pGL3-uPAR into cells. After incubation with 100 nM TPA for 4 h, the luciferase activities were determined using a luminometer. (F) Cells were treated with DHA (25, 50, 100 μM) prior exposure to 100 nM TPA, and the expressions of phos-p65 (Ser 536), phos-IкB-α (Ser 32), and IкB-α were analyzed by western blotting. (G) Cells were transiently transfected with the pNF-кB luciferase reporter construct, after being pretreated with DHA (25, 50, 100 μM), and then were incubated with 100 nM TPA for 4 h. After incubation, the cells were lysed and luciferase activity was determined. * P
    Figure Legend Snippet: DHA inhibits TPA-induced uPAR by suppressing the DNA-binding activities of NF-кB p65 in ECV304 cells. (A) Cells were treated with TPA for 0–90 min, and the cellular extracts were blotted using specific antibodies. (B) Cells were transiently transfected with the pNF-кB luciferase reporter construct. The transfected cells were incubated with TPA for 4 h and the luciferase activities were determined using a luminometer. (C) Cells were treated with 0–10 μM BAY11-7082 for 1 h prior to exposure to 100 nM TPA for 4 h. After incubation, the uPAR mRNA levels in the cell lysates were determined by RT-PCR. (D) Cells were treated with 0–10 μM BAY11-7082 for 1 h prior to exposure to 100 nM TPA for 16 h. After incubation, the uPAR protein levels were determined by western blotting. (E) The dominant negative mutant of I-κBα, I-κBβ, and NIK were co-transfected with pGL3-uPAR into cells. After incubation with 100 nM TPA for 4 h, the luciferase activities were determined using a luminometer. (F) Cells were treated with DHA (25, 50, 100 μM) prior exposure to 100 nM TPA, and the expressions of phos-p65 (Ser 536), phos-IкB-α (Ser 32), and IкB-α were analyzed by western blotting. (G) Cells were transiently transfected with the pNF-кB luciferase reporter construct, after being pretreated with DHA (25, 50, 100 μM), and then were incubated with 100 nM TPA for 4 h. After incubation, the cells were lysed and luciferase activity was determined. * P

    Techniques Used: Binding Assay, Transfection, Luciferase, Construct, Incubation, Reverse Transcription Polymerase Chain Reaction, Western Blot, Dominant Negative Mutation, Activity Assay

    19) Product Images from "Receptor-interacting protein kinase 1 is a key mediator in TLR3 ligand and Smac mimetic-induced cell death and suppresses TLR3 ligand-promoted invasion in cholangiocarcinoma"

    Article Title: Receptor-interacting protein kinase 1 is a key mediator in TLR3 ligand and Smac mimetic-induced cell death and suppresses TLR3 ligand-promoted invasion in cholangiocarcinoma

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-020-00661-3

    Smac mimetic reverses TLR3 ligand, Poly(I:C)-induced invasion in CCA cells. a KKU213 cells were pretreated with 10 μM Bay11–7082, 10 μM U0126, 20 μM SP600125 or 10 μM SB203580 for 30 min followed by transfection with TurboFect or 2.5 μg/ml Poly(I:C) for 12 h and then subjected to invasion assay. b CRISPR-V2 and CRISPR-RIPK1 KKU213 cells were treated as in ( a ) for 12 h and then subjected to invasion assay. c KKU213 cells were transfected with TurboFect or 2.5 μg/ml Poly(I:C) for indicated time points and cell lysates were collected, after that RIPK1, pERK, and IκBα were analyzed by Western blot analysis. Total ERK and β-actin were served as loading control. Data shown was a representative of two independent experiments. d KKU213 cells were pretreated with DMSO control or TLR3 inhibitor, CuCpt4a for 1 h followed by transfection with TurboFect or 2.5 μg/ml Poly(I:C) for 12 h and then subjected to invasion assay. e KKU213 cells were pretreated with 5 nM Smac mimetic for 2 h followed by transfection with 2.5 μg/ml Poly(I:C) for 12 h and then subjected to invasion assay. f Representative images of CRISPR-V2 and CRISPR-RIPK1 invaded cells stained with crystal violet. g Quantification of number of CRISPR-V2 and CRISPR-RIPK1 KKU213 invaded cells treated with 5 nM Smac mimetic, 2.5 μg/ml Poly(I:C) alone or the combination treatment for 12 h. h KKU213 cells were pretreated with RIPK1 inhibitor (Nec-1) with or without 5 nM Smac mimetic followed by transfection with 2.5 μg/ml Poly(I:C) for 12 h. Number of invaded cells were counted. Data from three independent experiments was presented as mean ± S.D.; * p
    Figure Legend Snippet: Smac mimetic reverses TLR3 ligand, Poly(I:C)-induced invasion in CCA cells. a KKU213 cells were pretreated with 10 μM Bay11–7082, 10 μM U0126, 20 μM SP600125 or 10 μM SB203580 for 30 min followed by transfection with TurboFect or 2.5 μg/ml Poly(I:C) for 12 h and then subjected to invasion assay. b CRISPR-V2 and CRISPR-RIPK1 KKU213 cells were treated as in ( a ) for 12 h and then subjected to invasion assay. c KKU213 cells were transfected with TurboFect or 2.5 μg/ml Poly(I:C) for indicated time points and cell lysates were collected, after that RIPK1, pERK, and IκBα were analyzed by Western blot analysis. Total ERK and β-actin were served as loading control. Data shown was a representative of two independent experiments. d KKU213 cells were pretreated with DMSO control or TLR3 inhibitor, CuCpt4a for 1 h followed by transfection with TurboFect or 2.5 μg/ml Poly(I:C) for 12 h and then subjected to invasion assay. e KKU213 cells were pretreated with 5 nM Smac mimetic for 2 h followed by transfection with 2.5 μg/ml Poly(I:C) for 12 h and then subjected to invasion assay. f Representative images of CRISPR-V2 and CRISPR-RIPK1 invaded cells stained with crystal violet. g Quantification of number of CRISPR-V2 and CRISPR-RIPK1 KKU213 invaded cells treated with 5 nM Smac mimetic, 2.5 μg/ml Poly(I:C) alone or the combination treatment for 12 h. h KKU213 cells were pretreated with RIPK1 inhibitor (Nec-1) with or without 5 nM Smac mimetic followed by transfection with 2.5 μg/ml Poly(I:C) for 12 h. Number of invaded cells were counted. Data from three independent experiments was presented as mean ± S.D.; * p

    Techniques Used: Transfection, Invasion Assay, CRISPR, Western Blot, Staining

    20) Product Images from "Tetracyclines downregulate the production of LPS-induced cytokines and chemokines in THP-1 cells via ERK, p38, and nuclear factor-κB signaling pathways"

    Article Title: Tetracyclines downregulate the production of LPS-induced cytokines and chemokines in THP-1 cells via ERK, p38, and nuclear factor-κB signaling pathways

    Journal: Biochemistry and Biophysics Reports

    doi: 10.1016/j.bbrep.2015.11.003

    SB203580, U0126 and BAY11-7082 suppressed TNF-α and IL-8 production in LPS-stimulated THP-1 cells on treatment with or without tetracyclines. THP-1 cells were pre-incubated by SB203580 (10 μM), U0126 (5 μM) and BAY11-7082 (5 μM) for 30 min, followed treatment without or with LPS (10 μg/ml), or with LPS (10 μg/ml) plus minocycline (50 μg/ml), doxycycline (50 μg/ml), or tigecycline (50 μg/ml) for 60 min. TNF-α were measured with ELISA. * p
    Figure Legend Snippet: SB203580, U0126 and BAY11-7082 suppressed TNF-α and IL-8 production in LPS-stimulated THP-1 cells on treatment with or without tetracyclines. THP-1 cells were pre-incubated by SB203580 (10 μM), U0126 (5 μM) and BAY11-7082 (5 μM) for 30 min, followed treatment without or with LPS (10 μg/ml), or with LPS (10 μg/ml) plus minocycline (50 μg/ml), doxycycline (50 μg/ml), or tigecycline (50 μg/ml) for 60 min. TNF-α were measured with ELISA. * p

    Techniques Used: Incubation, Enzyme-linked Immunosorbent Assay

    21) Product Images from "The homeobox gene DLX4 regulates erythro-megakaryocytic differentiation by stimulating IL-1β and NF-κB signaling"

    Article Title: The homeobox gene DLX4 regulates erythro-megakaryocytic differentiation by stimulating IL-1β and NF-κB signaling

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.168187

    DLX4 stimulates NF-κB signaling. (A) Expression of NF-κB target genes was assayed in vector control and +DLX4 K562 cells by qRT-PCR. Shown is the average fold induction in the mRNA level of each gene in +DLX4 cells relative to its respective level in vector control cells. (B) NF-κB-LUC reporter activity was assayed in vector control K562 cells and in +DLX4 K562 cells that lacked or expressed ΙκΒα-dn (upper panel), and also in K562 cells that were transfected with non-targeting shRNA (shControl) and with two different DLX4 shRNAs (shDLX4-A, shDLX4-B) (lower panel). (C) Upper panel, representative examples of flow cytometric analysis of intracellular staining of phosphorylated NF-κB p65 in K562 cells and in CD34 + cells (solid gray histograms with MFI indicated). Dotted histograms represent staining with isotype control. Lower panel, average MFI of staining. In D, E and F, lineage markers, DNA content and morphology were evaluated in vector control K562 cells, in +DLX4 K562 cells that lacked or expressed ΙκΒα-dn, and in +DLX4 K562 cells that were treated with the IκB kinase inhibitor BAY11-7082 (1 µM) for 3 days. (D) Average MFI of CD61, CD41 and GYPA staining detected by flow cytometry. (E) Analysis of DNA content. (F) Morphologic features of K562 cells stained with Wright Giemsa solution. Scale bar: 20 µm. Shown in A–E are mean±s.d. values of three independent experiments. * P
    Figure Legend Snippet: DLX4 stimulates NF-κB signaling. (A) Expression of NF-κB target genes was assayed in vector control and +DLX4 K562 cells by qRT-PCR. Shown is the average fold induction in the mRNA level of each gene in +DLX4 cells relative to its respective level in vector control cells. (B) NF-κB-LUC reporter activity was assayed in vector control K562 cells and in +DLX4 K562 cells that lacked or expressed ΙκΒα-dn (upper panel), and also in K562 cells that were transfected with non-targeting shRNA (shControl) and with two different DLX4 shRNAs (shDLX4-A, shDLX4-B) (lower panel). (C) Upper panel, representative examples of flow cytometric analysis of intracellular staining of phosphorylated NF-κB p65 in K562 cells and in CD34 + cells (solid gray histograms with MFI indicated). Dotted histograms represent staining with isotype control. Lower panel, average MFI of staining. In D, E and F, lineage markers, DNA content and morphology were evaluated in vector control K562 cells, in +DLX4 K562 cells that lacked or expressed ΙκΒα-dn, and in +DLX4 K562 cells that were treated with the IκB kinase inhibitor BAY11-7082 (1 µM) for 3 days. (D) Average MFI of CD61, CD41 and GYPA staining detected by flow cytometry. (E) Analysis of DNA content. (F) Morphologic features of K562 cells stained with Wright Giemsa solution. Scale bar: 20 µm. Shown in A–E are mean±s.d. values of three independent experiments. * P

    Techniques Used: Expressing, Plasmid Preparation, Quantitative RT-PCR, Activity Assay, Transfection, shRNA, Flow Cytometry, Staining, Cytometry

    22) Product Images from "Ehrlichia chaffeensis Exploits Canonical and Noncanonical Host Wnt Signaling Pathways To Stimulate Phagocytosis and Promote Intracellular Survival"

    Article Title: Ehrlichia chaffeensis Exploits Canonical and Noncanonical Host Wnt Signaling Pathways To Stimulate Phagocytosis and Promote Intracellular Survival

    Journal: Infection and Immunity

    doi: 10.1128/IAI.01289-15

    E. chaffeensis tandem repeat proteins stimulate phagocytosis and intracellular Ca 2+ release in macrophages, and Wnt pathway inhibitors reduce the stimulation. (A) Compared with control TRP120N-coated beads, TRP120-coated beads were phagocytosed by the THP-1 cells. After treatment with Wnt pathway inhibitor Bay11-7082 (10 μM), the promotion of bead internalization by TRP120 was largely reduced. (B) Efficiency of promotion of bead internalization by different tandem repeat proteins and domains. (C) Effect of different Wnt pathway inhibitors on the promotion of bead internalization by TRP120. All experiments were repeated three times, and the values are means ± standard deviations (*, P
    Figure Legend Snippet: E. chaffeensis tandem repeat proteins stimulate phagocytosis and intracellular Ca 2+ release in macrophages, and Wnt pathway inhibitors reduce the stimulation. (A) Compared with control TRP120N-coated beads, TRP120-coated beads were phagocytosed by the THP-1 cells. After treatment with Wnt pathway inhibitor Bay11-7082 (10 μM), the promotion of bead internalization by TRP120 was largely reduced. (B) Efficiency of promotion of bead internalization by different tandem repeat proteins and domains. (C) Effect of different Wnt pathway inhibitors on the promotion of bead internalization by TRP120. All experiments were repeated three times, and the values are means ± standard deviations (*, P

    Techniques Used:

    23) Product Images from "Bay11-7082 inhibits the disintegration of the lymphendothelial barrier triggered by MCF-7 breast cancer spheroids; the role of ICAM-1 and adhesion"

    Article Title: Bay11-7082 inhibits the disintegration of the lymphendothelial barrier triggered by MCF-7 breast cancer spheroids; the role of ICAM-1 and adhesion

    Journal: British Journal of Cancer

    doi: 10.1038/bjc.2012.485

    ( A ) Additive inhibition of CCIDs by baicalein and Bay11-7082. MCF-7 spheroids and LEC co-cultures were treated with 10 μ ℳ Bay11-7082 and/or 100 μ ℳ baicalein for 4 h.Then the CCID areas underneath at least 12 spheroids (per condition) were measured using a Zeiss Axiovert microscope and Axiovision software. Error bars indicate s.e.m., asterisks significance compared with control ( P
    Figure Legend Snippet: ( A ) Additive inhibition of CCIDs by baicalein and Bay11-7082. MCF-7 spheroids and LEC co-cultures were treated with 10 μ ℳ Bay11-7082 and/or 100 μ ℳ baicalein for 4 h.Then the CCID areas underneath at least 12 spheroids (per condition) were measured using a Zeiss Axiovert microscope and Axiovision software. Error bars indicate s.e.m., asterisks significance compared with control ( P

    Techniques Used: Inhibition, Microscopy, Software

    Inhibition of CCIDs and adhesion protein ICAM-1 by Bay11-7082. ( A ) Trypsinised and cytotracker-stained MCF-7 cells were placed on LEC monolayers and co-cultivated for 40 min with solvent (DMSO; Co), or with increasing concentrations of Bay11-7082 (2.5, 5, 10 and 15 μ ℳ, 0.5 h pretreatment). Then the cells were washed, and the percentages of MCF-7 cells that adhered to LECs were determined by measuring the fluorescence 485/530 nm in the mixed cell lysate. Error bars indicate s.e.m., asterisks significance compared with control ( P
    Figure Legend Snippet: Inhibition of CCIDs and adhesion protein ICAM-1 by Bay11-7082. ( A ) Trypsinised and cytotracker-stained MCF-7 cells were placed on LEC monolayers and co-cultivated for 40 min with solvent (DMSO; Co), or with increasing concentrations of Bay11-7082 (2.5, 5, 10 and 15 μ ℳ, 0.5 h pretreatment). Then the cells were washed, and the percentages of MCF-7 cells that adhered to LECs were determined by measuring the fluorescence 485/530 nm in the mixed cell lysate. Error bars indicate s.e.m., asterisks significance compared with control ( P

    Techniques Used: Inhibition, Staining, Fluorescence

    24) Product Images from "Lymphomagenic CARD11/BCL10/MALT1 signaling drives malignant B-cell proliferation via cooperative NF-κB and JNK activation"

    Article Title: Lymphomagenic CARD11/BCL10/MALT1 signaling drives malignant B-cell proliferation via cooperative NF-κB and JNK activation

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1507459112

    Low dose treatment with NF-κB and JNK inhibitors. B cells from CARD11(L225LI)CD19-Cre mice were treated with solvent control (−) or 1 μM Bay11-7082 ( A ) or 1 μM SP600125 ( B ) (+) for 4 h, and nuclear lysates were examined
    Figure Legend Snippet: Low dose treatment with NF-κB and JNK inhibitors. B cells from CARD11(L225LI)CD19-Cre mice were treated with solvent control (−) or 1 μM Bay11-7082 ( A ) or 1 μM SP600125 ( B ) (+) for 4 h, and nuclear lysates were examined

    Techniques Used: Mouse Assay

    25) Product Images from "Changes in mitochondrial DNA alter expression of nuclear encoded genes associated with tumorigenesis"

    Article Title: Changes in mitochondrial DNA alter expression of nuclear encoded genes associated with tumorigenesis

    Journal: Experimental cell research

    doi: 10.1016/j.yexcr.2012.06.006

    Migration and invasion capabilities of mtBALB cybrid cells in the presence of Bay11-7082
    Figure Legend Snippet: Migration and invasion capabilities of mtBALB cybrid cells in the presence of Bay11-7082

    Techniques Used: Migration

    26) Product Images from "Cytoplasmic accumulation of NCoR in malignant melanoma: consequences of altered gene repression and prognostic significance"

    Article Title: Cytoplasmic accumulation of NCoR in malignant melanoma: consequences of altered gene repression and prognostic significance

    Journal: Oncotarget

    doi:

    IKK activity regulates NCoR subcellular distribution and function in melanoma cells (A) Immunohistochemistry of NCoR in SKMEL-37 melanoma cells untreated or treated for 60 minutes with the IKK inhibitor BAY11-7082. (B) Western blot analysis of cytoplasmic, nuclear and chromatin fractions of SKMEL-37 cells, treated with two different concentration of BAY11-7082 (Calbiochem) for 60 minutes. (C) qRT-PCR to determine the effect of IKK inhibition by BAY11-7082 (16 hours of treatment) in the levels of various NCoR target genes.
    Figure Legend Snippet: IKK activity regulates NCoR subcellular distribution and function in melanoma cells (A) Immunohistochemistry of NCoR in SKMEL-37 melanoma cells untreated or treated for 60 minutes with the IKK inhibitor BAY11-7082. (B) Western blot analysis of cytoplasmic, nuclear and chromatin fractions of SKMEL-37 cells, treated with two different concentration of BAY11-7082 (Calbiochem) for 60 minutes. (C) qRT-PCR to determine the effect of IKK inhibition by BAY11-7082 (16 hours of treatment) in the levels of various NCoR target genes.

    Techniques Used: Activity Assay, Immunohistochemistry, Western Blot, Concentration Assay, Quantitative RT-PCR, Inhibition

    27) Product Images from "Photobiomodulation of extracellular matrix enzymes in human nucleus pulposus cells as a potential treatment for intervertebral disk degeneration"

    Article Title: Photobiomodulation of extracellular matrix enzymes in human nucleus pulposus cells as a potential treatment for intervertebral disk degeneration

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-30185-3

    Effects of potential contributing factors, derived from macrophages, on human NP cells with/without BAY11-7082 as an inhibitor of the nuclear factor kappa B (NF-κB) activity. ( A ) Production of IL-1β and ( B ) TNF-α; ( C ) total collagen secretion; ( D ) production of MMP-1 and ( E ) MMP-3. ( F ) Gene expression of MMP1 and ( G ) MMP3 . ( H ) Production of TIMP-1 and ( I ) TIMP-2 as endogenous inhibitors of MMP-3 and MMP-1, respectively. Values are mean ± SE of three or four independent experiments. *p
    Figure Legend Snippet: Effects of potential contributing factors, derived from macrophages, on human NP cells with/without BAY11-7082 as an inhibitor of the nuclear factor kappa B (NF-κB) activity. ( A ) Production of IL-1β and ( B ) TNF-α; ( C ) total collagen secretion; ( D ) production of MMP-1 and ( E ) MMP-3. ( F ) Gene expression of MMP1 and ( G ) MMP3 . ( H ) Production of TIMP-1 and ( I ) TIMP-2 as endogenous inhibitors of MMP-3 and MMP-1, respectively. Values are mean ± SE of three or four independent experiments. *p

    Techniques Used: Derivative Assay, Activity Assay, Expressing

    28) Product Images from "Discovery of pan autophagy inhibitors through a high-throughput screen highlights macroautophagy as an evolutionarily conserved process across 3 eukaryotic kingdoms"

    Article Title: Discovery of pan autophagy inhibitors through a high-throughput screen highlights macroautophagy as an evolutionarily conserved process across 3 eukaryotic kingdoms

    Journal: Autophagy

    doi: 10.1080/15548627.2017.1339002

    Screening of small molecule libraries. (A) Using the luciferase based assay for monitoring autophagy, the library of pharmacologically active compounds from Sigma containing 1280 FDA-approved small molecules was screened for its effect on autophagy. The rates of degradation of the untreated cells were compared with the ones treated with 50 µM concentration of the compounds. The time taken for 50% decrease in cargo activity (firefly luciferase) was taken as the criteria for comparing the control with the compounds. The compounds that differed from the control by 3 SD units were considered as putative hits. Each black dot represents individual small molecule from the library and the 2 inhibitors Bay11 and ZPCK have also been depicted from the screening data. (B) The dot-plot depicts the comparison between the known modulators picked up from the screen and Bay11 and ZPCK with the shaded region showing the 3 SD area. (C) Two putative inhibitors, Bay11-7082 (Bay11) and Z- L -phenyl chloromethyl ketone (ZPCK) obtained from the primary screening were further confirmed using firefly luciferase assay done in triplicates. (D) Time (in hours) taken for 50% decay in the firefly luciferase activity was plotted for untreated, Bay11- and ZPCK-treated cells (shaded region indicates 3 SD units). (E) A dose-dependent effect on the rates of degradation of firefly luciferase luciferase was seen in Bay11- and (F) ZPCK-treated cells.
    Figure Legend Snippet: Screening of small molecule libraries. (A) Using the luciferase based assay for monitoring autophagy, the library of pharmacologically active compounds from Sigma containing 1280 FDA-approved small molecules was screened for its effect on autophagy. The rates of degradation of the untreated cells were compared with the ones treated with 50 µM concentration of the compounds. The time taken for 50% decrease in cargo activity (firefly luciferase) was taken as the criteria for comparing the control with the compounds. The compounds that differed from the control by 3 SD units were considered as putative hits. Each black dot represents individual small molecule from the library and the 2 inhibitors Bay11 and ZPCK have also been depicted from the screening data. (B) The dot-plot depicts the comparison between the known modulators picked up from the screen and Bay11 and ZPCK with the shaded region showing the 3 SD area. (C) Two putative inhibitors, Bay11-7082 (Bay11) and Z- L -phenyl chloromethyl ketone (ZPCK) obtained from the primary screening were further confirmed using firefly luciferase assay done in triplicates. (D) Time (in hours) taken for 50% decay in the firefly luciferase activity was plotted for untreated, Bay11- and ZPCK-treated cells (shaded region indicates 3 SD units). (E) A dose-dependent effect on the rates of degradation of firefly luciferase luciferase was seen in Bay11- and (F) ZPCK-treated cells.

    Techniques Used: Luciferase, Concentration Assay, Activity Assay

    29) Product Images from "Mutations in BALB Mitochondrial DNA Induce CCL20 Up-regulation Promoting Tumorigenic Phenotypes"

    Article Title: Mutations in BALB Mitochondrial DNA Induce CCL20 Up-regulation Promoting Tumorigenic Phenotypes

    Journal: Mutation research

    doi: 10.1016/j.mrfmmm.2014.07.003

    mRNA expression levels of chemokine CCL20 and its receptor CCR6 in mtB6 and mtBALB cybrid cells after the treatment with rmCCL20 and pathway specific inhibitors BAY11-7082 and PD98059. Quantitative RT-PCR histogram showing the mRNA expression levels of
    Figure Legend Snippet: mRNA expression levels of chemokine CCL20 and its receptor CCR6 in mtB6 and mtBALB cybrid cells after the treatment with rmCCL20 and pathway specific inhibitors BAY11-7082 and PD98059. Quantitative RT-PCR histogram showing the mRNA expression levels of

    Techniques Used: Expressing, Quantitative RT-PCR

    Migratory capabilities of fibroblast cybrid cells in the presence of MAPK inhibitor PD98059, NF-κB inhibitor BAY11-7082 and functional blocking antibody against CCL20. Migratory experiments were performed using uncoated inserts in transwell system.
    Figure Legend Snippet: Migratory capabilities of fibroblast cybrid cells in the presence of MAPK inhibitor PD98059, NF-κB inhibitor BAY11-7082 and functional blocking antibody against CCL20. Migratory experiments were performed using uncoated inserts in transwell system.

    Techniques Used: Functional Assay, Blocking Assay

    30) Product Images from "Betaglycan Alters NFκB-TGFβ2 Cross Talk to Reduce Survival of Human Granulosa Tumor Cells"

    Article Title: Betaglycan Alters NFκB-TGFβ2 Cross Talk to Reduce Survival of Human Granulosa Tumor Cells

    Journal: Molecular Endocrinology

    doi: 10.1210/me.2012-1239

    SMAD3 overexpression counters BAY11-7082/TGFβ2-mediated GCT cell death. A, Quantitative real-time RT-PCR on GCT (n = 17) and normal premenopausal ovary (n = 11) samples, using primers specific to human SMAD3 . Mean ± SEM is shown for each
    Figure Legend Snippet: SMAD3 overexpression counters BAY11-7082/TGFβ2-mediated GCT cell death. A, Quantitative real-time RT-PCR on GCT (n = 17) and normal premenopausal ovary (n = 11) samples, using primers specific to human SMAD3 . Mean ± SEM is shown for each

    Techniques Used: Over Expression, Quantitative RT-PCR

    SMAD3 expression is dependent on NFκB activity in KGN cells. A, Western blot assessment of total SMAD2 and SMAD3 levels in cell lysates from KGN control and WT-BG cells lines after overnight treatment with the NFκB inhibitor, BAY11-7082
    Figure Legend Snippet: SMAD3 expression is dependent on NFκB activity in KGN cells. A, Western blot assessment of total SMAD2 and SMAD3 levels in cell lysates from KGN control and WT-BG cells lines after overnight treatment with the NFκB inhibitor, BAY11-7082

    Techniques Used: Expressing, Activity Assay, Western Blot

    31) Product Images from "Kainic acid hyperphosphorylates tau via inflammasome activation in MAPT transgenic mice"

    Article Title: Kainic acid hyperphosphorylates tau via inflammasome activation in MAPT transgenic mice

    Journal: Aging (Albany NY)

    doi: 10.18632/aging.102495

    Bay11-7082 mitigates KA-induced memory deficits in the Morris water maze test. ( A , B ) During the first 2 days of visible platform tests, the KA and Bay11-7082 treated and control MAPT Tg mice exhibited a similar latency to escape onto the visible platform. P > 0.05 with Student’s t-test. ( C , D ) In the hidden platform tests, KA-treated MAPT mice showed a longer latency and length to escape onto the hidden platform on the 3 rd and 4 th days, which was ameliorated by the addition of Bay11-7082 on the 4 th day. * P
    Figure Legend Snippet: Bay11-7082 mitigates KA-induced memory deficits in the Morris water maze test. ( A , B ) During the first 2 days of visible platform tests, the KA and Bay11-7082 treated and control MAPT Tg mice exhibited a similar latency to escape onto the visible platform. P > 0.05 with Student’s t-test. ( C , D ) In the hidden platform tests, KA-treated MAPT mice showed a longer latency and length to escape onto the hidden platform on the 3 rd and 4 th days, which was ameliorated by the addition of Bay11-7082 on the 4 th day. * P

    Techniques Used: Mouse Assay

    A functional model of KA-induced inflammasome activity through tau phosphorylation and memory deficits were exacerbated in an ER stress-dependent mechanism. KA treatment triggers activation of the inflammasome and causes the phosphorylation of NF-κB, leading to NLRP3 upregulation via ER stress. Upregulated NLRP3 eventually results in the phosphorylation of tau by enhancing the expression of IL-1β. Bay11-7082 inhibits KA-induced IL-1β activation and tau phosphorylation by alleviating the activity of inflammasome, which ultimately improved the cognitive decline in MAPT Tg mice.
    Figure Legend Snippet: A functional model of KA-induced inflammasome activity through tau phosphorylation and memory deficits were exacerbated in an ER stress-dependent mechanism. KA treatment triggers activation of the inflammasome and causes the phosphorylation of NF-κB, leading to NLRP3 upregulation via ER stress. Upregulated NLRP3 eventually results in the phosphorylation of tau by enhancing the expression of IL-1β. Bay11-7082 inhibits KA-induced IL-1β activation and tau phosphorylation by alleviating the activity of inflammasome, which ultimately improved the cognitive decline in MAPT Tg mice.

    Techniques Used: Functional Assay, Activity Assay, Activation Assay, Expressing, Mouse Assay

    KA-induced tau hyperphosphorylation is highly correlated with ER stress-activated inflammasome. ( A , B ) Truncation of GSK3β, phosphorylation levels of NF-κB, and the expression levels of NLRP3 and IL-1β as well as the phosphorylation of tau were determined by western blots of samples from MAPT Tg mice treated with KA (10 mg/kg) and/or salubrinal (1 mg/kg) together with KA (10 mg/kg). The KA group was given i.p. injection of 10 mg/kg KA. The salubrinal+KA group mice were additionally given i.p. injections of 1 mg/kg Bay11-7082. Both groups were assessed after 48 h. ( C , D ) Truncation of GSK3β, phosphorylation levels of NF-κB, and the expression levels of NLRP3 and IL-1β as well as the phosphorylation of tau were determined by western blots in cells treated with KA (10 μM) and/or salubrinal (5 μM) together with KA (10 μM). The KA group was treated with 10 μM KA. The salubrinal+KA group was additionally treated with 5 μM salubrinal. Both groups were assessed after 48 h. The optical density of the bands in western blots was analyzed by Image J software (* P
    Figure Legend Snippet: KA-induced tau hyperphosphorylation is highly correlated with ER stress-activated inflammasome. ( A , B ) Truncation of GSK3β, phosphorylation levels of NF-κB, and the expression levels of NLRP3 and IL-1β as well as the phosphorylation of tau were determined by western blots of samples from MAPT Tg mice treated with KA (10 mg/kg) and/or salubrinal (1 mg/kg) together with KA (10 mg/kg). The KA group was given i.p. injection of 10 mg/kg KA. The salubrinal+KA group mice were additionally given i.p. injections of 1 mg/kg Bay11-7082. Both groups were assessed after 48 h. ( C , D ) Truncation of GSK3β, phosphorylation levels of NF-κB, and the expression levels of NLRP3 and IL-1β as well as the phosphorylation of tau were determined by western blots in cells treated with KA (10 μM) and/or salubrinal (5 μM) together with KA (10 μM). The KA group was treated with 10 μM KA. The salubrinal+KA group was additionally treated with 5 μM salubrinal. Both groups were assessed after 48 h. The optical density of the bands in western blots was analyzed by Image J software (* P

    Techniques Used: Expressing, Western Blot, Mouse Assay, Injection, Software

    KA-induced activation of inflammasome promotes the phosphorylation of tau. ( A , B ) The expression levels of IL-1β and the phosphorylation of tau were determined by western blots of samples from MAPT Tg mice treated with KA (10 mg/kg) and/or Bay11-7082 (1 mg/kg) together with KA (10 mg/kg). The KA group was given i.p. injection of 10 mg/kg KA. The Bay11-7082+KA group mice were additionally given i.p. injections of 1 mg/kg Bay11-7082. Both groups were assessed after 48 h. ( C , D ) The expression levels of IL-1β and the phosphorylation of tau were determined by western blots using cells treated with KA (10 μM) and/or Bay11-7082 (1 μM) together with KA (10 μM). The KA group was treated with 10 μM KA. The Bay11-7082+KA group was additionally treated with 1 μM Bay11-7082. Both groups were assessed after 48 h. The optical density of bands in western blots was analyzed by Image J software (* P
    Figure Legend Snippet: KA-induced activation of inflammasome promotes the phosphorylation of tau. ( A , B ) The expression levels of IL-1β and the phosphorylation of tau were determined by western blots of samples from MAPT Tg mice treated with KA (10 mg/kg) and/or Bay11-7082 (1 mg/kg) together with KA (10 mg/kg). The KA group was given i.p. injection of 10 mg/kg KA. The Bay11-7082+KA group mice were additionally given i.p. injections of 1 mg/kg Bay11-7082. Both groups were assessed after 48 h. ( C , D ) The expression levels of IL-1β and the phosphorylation of tau were determined by western blots using cells treated with KA (10 μM) and/or Bay11-7082 (1 μM) together with KA (10 μM). The KA group was treated with 10 μM KA. The Bay11-7082+KA group was additionally treated with 1 μM Bay11-7082. Both groups were assessed after 48 h. The optical density of bands in western blots was analyzed by Image J software (* P

    Techniques Used: Activation Assay, Expressing, Western Blot, Mouse Assay, Injection, Software

    32) Product Images from "Anti-allergic Inflammatory Effects of the Essential Oil From Fruits of Zanthoxylum coreanum Nakai"

    Article Title: Anti-allergic Inflammatory Effects of the Essential Oil From Fruits of Zanthoxylum coreanum Nakai

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2018.01441

    Effect of ZCO on the production of inflammatory mediators in LPS-activated RAW264.7 cells. RAW264.7 cells seeded into 48-well plate were pretreated with ZCO (0.0025, 0.005, and 0.01%) or Bay11-7082 (20 μM) for 2 h prior to addition of LPS (500 ng/mL) for 24 h. TNF-α (A) and IL-6 (B) in the supernatants was measured by ELISA and NO production (C) in the supernatants was detected by Griess reagent. Experiments were conducted in quadruplicate and expressed as mean ± SEM ( ∗∗∗ P
    Figure Legend Snippet: Effect of ZCO on the production of inflammatory mediators in LPS-activated RAW264.7 cells. RAW264.7 cells seeded into 48-well plate were pretreated with ZCO (0.0025, 0.005, and 0.01%) or Bay11-7082 (20 μM) for 2 h prior to addition of LPS (500 ng/mL) for 24 h. TNF-α (A) and IL-6 (B) in the supernatants was measured by ELISA and NO production (C) in the supernatants was detected by Griess reagent. Experiments were conducted in quadruplicate and expressed as mean ± SEM ( ∗∗∗ P

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Effect of ZCO on NF-κB transcription and translocation. (A) Effect of ZCO on PMA-induced NF-κB activation in 293T cells. 293T cells seeded into poly-D-lysine hydrobromide coated 96-well plate were transfected with a reporter plasmid, pNF-κB-SEAP for 4 h. Cells were treated with ZCO (0.0025, 0.005, and 0.01%) or Bay11-7082 (20 μM) for 2 h prior to stimulation with 3 ng/mL of PMA for 24 h. The supernatants were collected for NF-κB activity assay. Experiments were conducted in quadruplicate and expressed as mean ± SEM ( ∗∗∗ P
    Figure Legend Snippet: Effect of ZCO on NF-κB transcription and translocation. (A) Effect of ZCO on PMA-induced NF-κB activation in 293T cells. 293T cells seeded into poly-D-lysine hydrobromide coated 96-well plate were transfected with a reporter plasmid, pNF-κB-SEAP for 4 h. Cells were treated with ZCO (0.0025, 0.005, and 0.01%) or Bay11-7082 (20 μM) for 2 h prior to stimulation with 3 ng/mL of PMA for 24 h. The supernatants were collected for NF-κB activity assay. Experiments were conducted in quadruplicate and expressed as mean ± SEM ( ∗∗∗ P

    Techniques Used: Translocation Assay, Activation Assay, Transfection, Plasmid Preparation, Activity Assay

    Effect of ZCO on MAPKs in LPS-activated RAW264.7 cells. RAW264.7 cells cultured into 6-well plate were pretreated with ZCO (0.01 and 0.005%) or Bay11-7082 (10 μM) for 4 h, and then stimulated with LPS (1 μg/mL) for 30 min. Cell lysates (50 μg) were used for Western blotting of the target proteins. Phosphorylated MAPKs were detected by using anti-phospho-JNK, anti-phospho-ERK or anti-phospho-p38 antibody. The membrane was stripped and reassessed with the antibodies targeting non-phosphorylated MAPKs.
    Figure Legend Snippet: Effect of ZCO on MAPKs in LPS-activated RAW264.7 cells. RAW264.7 cells cultured into 6-well plate were pretreated with ZCO (0.01 and 0.005%) or Bay11-7082 (10 μM) for 4 h, and then stimulated with LPS (1 μg/mL) for 30 min. Cell lysates (50 μg) were used for Western blotting of the target proteins. Phosphorylated MAPKs were detected by using anti-phospho-JNK, anti-phospho-ERK or anti-phospho-p38 antibody. The membrane was stripped and reassessed with the antibodies targeting non-phosphorylated MAPKs.

    Techniques Used: Cell Culture, Western Blot

    33) Product Images from "Proteasome Inhibitors Prevent Oxidative Stress-Induced Nerve Cell Death by a Novel Mechanism"

    Article Title: Proteasome Inhibitors Prevent Oxidative Stress-Induced Nerve Cell Death by a Novel Mechanism

    Journal: Biochemical pharmacology

    doi: 10.1016/j.bcp.2008.02.008

    The IKK inhibitor Bay11-7082 blocks activation of IκBα and NF-κB by proteasome inhibitors
    Figure Legend Snippet: The IKK inhibitor Bay11-7082 blocks activation of IκBα and NF-κB by proteasome inhibitors

    Techniques Used: Activation Assay

    34) Product Images from "CRP and TNF-? Induce PAPP-A Expression in Human Peripheral Blood Mononuclear Cells"

    Article Title: CRP and TNF-? Induce PAPP-A Expression in Human Peripheral Blood Mononuclear Cells

    Journal: Mediators of Inflammation

    doi: 10.1155/2012/697832

    Effect of BAY11-7082 on cytokine-induced PAPP-A expression. PBMCs were pretreated with BAY11-7082 (20 μ M) for 60 min and then treated with CRP (20 mg/L) or TNF- α (100 ng/mL) for 24 hours. (a) Detection of PAPP-A mRNA expression was conducted by RT-PCR. (b) PAPP-A protein expression were determined by Western blotting. (c) PAPP-A concentrations were performed by an ultra-sensitive ELISA. The results are expressed as the means ± SD of six donors. ∗: P
    Figure Legend Snippet: Effect of BAY11-7082 on cytokine-induced PAPP-A expression. PBMCs were pretreated with BAY11-7082 (20 μ M) for 60 min and then treated with CRP (20 mg/L) or TNF- α (100 ng/mL) for 24 hours. (a) Detection of PAPP-A mRNA expression was conducted by RT-PCR. (b) PAPP-A protein expression were determined by Western blotting. (c) PAPP-A concentrations were performed by an ultra-sensitive ELISA. The results are expressed as the means ± SD of six donors. ∗: P

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

    35) Product Images from "Betaglycan Alters NFκB-TGFβ2 Cross Talk to Reduce Survival of Human Granulosa Tumor Cells"

    Article Title: Betaglycan Alters NFκB-TGFβ2 Cross Talk to Reduce Survival of Human Granulosa Tumor Cells

    Journal: Molecular Endocrinology

    doi: 10.1210/me.2012-1239

    SMAD3 overexpression counters BAY11-7082/TGFβ2-mediated GCT cell death. A, Quantitative real-time RT-PCR on GCT (n = 17) and normal premenopausal ovary (n = 11) samples, using primers specific to human SMAD3 . Mean ± SEM is shown for each
    Figure Legend Snippet: SMAD3 overexpression counters BAY11-7082/TGFβ2-mediated GCT cell death. A, Quantitative real-time RT-PCR on GCT (n = 17) and normal premenopausal ovary (n = 11) samples, using primers specific to human SMAD3 . Mean ± SEM is shown for each

    Techniques Used: Over Expression, Quantitative RT-PCR

    SMAD3 expression is dependent on NFκB activity in KGN cells. A, Western blot assessment of total SMAD2 and SMAD3 levels in cell lysates from KGN control and WT-BG cells lines after overnight treatment with the NFκB inhibitor, BAY11-7082
    Figure Legend Snippet: SMAD3 expression is dependent on NFκB activity in KGN cells. A, Western blot assessment of total SMAD2 and SMAD3 levels in cell lysates from KGN control and WT-BG cells lines after overnight treatment with the NFκB inhibitor, BAY11-7082

    Techniques Used: Expressing, Activity Assay, Western Blot

    36) Product Images from "Betaglycan Alters NFκB-TGFβ2 Cross Talk to Reduce Survival of Human Granulosa Tumor Cells"

    Article Title: Betaglycan Alters NFκB-TGFβ2 Cross Talk to Reduce Survival of Human Granulosa Tumor Cells

    Journal: Molecular Endocrinology

    doi: 10.1210/me.2012-1239

    SMAD3 overexpression counters BAY11-7082/TGFβ2-mediated GCT cell death. A, Quantitative real-time RT-PCR on GCT (n = 17) and normal premenopausal ovary (n = 11) samples, using primers specific to human SMAD3 . Mean ± SEM is shown for each
    Figure Legend Snippet: SMAD3 overexpression counters BAY11-7082/TGFβ2-mediated GCT cell death. A, Quantitative real-time RT-PCR on GCT (n = 17) and normal premenopausal ovary (n = 11) samples, using primers specific to human SMAD3 . Mean ± SEM is shown for each

    Techniques Used: Over Expression, Quantitative RT-PCR

    SMAD3 expression is dependent on NFκB activity in KGN cells. A, Western blot assessment of total SMAD2 and SMAD3 levels in cell lysates from KGN control and WT-BG cells lines after overnight treatment with the NFκB inhibitor, BAY11-7082
    Figure Legend Snippet: SMAD3 expression is dependent on NFκB activity in KGN cells. A, Western blot assessment of total SMAD2 and SMAD3 levels in cell lysates from KGN control and WT-BG cells lines after overnight treatment with the NFκB inhibitor, BAY11-7082

    Techniques Used: Expressing, Activity Assay, Western Blot

    37) Product Images from "The SH3-SAM Adaptor HACS1 is Up-regulated in B Cell Activation Signaling Cascades"

    Article Title: The SH3-SAM Adaptor HACS1 is Up-regulated in B Cell Activation Signaling Cascades

    Journal: The Journal of Experimental Medicine

    doi: 10.1084/jem.20031816

    IL-4–activated PKCζ and up-regulation of Hacs1 was blocked by inhibition of NF-κB. (A) IL-4 induced phosphorylation of PKCζ in murine splenic B cells. B220 + cells were incubated with 10 ng/ml IL-4 for the indicated time, and expression of phosphorylated PKCζ was analyzed by Western blot. (B and C) Inhibition of NF-κB blocked nuclear expression of NF-κB and the subsequent up-regulation of Hacs1 by IL-4. B220 + cells were pretreated with or without Bay11-7082 or PDTC for 15 min and then incubated with 10 ng/ml IL-4 for the indicated time. The nuclear extracts or whole cell lysates were prepared and analyzed for expression of NF-κB p50 and Stat6 in nuclei (B) or for expression of Hacs1 in whole cells (C) by Western blot.
    Figure Legend Snippet: IL-4–activated PKCζ and up-regulation of Hacs1 was blocked by inhibition of NF-κB. (A) IL-4 induced phosphorylation of PKCζ in murine splenic B cells. B220 + cells were incubated with 10 ng/ml IL-4 for the indicated time, and expression of phosphorylated PKCζ was analyzed by Western blot. (B and C) Inhibition of NF-κB blocked nuclear expression of NF-κB and the subsequent up-regulation of Hacs1 by IL-4. B220 + cells were pretreated with or without Bay11-7082 or PDTC for 15 min and then incubated with 10 ng/ml IL-4 for the indicated time. The nuclear extracts or whole cell lysates were prepared and analyzed for expression of NF-κB p50 and Stat6 in nuclei (B) or for expression of Hacs1 in whole cells (C) by Western blot.

    Techniques Used: Inhibition, Incubation, Expressing, Western Blot

    38) Product Images from "Gene Regulation and Functional Alterations Induced by Kaposi's Sarcoma-Associated Herpesvirus-Encoded ORFK13/vFLIP in Endothelial Cells ▿ in Endothelial Cells ▿ †"

    Article Title: Gene Regulation and Functional Alterations Induced by Kaposi's Sarcoma-Associated Herpesvirus-Encoded ORFK13/vFLIP in Endothelial Cells ▿ in Endothelial Cells ▿ †

    Journal:

    doi: 10.1128/JVI.01871-08

    The IKK/IκB/NF-κB pathway is critical for altered gene expression by K13/vFLIP. (A) Effects of the NF-κB inhibitor Bay11-7082. (a) Schematic representation of the experiment. (b) Representative microscopic morphology of K13/vFLIP-HUVEC
    Figure Legend Snippet: The IKK/IκB/NF-κB pathway is critical for altered gene expression by K13/vFLIP. (A) Effects of the NF-κB inhibitor Bay11-7082. (a) Schematic representation of the experiment. (b) Representative microscopic morphology of K13/vFLIP-HUVEC

    Techniques Used: Expressing

    39) Product Images from "Naringenin-Mediated ATF3 Expression Contributes to Apoptosis in Human Colon Cancer"

    Article Title: Naringenin-Mediated ATF3 Expression Contributes to Apoptosis in Human Colon Cancer

    Journal: Biomolecules & Therapeutics

    doi: 10.4062/biomolther.2015.109

    Dependency of p38 in NAR-mediated ATF3 activation (A) HCT116 cells were pretreated with SB203580 (40 μM, p38 inhibitor), PD98059 (40 μM, ERK1/2 inhibitor), SP600125 (40 μM, JNK inhibitor), SB216763 (20 μM, GSK3β inhibitor) or BAY11-7082 (20 μM, NF-κB inhibitor) for 2 h and then co-treated with 200 μM of NAR for 6 h. Cell lysates were subjected to SDS-PAGE and Western blot was performed using antibodies against ATF3 or actin. (B) HCT116 cells were transfected with pATF3-1420/+34 construct (1 μg) and pRL-null vector (0.1 μg). The cells were pretreated with 40 μM of SB203580 for 2 h and then co-treated with 200 μM of NAR for 24 h. Then, luciferase activity was measured. * p
    Figure Legend Snippet: Dependency of p38 in NAR-mediated ATF3 activation (A) HCT116 cells were pretreated with SB203580 (40 μM, p38 inhibitor), PD98059 (40 μM, ERK1/2 inhibitor), SP600125 (40 μM, JNK inhibitor), SB216763 (20 μM, GSK3β inhibitor) or BAY11-7082 (20 μM, NF-κB inhibitor) for 2 h and then co-treated with 200 μM of NAR for 6 h. Cell lysates were subjected to SDS-PAGE and Western blot was performed using antibodies against ATF3 or actin. (B) HCT116 cells were transfected with pATF3-1420/+34 construct (1 μg) and pRL-null vector (0.1 μg). The cells were pretreated with 40 μM of SB203580 for 2 h and then co-treated with 200 μM of NAR for 24 h. Then, luciferase activity was measured. * p

    Techniques Used: Activation Assay, SDS Page, Western Blot, Transfection, Construct, Plasmid Preparation, Luciferase, Activity Assay

    40) Product Images from "Lactoferrin retargets adenoviruses to TLR4 to induce an abortive NLRP3-associated pyroptotic response in human dendritic cells"

    Article Title: Lactoferrin retargets adenoviruses to TLR4 to induce an abortive NLRP3-associated pyroptotic response in human dendritic cells

    Journal: bioRxiv

    doi: 10.1101/2020.06.03.131664

    Pharmacological inhibition organized by HAdV type DCs were treated for 1 h pre-infection with TLR4 inhibitors oxPAPC, Pepinh-TRIF, Syk inhibitor R406, NLRP3 inhibitor Bay11-7082, RIPK1 inhibitor GSK963 and RIPK3 inhibitors necrosulfonamide and GSK872 (n ≥ 3). Cells were infected with A) HAdV-C5-lactoferrin, B) HAdV-D26-lactoferrin or C) HAdV-B35-lactoferrin complexes and IL-1β release was analyzed 24 h postinfection (n ≥ 3). Statistical analyses by two-tailed Mann-Whitney test.
    Figure Legend Snippet: Pharmacological inhibition organized by HAdV type DCs were treated for 1 h pre-infection with TLR4 inhibitors oxPAPC, Pepinh-TRIF, Syk inhibitor R406, NLRP3 inhibitor Bay11-7082, RIPK1 inhibitor GSK963 and RIPK3 inhibitors necrosulfonamide and GSK872 (n ≥ 3). Cells were infected with A) HAdV-C5-lactoferrin, B) HAdV-D26-lactoferrin or C) HAdV-B35-lactoferrin complexes and IL-1β release was analyzed 24 h postinfection (n ≥ 3). Statistical analyses by two-tailed Mann-Whitney test.

    Techniques Used: Inhibition, Infection, Two Tailed Test, MANN-WHITNEY

    Blocking TLR4 engagement and signaling decrease HAdV-lactoferrin entry and DC maturation A) HAdV-lactoferrin complexes were incubate with TLR4/MD-2 recombinant protein for 30 min. Infection was analyzed 24 h postinfection by flow cytometry (n =11); B) DCs were treated for 1 h pre-infection with TAK-242, HAdV-lactoferrin complex infection was analyzed 24 h postinfection by flow cytometry (n≥3). Cytokine profile of DCs treated HAdV-lactoferrin ± TAK-242; C) IL-1β release following inhibition with TAK-242; D) TNF levels 24 h postinfection ± TAK-242 (n ≥ 3); E) Percent infection following inhibition with oxPAPC (n = 6); F) Percent infection following inhibition with Pepinh-TRIF, R406 or Bay11-7082 (n = 6). G) IL-1β release from DCs incubated with HAdV-lactoferrin ± oxPAPC, Pepinh-TRIF, R406 or Bay11-7082 (n ≥ 3). Statistical analyses by two-tailed Mann-Whitney test.
    Figure Legend Snippet: Blocking TLR4 engagement and signaling decrease HAdV-lactoferrin entry and DC maturation A) HAdV-lactoferrin complexes were incubate with TLR4/MD-2 recombinant protein for 30 min. Infection was analyzed 24 h postinfection by flow cytometry (n =11); B) DCs were treated for 1 h pre-infection with TAK-242, HAdV-lactoferrin complex infection was analyzed 24 h postinfection by flow cytometry (n≥3). Cytokine profile of DCs treated HAdV-lactoferrin ± TAK-242; C) IL-1β release following inhibition with TAK-242; D) TNF levels 24 h postinfection ± TAK-242 (n ≥ 3); E) Percent infection following inhibition with oxPAPC (n = 6); F) Percent infection following inhibition with Pepinh-TRIF, R406 or Bay11-7082 (n = 6). G) IL-1β release from DCs incubated with HAdV-lactoferrin ± oxPAPC, Pepinh-TRIF, R406 or Bay11-7082 (n ≥ 3). Statistical analyses by two-tailed Mann-Whitney test.

    Techniques Used: Blocking Assay, Recombinant, Infection, Flow Cytometry, Inhibition, Incubation, Two Tailed Test, MANN-WHITNEY

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    Article Snippet: .. These cells were then treated with Verteporfin, Selleck, S1786) for 24 h or BAY 11–7082, a NF-κB small molecule inhibitor, for 24 h. RPMI 2650 (Sigma Aldrich), a nasal epithelial cell line, was cultured in 1640 medium with 10% FBS at 37°C in an atmosphere of 5% CO2. ..

    Protease Inhibitor:

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    Article Snippet: .. Isoliquiritigenin (1), phorbol 12-myristate 13-acetate (PMA), phenylmethylsulfonyl fluoride (PMSF), polyvinylidene fluoride (PVDF), PF 06650833 (IRAK4 inhibitor), Bay 11-7082 (NF-κB inhibitor) and protease inhibitor cocktail were purchased from Sigma-Aldrich (St. Louis, MO, USA). ..

    other:

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    Article Snippet: A 10 mM BAY 11–7082 (Millipore Sigma, cat.no.

    Article Title: NF‐κB/IKK activation by small extracellular vesicles within the SASP). NF‐κB/IKK activation by small extracellular vesicles within the SASP
    Article Snippet: Additional small molecular inhibitors used: 10 µM MLN120B (IKKβ, IκB kinase beta; MedChemExpress) and 10 µM BAY11‐7082 (IKKα/β, IκB kinase alpha/beta; Sigma‐Aldrich).

    Incubation:

    Article Title: Anti-Inflammatory and Mineralization Effects of Bromelain on Lipopolysaccharide-Induced Inflammation of Human Dental Pulp Cells
    Article Snippet: .. Then, we exposed them to 5 μg/mL LPS with or without 5 μg/mL bromelain or Bay11-7082 (Sigma-Aldrich), an inhibitor of NF-κB, for 3 h. Then, we fixed the cells with 4% paraformaldehyde for 10 min, permeabilized them with 0.1% Triton X-100 for 15 min, and blocked them with 3% BSA for 1 h. We incubated the cells with a primary antibody against p65 (1:500; Cell Signaling) overnight at 4 °C and then incubated them with an antirabbit secondary antibody (1:200; Cell Signaling) for 1 h at room temperature. ..

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    Millipore bay 11 7082
    RACK1 and ITGB3 are NF-κB target genes and treatment with NF-κB inhibitor BAY 11-7082 alleviates PRRSV replication in Marc-145 cells through TRAF2 and its phosphorylation. Marc-145 cells were infected with PRRSV YN-1 strain two hours after or without pre-treatment with BAY 11-7082. The cells at different time points (2, 12, 24, 36, 48 and 60 hpi) were collected for western blot against RACK1 (A), ITGB3 (B), TRAF2 (C), phosphor-TRAF2 (D), phosphorylated-IκBα (E), p65 (F), phosphorylated-p65 (G), viral N protein (H) and GAPDH (I). Non-infected cells were applied as control.
    Bay 11 7082, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bay 11 7082/product/Millipore
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    Millipore nf κb inhibitor bay117082
    Signaling pathways implicated in SDC1 expression by senescent human breast stromal fibroblasts ( A ) Ionizing radiation-mediated senescent human breast fibroblasts (IS) were treated with the p38 MAPK inhibitor SB203580 or the NF-κB inhibitor <t>BAY117082</t> (10 μM) and 24 h later SDC1 expression was assessed by real-time PCR. ( B ) p53 expression was silenced in IS cells by siRNA, as indicated in the Materials and Methods and SDC1 expression was estimated as in A . One representative experiment out of three similar ones is depicted in each case (* indicates p
    Nf κb Inhibitor Bay117082, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nf κb inhibitor bay117082/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    nf κb inhibitor bay117082 - by Bioz Stars, 2021-09
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    RACK1 and ITGB3 are NF-κB target genes and treatment with NF-κB inhibitor BAY 11-7082 alleviates PRRSV replication in Marc-145 cells through TRAF2 and its phosphorylation. Marc-145 cells were infected with PRRSV YN-1 strain two hours after or without pre-treatment with BAY 11-7082. The cells at different time points (2, 12, 24, 36, 48 and 60 hpi) were collected for western blot against RACK1 (A), ITGB3 (B), TRAF2 (C), phosphor-TRAF2 (D), phosphorylated-IκBα (E), p65 (F), phosphorylated-p65 (G), viral N protein (H) and GAPDH (I). Non-infected cells were applied as control.

    Journal: bioRxiv

    Article Title: Integrin β3, a RACK1 interacting protein, is required for porcine reproductive and respiratory syndrome virus infection and NF-κB activation in Marc-145 cells

    doi: 10.1101/2020.01.27.922476

    Figure Lengend Snippet: RACK1 and ITGB3 are NF-κB target genes and treatment with NF-κB inhibitor BAY 11-7082 alleviates PRRSV replication in Marc-145 cells through TRAF2 and its phosphorylation. Marc-145 cells were infected with PRRSV YN-1 strain two hours after or without pre-treatment with BAY 11-7082. The cells at different time points (2, 12, 24, 36, 48 and 60 hpi) were collected for western blot against RACK1 (A), ITGB3 (B), TRAF2 (C), phosphor-TRAF2 (D), phosphorylated-IκBα (E), p65 (F), phosphorylated-p65 (G), viral N protein (H) and GAPDH (I). Non-infected cells were applied as control.

    Article Snippet: For NF-κB inhibition, Marc-145 cells were pre-treated with 10 μM BAY 11-7082 (#B5556-10MG, Sigma-Aldrich) for 2 hours, followed by medium change and PRRSV infection.

    Techniques: Infection, Western Blot

    Aconine inhibits RANKL-induced NF-κB activation. (A) RAW264.7 cells that were stably transfected with a NF-κB luciferase reporter construct were pretreated with varying concentrations of aconine and the NF-κB inhibitor, BAY11-7082,

    Journal: Acta Pharmacologica Sinica

    Article Title: Aconine inhibits RANKL-induced osteoclast differentiation in RAW264.7 cells by suppressing NF-κB and NFATc1 activation and DC-STAMP expression

    doi: 10.1038/aps.2015.85

    Figure Lengend Snippet: Aconine inhibits RANKL-induced NF-κB activation. (A) RAW264.7 cells that were stably transfected with a NF-κB luciferase reporter construct were pretreated with varying concentrations of aconine and the NF-κB inhibitor, BAY11-7082,

    Article Snippet: Leukocyte Acid Phosphatase (TRAP) Kits, cyclosporin A (CsA) and BAY11-7082 were obtained from Sigma-Aldrich (St Louis, MO, USA).

    Techniques: Activation Assay, Stable Transfection, Transfection, Luciferase, Construct

    xCT inhibition induces intracellular ROS levels through upregulation of NADPH oxidases activities from KSHV-infected PEL cells. (A) BCP-1 and BCBL-1 were incubated with either MSG or SASP at the indicated concentrations for 24 h, then intracellular reactive oxygen species (ROS) were quantified using the ROS-specific dye CM-H2DCFDA and flow cytometry, and normalized to ROS levels for the vehicle-incubated cells. NF-κB inhibitor Bay11-7082 was used as a positive control. (B-C) BCP-1 and BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle for 24 h, then proteins expression were measured by immuoblots. NADPH oxidases activities were measured as described in Methods. (D) BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle in the presence or absence of the antioxidant N -acetylcysteine (NAC) 2.5 mM for 48 h, then cell apoptosis was assessed using Annexin V-PI staining and flow cytometry analysis (** vs MSG group; ## vs SASP group). Error bars represent the S.E.M. for 3 independent experiments. * = p

    Journal: Journal of Hematology & Oncology

    Article Title: Targeting xCT, a cystine-glutamate transporter induces apoptosis and tumor regression for KSHV/HIV-associated lymphoma

    doi: 10.1186/1756-8722-7-30

    Figure Lengend Snippet: xCT inhibition induces intracellular ROS levels through upregulation of NADPH oxidases activities from KSHV-infected PEL cells. (A) BCP-1 and BCBL-1 were incubated with either MSG or SASP at the indicated concentrations for 24 h, then intracellular reactive oxygen species (ROS) were quantified using the ROS-specific dye CM-H2DCFDA and flow cytometry, and normalized to ROS levels for the vehicle-incubated cells. NF-κB inhibitor Bay11-7082 was used as a positive control. (B-C) BCP-1 and BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle for 24 h, then proteins expression were measured by immuoblots. NADPH oxidases activities were measured as described in Methods. (D) BCBL-1 were treated with either MSG (20 mM), SASP (0.5 mM) or vehicle in the presence or absence of the antioxidant N -acetylcysteine (NAC) 2.5 mM for 48 h, then cell apoptosis was assessed using Annexin V-PI staining and flow cytometry analysis (** vs MSG group; ## vs SASP group). Error bars represent the S.E.M. for 3 independent experiments. * = p

    Article Snippet: Monosodium glutamate (MSG), Sulfasalazine (SASP) and Bay11-7082 were purchased from Sigma.

    Techniques: Inhibition, Infection, Incubation, Flow Cytometry, Cytometry, Positive Control, Expressing, Staining

    Signaling pathways implicated in SDC1 expression by senescent human breast stromal fibroblasts ( A ) Ionizing radiation-mediated senescent human breast fibroblasts (IS) were treated with the p38 MAPK inhibitor SB203580 or the NF-κB inhibitor BAY117082 (10 μM) and 24 h later SDC1 expression was assessed by real-time PCR. ( B ) p53 expression was silenced in IS cells by siRNA, as indicated in the Materials and Methods and SDC1 expression was estimated as in A . One representative experiment out of three similar ones is depicted in each case (* indicates p

    Journal: Aging (Albany NY)

    Article Title: Ionizing radiation-mediated premature senescence and paracrine interactions with cancer cells enhance the expression of syndecan 1 in human breast stromal fibroblasts: the role of TGF-β

    doi: 10.18632/aging.100989

    Figure Lengend Snippet: Signaling pathways implicated in SDC1 expression by senescent human breast stromal fibroblasts ( A ) Ionizing radiation-mediated senescent human breast fibroblasts (IS) were treated with the p38 MAPK inhibitor SB203580 or the NF-κB inhibitor BAY117082 (10 μM) and 24 h later SDC1 expression was assessed by real-time PCR. ( B ) p53 expression was silenced in IS cells by siRNA, as indicated in the Materials and Methods and SDC1 expression was estimated as in A . One representative experiment out of three similar ones is depicted in each case (* indicates p

    Article Snippet: The p38 MAPK inhibitor SB203580, and the NF-κB inhibitor BAY117082 were from Sigma, while the Sp1 inhibitor mithramycin from Cayman Chemical (Ann Arbor, MI, USA).

    Techniques: Expressing, Real-time Polymerase Chain Reaction