erk inhibitor pd98059  (Millipore)


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  • 99
    Name:
    PD 98 059
    Description:

    Catalog Number:
    p215
    Price:
    None
    Applications:
    PD 98,059 has been used:. in growth medium as a mitogen-activated protein (MAP) kinase inhibitor, in order to study the secondary messengers involved in the effect of D1-like receptors. in calcium-free RPMI (Roswell park memorial institute)-1640 medium to study its effect on inflammation, proliferation and differentiation in human epidermal keratinocyte cell line in conjunction of cystic fibrosis transmembrane conductance regulator (CFTR) knockdown. in culture medium for cell migration assay
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    Structured Review

    Millipore erk inhibitor pd98059
    PD 98 059

    https://www.bioz.com/result/erk inhibitor pd98059/product/Millipore
    Average 99 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    erk inhibitor pd98059 - by Bioz Stars, 2020-11
    99/100 stars

    Images

    1) Product Images from "p38MAPK, ERK and PI3K Signaling Pathways Are Involved in C5a-Primed Neutrophils for ANCA-Mediated Activation"

    Article Title: p38MAPK, ERK and PI3K Signaling Pathways Are Involved in C5a-Primed Neutrophils for ANCA-Mediated Activation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0038317

    Neutrophil respiratory burst induced by patient-derived MPO-ANCA-positive IgG or PR3-ANCA-positive IgG in C5a-primed cells. Neutrophil respiratory burst induced by patient-derived MPO-ANCA-positive IgG (A) or PR3-ANCA-positive IgG (B) was measured by conversion of dihydrorhodamine-123 (DHR-123) to rhodamine-123 in C5a-primed cells in the presence and absence of SB202190, PD98059, LY294002 or the mixture of above-mentioned three inhibitors, respectively. Differences of MFI between groups were assessed using the paired t test. C–H were representative histograms showing that MPO-ANCA-positive IgG and PR3-ANCA-positive IgG induced respiratory burst in C5a-primed neutrophils and that inhibition of p38MAPK, ERK and PI3K reduced the ANCA-induced respiratory burst. Bars represent mean±SD of 5 MPO-ANCA-positive IgG and 3 PR3-ANCA-positive IgG preparations, each measured on neutrophils of 10 independent experiments and donors.
    Figure Legend Snippet: Neutrophil respiratory burst induced by patient-derived MPO-ANCA-positive IgG or PR3-ANCA-positive IgG in C5a-primed cells. Neutrophil respiratory burst induced by patient-derived MPO-ANCA-positive IgG (A) or PR3-ANCA-positive IgG (B) was measured by conversion of dihydrorhodamine-123 (DHR-123) to rhodamine-123 in C5a-primed cells in the presence and absence of SB202190, PD98059, LY294002 or the mixture of above-mentioned three inhibitors, respectively. Differences of MFI between groups were assessed using the paired t test. C–H were representative histograms showing that MPO-ANCA-positive IgG and PR3-ANCA-positive IgG induced respiratory burst in C5a-primed neutrophils and that inhibition of p38MAPK, ERK and PI3K reduced the ANCA-induced respiratory burst. Bars represent mean±SD of 5 MPO-ANCA-positive IgG and 3 PR3-ANCA-positive IgG preparations, each measured on neutrophils of 10 independent experiments and donors.

    Techniques Used: Derivative Assay, Inhibition

    Effects of the p38MAPK inhibitor, ERK and PI3K inhibitor on translocation of PR3. A: Neutrophils were incubated with the SB202190, PD98059, LY294002 or the inhibitors mixture or vehicle for 30 min prior to incubation with C5a (100 ng/ml). Bars represent mean±SD of repeated measurements on neutrophils of 10 independent experiments and donors. T test was used for comparison. B-D: a representative histogram of effects of the above inhibitors on translocation of PR3 upon C5a priming.
    Figure Legend Snippet: Effects of the p38MAPK inhibitor, ERK and PI3K inhibitor on translocation of PR3. A: Neutrophils were incubated with the SB202190, PD98059, LY294002 or the inhibitors mixture or vehicle for 30 min prior to incubation with C5a (100 ng/ml). Bars represent mean±SD of repeated measurements on neutrophils of 10 independent experiments and donors. T test was used for comparison. B-D: a representative histogram of effects of the above inhibitors on translocation of PR3 upon C5a priming.

    Techniques Used: Translocation Assay, Incubation

    2) Product Images from "Hypoxia Promotes Dopaminergic Differentiation of Mesenchymal Stem Cells and Shows Benefits for Transplantation in a Rat Model of Parkinson's Disease"

    Article Title: Hypoxia Promotes Dopaminergic Differentiation of Mesenchymal Stem Cells and Shows Benefits for Transplantation in a Rat Model of Parkinson's Disease

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0054296

    HIF-1α, ERK and p38 are involved in hypoxia-induced neural differentiation of rMSCs. (A) HIF-1α is stably expressed in 3% O 2 -induced neurospheres. (B) Immunostaining of nestin in rMSC-derived neurospheres after respective treatment with HIF-1α inhibitor echinomycin, JNK inhibitor SP600125, ERK inhibitor PD98059 and p38 inhibitor SB203580. Scale bar = 100 µm. (C) Quantitative analysis of optical density of nestin expression in B by densitometry. The data are presented as means ± SEM of 6 individual wells. (D) Western blot analysis of phosphorylated JNK, ERK and p38 in rMSC-derived neurospheres. The graph presented is representative of 3 independent experiments with similar results. (E) Quantitative analysis of phosphorylated JNK, ERK and p38 in D. (F) The effect of inhibitors on mRNA of En1 , En2 , Nurr1 , Pitx3 and Lmx1b in rMSC-derived neurospheres. The data presented are normalized to their respective control ( n = 4). (G) Western blot analysis of total HIF-1α in 3% O 2 -induced neurospheres after respective treatment with echinomycin, PD98059 and SB203580. HIF-1β was used as an internal control. The graph presented is representative of 4 independent experiments with similar results. (H) Quantitative analysis of HIF-1α in G. (I) Western blot analysis of cytoplasmic and nuclear HIF-1α in 3% O 2 -induced neurospheres after respective treatment with echinomycin, PD98059 and SB203580. The graph presented is representative of 4 independent experiments with similar results. (J) Quantitative analysis of cytoplasmic and nuclear HIF-1α in I. Data represent mean ± SEM, * P
    Figure Legend Snippet: HIF-1α, ERK and p38 are involved in hypoxia-induced neural differentiation of rMSCs. (A) HIF-1α is stably expressed in 3% O 2 -induced neurospheres. (B) Immunostaining of nestin in rMSC-derived neurospheres after respective treatment with HIF-1α inhibitor echinomycin, JNK inhibitor SP600125, ERK inhibitor PD98059 and p38 inhibitor SB203580. Scale bar = 100 µm. (C) Quantitative analysis of optical density of nestin expression in B by densitometry. The data are presented as means ± SEM of 6 individual wells. (D) Western blot analysis of phosphorylated JNK, ERK and p38 in rMSC-derived neurospheres. The graph presented is representative of 3 independent experiments with similar results. (E) Quantitative analysis of phosphorylated JNK, ERK and p38 in D. (F) The effect of inhibitors on mRNA of En1 , En2 , Nurr1 , Pitx3 and Lmx1b in rMSC-derived neurospheres. The data presented are normalized to their respective control ( n = 4). (G) Western blot analysis of total HIF-1α in 3% O 2 -induced neurospheres after respective treatment with echinomycin, PD98059 and SB203580. HIF-1β was used as an internal control. The graph presented is representative of 4 independent experiments with similar results. (H) Quantitative analysis of HIF-1α in G. (I) Western blot analysis of cytoplasmic and nuclear HIF-1α in 3% O 2 -induced neurospheres after respective treatment with echinomycin, PD98059 and SB203580. The graph presented is representative of 4 independent experiments with similar results. (J) Quantitative analysis of cytoplasmic and nuclear HIF-1α in I. Data represent mean ± SEM, * P

    Techniques Used: Stable Transfection, Immunostaining, Derivative Assay, Expressing, Western Blot

    3) Product Images from "Upregulation of ERK phosphorylation in rat dorsal root ganglion neurons contributes to oxaliplatin-induced chronic neuropathic pain"

    Article Title: Upregulation of ERK phosphorylation in rat dorsal root ganglion neurons contributes to oxaliplatin-induced chronic neuropathic pain

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0225586

    Effect of ERK inhibitor PD98059 on oxaliplatin-induced upregulation of ERK phosphorylation in rat DRG. (A) The ratio of p-ERK to ERK expression was significantly increased in DRG of oxaliplatin treated rats, which was inhibited by PD98059. (B) No difference was observed in the protein level of ERK among sham, oxaliplatin + vehicle (20% DMSO), and oxaliplatin + PD98059 treatment groups. Comparisons between two groups of the blots were performed by Student’s t-test. All data are calculated as mean ± SD of 5 animals. ** P
    Figure Legend Snippet: Effect of ERK inhibitor PD98059 on oxaliplatin-induced upregulation of ERK phosphorylation in rat DRG. (A) The ratio of p-ERK to ERK expression was significantly increased in DRG of oxaliplatin treated rats, which was inhibited by PD98059. (B) No difference was observed in the protein level of ERK among sham, oxaliplatin + vehicle (20% DMSO), and oxaliplatin + PD98059 treatment groups. Comparisons between two groups of the blots were performed by Student’s t-test. All data are calculated as mean ± SD of 5 animals. ** P

    Techniques Used: Expressing

    Inhibition of oxaliplatin-induced mechanical allodynia by ERK inhibitor PD98059. PD98059 (6 μg day -1 ) or vehicle (20% DMSO) was injected i.t. for 4 weeks using an osmotic pressure pump. One week after the pump placement, oxaliplatin (4 mg kg -1 ) or vehicle (5% glucose) was injected i.p. twice a week for 3 weeks. von Frey test was done before the pump placement, and before and 1 week after each oxaliplatin or vehicle treatment (days 1, 2, 8, 9, 15, and 16). We confirmed the incidence of mechanical allodynia on day 22 (day 28 from pump placement). The hindpaw data within each group were analyzed using one-way repeated measures ANOVA followed by Bonferroni post hoc analysis. Welch’s test was used to compare between groups. All data are calculated as mean ± SEM of 5 animals. * P
    Figure Legend Snippet: Inhibition of oxaliplatin-induced mechanical allodynia by ERK inhibitor PD98059. PD98059 (6 μg day -1 ) or vehicle (20% DMSO) was injected i.t. for 4 weeks using an osmotic pressure pump. One week after the pump placement, oxaliplatin (4 mg kg -1 ) or vehicle (5% glucose) was injected i.p. twice a week for 3 weeks. von Frey test was done before the pump placement, and before and 1 week after each oxaliplatin or vehicle treatment (days 1, 2, 8, 9, 15, and 16). We confirmed the incidence of mechanical allodynia on day 22 (day 28 from pump placement). The hindpaw data within each group were analyzed using one-way repeated measures ANOVA followed by Bonferroni post hoc analysis. Welch’s test was used to compare between groups. All data are calculated as mean ± SEM of 5 animals. * P

    Techniques Used: Inhibition, Injection

    4) Product Images from "Microbial Antigens Stimulate Metalloprotease-7 Secretion in Human B-Lymphocytes Using mTOR-Dependent and Independent Pathways"

    Article Title: Microbial Antigens Stimulate Metalloprotease-7 Secretion in Human B-Lymphocytes Using mTOR-Dependent and Independent Pathways

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-04199-2

    CpG and Curdlan have synergistic effect on MMP-7. MMP-7 was detected by Immunoblotting ( A ) or ELISA ( B , C ) in the supernatant of B-lymphocytes after stimulation with CpG, Curdlan and the combination of CpG and Curdlan overnight. Cells were pre-incubated with 30 μM PD98059 and the 20 μM SP600125, 10 μM SR11302, 10 μM Bay 117085 and (100 nM) Rapamycin prior to Curdlan stimulation as indicated. Data are representative of at least three independent experiments. * p
    Figure Legend Snippet: CpG and Curdlan have synergistic effect on MMP-7. MMP-7 was detected by Immunoblotting ( A ) or ELISA ( B , C ) in the supernatant of B-lymphocytes after stimulation with CpG, Curdlan and the combination of CpG and Curdlan overnight. Cells were pre-incubated with 30 μM PD98059 and the 20 μM SP600125, 10 μM SR11302, 10 μM Bay 117085 and (100 nM) Rapamycin prior to Curdlan stimulation as indicated. Data are representative of at least three independent experiments. * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Incubation

    JNK and the transcriptions factors AP-1 and NF-κB participate in the regulation of MMP7 of CpG-Activated B-lymphocytes. MMP-7 was detected by immunoblotting ( A , C ) or by ELISA ( B , D ) in the cell supernatant (med) of unstimulated or CpG-stimulated cells. Cells were pretreated for one hour with the MAPK inhibitors, 30 μM PD98059 and 20 μM SP600125; or the transcription factor inhibitors, 10 μM Bay 117085 and 10 μM SR11302. ( D ) Cells were treated with different concentrations of the inhibitors as indicated. XTT was measured after 24 hours. Data are representative of at least three independent experiments. * p
    Figure Legend Snippet: JNK and the transcriptions factors AP-1 and NF-κB participate in the regulation of MMP7 of CpG-Activated B-lymphocytes. MMP-7 was detected by immunoblotting ( A , C ) or by ELISA ( B , D ) in the cell supernatant (med) of unstimulated or CpG-stimulated cells. Cells were pretreated for one hour with the MAPK inhibitors, 30 μM PD98059 and 20 μM SP600125; or the transcription factor inhibitors, 10 μM Bay 117085 and 10 μM SR11302. ( D ) Cells were treated with different concentrations of the inhibitors as indicated. XTT was measured after 24 hours. Data are representative of at least three independent experiments. * p

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Curdlan induces MMP7 in an mTOR-independent manner. MMP-7 secretion was measured by immunoblotting ( A , C , E ) or ELISA ( B , D , F ) in the cell supernatant of unstimulated or Curdlan-stimulated cells. Cells were pre-incubated with 30 μM PD98059, 20 μM SP600125, 10 μM SR11302, 10 μM Bay 11-7085 and (100 nM) Rapamycin prior to Curdlan stimulation as indicated. ( G ) Phosphorylation of mTOR, S6K and ERK were detected by immunoblotting in the cell lysate of Curdlan-stimulated cells in the presence of 30 μM PD98059 and (100 nM) Rapamycin. Total mTOR, S6K and ERK were used as controls. Data are representative of at least three independent experiments. * p
    Figure Legend Snippet: Curdlan induces MMP7 in an mTOR-independent manner. MMP-7 secretion was measured by immunoblotting ( A , C , E ) or ELISA ( B , D , F ) in the cell supernatant of unstimulated or Curdlan-stimulated cells. Cells were pre-incubated with 30 μM PD98059, 20 μM SP600125, 10 μM SR11302, 10 μM Bay 11-7085 and (100 nM) Rapamycin prior to Curdlan stimulation as indicated. ( G ) Phosphorylation of mTOR, S6K and ERK were detected by immunoblotting in the cell lysate of Curdlan-stimulated cells in the presence of 30 μM PD98059 and (100 nM) Rapamycin. Total mTOR, S6K and ERK were used as controls. Data are representative of at least three independent experiments. * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Incubation

    5) Product Images from "Bryostatin and its synthetic analog, picolog rescue dermal fibroblasts from prolonged stress and contribute to survival and rejuvenation of human skin equivalents"

    Article Title: Bryostatin and its synthetic analog, picolog rescue dermal fibroblasts from prolonged stress and contribute to survival and rejuvenation of human skin equivalents

    Journal: Journal of cellular physiology

    doi: 10.1002/jcp.26043

    Activation of Erk by bryostatin-1 protect dermal fibroblasts Inhibition of Erk reverses the protective effect of bryostatin-1 on human skin fibroblasts (AG04560) cultured under long-term serum starvation conditions. (A) After 5 days of culture under serum-deprived conditions, untreated skin fibroblasts (Bry- Inh-) showed poor cellular integrity. Fibroblasts treated with bryostatin-1 (Bry+ Inh-) showed greater survival and fewer dead cells after 5 days of serum-free culture compared to untreated cells. Treatment of cells with the Erk inhibitor PD98059 (Bry- Inh+) decreased cellular integrity under serum deprived conditions, similar to untreated cells. Blocking Erk activation decreased cellular integrity even in the presence of bryostatin-1 (Bry+ Inh+). Images are representative of experiments conducted in triplicate. Immunoblot analysis of activated Erk in response to 0.3 nM bryostatin-1 in serum-deprived cultured human skin fibroblasts. (B) Bryostatin-1 induced prolonged activation of Erk measured by immunoblot analysis. Cultured dermal fibroblasts were serum starved for 24 hours and then treated with 0.3 nM bryostatin-1 (Bry) for 0, 1, 2, 4, 8, and 24 hours in serum-free conditions. Representative immunoblot showing activated p-Erk1 and p-Erk2, unphosphorylated Erk1/2, and β-Actin as a loading control. (C) Activated Erk1/2 (p-Erk1/2) was quantified by normalizing against total Erk1/2 (p-Erk/Erk). Results are mean±SEM from three independent measurements starting from cell culturing. (D) Representative immunoblot of Erk activation in fibroblasts treated with bryostatin-1 (Bry) in the presence or absence of the Erk inhibitor PD98059 (Inh; 30 µM). PD98059 blocked bryostatin-1 induced Erk activation in cultured human fibroblasts. Results are mean±SEM for three different experiments; Bar=10µm.
    Figure Legend Snippet: Activation of Erk by bryostatin-1 protect dermal fibroblasts Inhibition of Erk reverses the protective effect of bryostatin-1 on human skin fibroblasts (AG04560) cultured under long-term serum starvation conditions. (A) After 5 days of culture under serum-deprived conditions, untreated skin fibroblasts (Bry- Inh-) showed poor cellular integrity. Fibroblasts treated with bryostatin-1 (Bry+ Inh-) showed greater survival and fewer dead cells after 5 days of serum-free culture compared to untreated cells. Treatment of cells with the Erk inhibitor PD98059 (Bry- Inh+) decreased cellular integrity under serum deprived conditions, similar to untreated cells. Blocking Erk activation decreased cellular integrity even in the presence of bryostatin-1 (Bry+ Inh+). Images are representative of experiments conducted in triplicate. Immunoblot analysis of activated Erk in response to 0.3 nM bryostatin-1 in serum-deprived cultured human skin fibroblasts. (B) Bryostatin-1 induced prolonged activation of Erk measured by immunoblot analysis. Cultured dermal fibroblasts were serum starved for 24 hours and then treated with 0.3 nM bryostatin-1 (Bry) for 0, 1, 2, 4, 8, and 24 hours in serum-free conditions. Representative immunoblot showing activated p-Erk1 and p-Erk2, unphosphorylated Erk1/2, and β-Actin as a loading control. (C) Activated Erk1/2 (p-Erk1/2) was quantified by normalizing against total Erk1/2 (p-Erk/Erk). Results are mean±SEM from three independent measurements starting from cell culturing. (D) Representative immunoblot of Erk activation in fibroblasts treated with bryostatin-1 (Bry) in the presence or absence of the Erk inhibitor PD98059 (Inh; 30 µM). PD98059 blocked bryostatin-1 induced Erk activation in cultured human fibroblasts. Results are mean±SEM for three different experiments; Bar=10µm.

    Techniques Used: Activation Assay, Inhibition, Cell Culture, Blocking Assay

    6) Product Images from "The effects of ursolic acid on cytokine production via the MAPK pathways in leukemic T-cells"

    Article Title: The effects of ursolic acid on cytokine production via the MAPK pathways in leukemic T-cells

    Journal: EXCLI Journal

    doi:

    Inhibition of PMA/PHA induced-IL-2 and TNF-α production by ursolic acid via the JNK pathway; Western blot analysis (representative figure of three independent experiments). Cell were pre-incubated with UA for 0 to 12 hours, PD98059 or SP600125 for 12 hours prior to addition of PMA/PHA for a further 12 hours, or only DMSO (C) for 24 hours. For positive control (P) cells were left without treatment for 12 hours prior to addition of PMA/PHA for a further 12 hours. Protein expression of (a) p-ERK1/2 (42, 44 kDa), ERK1/2 (42, 44 kDa) and β-actin (45kDa) was detected by Western blot and normalized with β-actin. (b), (c), (d) Relative p-ERK, ERK and p-ERK/ERK protein level was calculated. Protein expression of (e) p-JNK (46, 54 kDa), JNK (46, 54 kDa) and β-actin (45kDa) was detected by Western blot and normalized with β-actin. (f), (g), (h) Relative p-JNK, JNK and p-JNK/JNK protein level was calculated. Statistical analysis was carried out with one-way ANOVA followed by Tukey's multiple comparison test compared with positive controls (PMA/PHA) (* P
    Figure Legend Snippet: Inhibition of PMA/PHA induced-IL-2 and TNF-α production by ursolic acid via the JNK pathway; Western blot analysis (representative figure of three independent experiments). Cell were pre-incubated with UA for 0 to 12 hours, PD98059 or SP600125 for 12 hours prior to addition of PMA/PHA for a further 12 hours, or only DMSO (C) for 24 hours. For positive control (P) cells were left without treatment for 12 hours prior to addition of PMA/PHA for a further 12 hours. Protein expression of (a) p-ERK1/2 (42, 44 kDa), ERK1/2 (42, 44 kDa) and β-actin (45kDa) was detected by Western blot and normalized with β-actin. (b), (c), (d) Relative p-ERK, ERK and p-ERK/ERK protein level was calculated. Protein expression of (e) p-JNK (46, 54 kDa), JNK (46, 54 kDa) and β-actin (45kDa) was detected by Western blot and normalized with β-actin. (f), (g), (h) Relative p-JNK, JNK and p-JNK/JNK protein level was calculated. Statistical analysis was carried out with one-way ANOVA followed by Tukey's multiple comparison test compared with positive controls (PMA/PHA) (* P

    Techniques Used: Inhibition, Western Blot, Incubation, Positive Control, Expressing

    7) Product Images from "Low molecular weight fucoidan protects renal tubular cells from injury induced by albumin overload"

    Article Title: Low molecular weight fucoidan protects renal tubular cells from injury induced by albumin overload

    Journal: Scientific Reports

    doi: 10.1038/srep31759

    LMWF blocked NF-κB pathway activation induced by albumin in NRK-52E cells. ( A ) Expression levels of p-ERK, ERK2, and β-actin were detected by Western blot analysis. NRK-52E cells were pretreated with 1~20 μg/mL LMWF or PBS for 2 h and then were exposed to 10 mg/mL albumin or PBS for 15 min. Representative blots (left) and relative ratios of protein levels (right) are shown. ( B ) Expression levels of p-p65, p65, and β-actin in NRK-52E cells incubated with 1~20 μg /mL LMWF or PBS under 10 mg/mL albumin or PBS treatment for 48 h were determined by Western blot analysis. Left graph shows the representative blots and the right graph shows the density ratios. ( C ) Effect of ERK inhibitor PD98059 on albumin induced COX-2 expression. Cells were incubated with 10 mg/mL albumin or PBS in the presence or absence of LMWF or 20 μmol/L ERK inhibitor PD98059 (PD) for 48 h and were collected for Western analysis. Left graph shows the representative blots and the right graph shows the density ratios. Means ± SEM, n = 3~4. *P
    Figure Legend Snippet: LMWF blocked NF-κB pathway activation induced by albumin in NRK-52E cells. ( A ) Expression levels of p-ERK, ERK2, and β-actin were detected by Western blot analysis. NRK-52E cells were pretreated with 1~20 μg/mL LMWF or PBS for 2 h and then were exposed to 10 mg/mL albumin or PBS for 15 min. Representative blots (left) and relative ratios of protein levels (right) are shown. ( B ) Expression levels of p-p65, p65, and β-actin in NRK-52E cells incubated with 1~20 μg /mL LMWF or PBS under 10 mg/mL albumin or PBS treatment for 48 h were determined by Western blot analysis. Left graph shows the representative blots and the right graph shows the density ratios. ( C ) Effect of ERK inhibitor PD98059 on albumin induced COX-2 expression. Cells were incubated with 10 mg/mL albumin or PBS in the presence or absence of LMWF or 20 μmol/L ERK inhibitor PD98059 (PD) for 48 h and were collected for Western analysis. Left graph shows the representative blots and the right graph shows the density ratios. Means ± SEM, n = 3~4. *P

    Techniques Used: Activation Assay, Expressing, Western Blot, Incubation

    8) Product Images from "Neuronal regulation of type 2 innate lymphoid cells via neuromedin U"

    Article Title: Neuronal regulation of type 2 innate lymphoid cells via neuromedin U

    Journal: Nature

    doi: 10.1038/nature23469

    NMU regulates ILC2-derived cytokines via ERK1/2 and a Ca 2+ /Calcineurin/NFAT cascade. Intestinal ILC2 activation by NMU. a , Top: p-ERK. Bottom: Percentage of p-ERK cells n=4. Mean fluorescence intensity (MFI) of p-ERK expression. n=4. b , Il5 , Il13 and Csf2 expression in ILC2s cultured with medium (control), NmU23 or NmU23 and ERK inhibitor PD98059. n=3. c , Left and centre: Ca 2+ influx, represented by Fluo-4 AM intensity. NmU23 was added 60 seconds after ILC2 baseline acquisition (arrow). Right: Mean intensity of Ca 2+ influx. n=3. d , Il5 , Il13 and Csf2 expression in ILC2s cultured with medium (control), NmU23 or NmU23 and Calcineurin inhibitor FK506. n=12. e , Nuclear translocation of NFAT (red) upon NmU23 activation in ILC2. f , Left: Percentage of ILC2 with nuclear NFAT. n=3. Right: NFAT nuclear fluorescence intensity. Control n=16; NmU23 n=7; P+I n=8. g , Il5 , Il13 and Csf2 expression in ILC2s cultured with medium (control), NmU23 or NmU23 and NFAT inhibitor 11R-VIVIT. n=6. Scale bars: 5μm. Data are representative of 2-4 independent experiments. Error bars show s.e.m. *P
    Figure Legend Snippet: NMU regulates ILC2-derived cytokines via ERK1/2 and a Ca 2+ /Calcineurin/NFAT cascade. Intestinal ILC2 activation by NMU. a , Top: p-ERK. Bottom: Percentage of p-ERK cells n=4. Mean fluorescence intensity (MFI) of p-ERK expression. n=4. b , Il5 , Il13 and Csf2 expression in ILC2s cultured with medium (control), NmU23 or NmU23 and ERK inhibitor PD98059. n=3. c , Left and centre: Ca 2+ influx, represented by Fluo-4 AM intensity. NmU23 was added 60 seconds after ILC2 baseline acquisition (arrow). Right: Mean intensity of Ca 2+ influx. n=3. d , Il5 , Il13 and Csf2 expression in ILC2s cultured with medium (control), NmU23 or NmU23 and Calcineurin inhibitor FK506. n=12. e , Nuclear translocation of NFAT (red) upon NmU23 activation in ILC2. f , Left: Percentage of ILC2 with nuclear NFAT. n=3. Right: NFAT nuclear fluorescence intensity. Control n=16; NmU23 n=7; P+I n=8. g , Il5 , Il13 and Csf2 expression in ILC2s cultured with medium (control), NmU23 or NmU23 and NFAT inhibitor 11R-VIVIT. n=6. Scale bars: 5μm. Data are representative of 2-4 independent experiments. Error bars show s.e.m. *P

    Techniques Used: Derivative Assay, Activation Assay, Fluorescence, Expressing, Cell Culture, Translocation Assay

    9) Product Images from "Disruption of transient receptor potential melastatin 2 decreases elastase release and bacterial clearance in neutrophils"

    Article Title: Disruption of transient receptor potential melastatin 2 decreases elastase release and bacterial clearance in neutrophils

    Journal: Innate Immunity

    doi: 10.1177/1753425918759181

    TRPM2 deficiency decreases fMLP-induced elastase release in neutrophils by decreasing p38 MAPKs phosphorylation. (a) Effects of MAPKs inhibitors on extracelluar elastase release in neutrophils in response to fMLP stimulation. WT BMNs were pre-treated with specific inhibitors of the MAPKs (p38 MAPK inhibitor SB203580 (10 µM), Erk inhibitor PD98059 (10 µM), Jnk inhibitor SP600125 (10 µM), or DMSO for 30 min. WT BMNs were then stimulated with 100 nM fMLP for 10 min at 37°C. Elastase concentration in the supernatant was measured by elastase assay kit ( n = 4 per group). *** P
    Figure Legend Snippet: TRPM2 deficiency decreases fMLP-induced elastase release in neutrophils by decreasing p38 MAPKs phosphorylation. (a) Effects of MAPKs inhibitors on extracelluar elastase release in neutrophils in response to fMLP stimulation. WT BMNs were pre-treated with specific inhibitors of the MAPKs (p38 MAPK inhibitor SB203580 (10 µM), Erk inhibitor PD98059 (10 µM), Jnk inhibitor SP600125 (10 µM), or DMSO for 30 min. WT BMNs were then stimulated with 100 nM fMLP for 10 min at 37°C. Elastase concentration in the supernatant was measured by elastase assay kit ( n = 4 per group). *** P

    Techniques Used: Concentration Assay

    10) Product Images from "TGF-β1 induces HMGA1 expression: The role of HMGA1 in thyroid cancer proliferation and invasion"

    Article Title: TGF-β1 induces HMGA1 expression: The role of HMGA1 in thyroid cancer proliferation and invasion

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.3958

    TGF-β1 induces HMGA1 expression through PI3K signaling and ERK signaling in SW579 cells. (A) The effects of wortmannin, PD98059 and U0126 on the mRNA expression of HMGA1 induced by treatment with 5 ng/ml of TGF-β1 in SW579 cells. (B and C) The effects of wortmannin, PD98059 and U0126 on the expression of HMGA1 induced by treatment 5 ng/ml with TGF-β1 in SW579 cells. Fluorescence were gathered and analyzed with a fluorescence microscope (Olympus). * P
    Figure Legend Snippet: TGF-β1 induces HMGA1 expression through PI3K signaling and ERK signaling in SW579 cells. (A) The effects of wortmannin, PD98059 and U0126 on the mRNA expression of HMGA1 induced by treatment with 5 ng/ml of TGF-β1 in SW579 cells. (B and C) The effects of wortmannin, PD98059 and U0126 on the expression of HMGA1 induced by treatment 5 ng/ml with TGF-β1 in SW579 cells. Fluorescence were gathered and analyzed with a fluorescence microscope (Olympus). * P

    Techniques Used: Expressing, Fluorescence, Microscopy

    11) Product Images from "Curcumin Improves Amyloid β-Peptide (1-42) Induced Spatial Memory Deficits through BDNF-ERK Signaling Pathway"

    Article Title: Curcumin Improves Amyloid β-Peptide (1-42) Induced Spatial Memory Deficits through BDNF-ERK Signaling Pathway

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0131525

    Effect of intra-hippocampal injections of ERK inhibitor or GSK3 activator on spatial learning function in the rat model of Alzheimer's disease. The ERK inhibitor PD98059 (20 μM) or GSK3 activator wortmannin (100 μM) (combined with chronic curcumin i.p. injection) was injected bilaterally into the hippocampus 30 min before the water-maze training trial. (A) Swim speed in each training trial. (B) The escape latency during the water maze training trials. (C) The time spent in the target quadrant and (D) the number of times crossing the platform in the probe task. n = 8/group. For panel B, * P
    Figure Legend Snippet: Effect of intra-hippocampal injections of ERK inhibitor or GSK3 activator on spatial learning function in the rat model of Alzheimer's disease. The ERK inhibitor PD98059 (20 μM) or GSK3 activator wortmannin (100 μM) (combined with chronic curcumin i.p. injection) was injected bilaterally into the hippocampus 30 min before the water-maze training trial. (A) Swim speed in each training trial. (B) The escape latency during the water maze training trials. (C) The time spent in the target quadrant and (D) the number of times crossing the platform in the probe task. n = 8/group. For panel B, * P

    Techniques Used: Injection

    12) Product Images from "Regulator of G-Protein Signaling 19 (RGS19) and Its Partner G?-Inhibiting Activity Polypeptide 3 (GNAI3) Are Required for zVAD-Induced Autophagy and Cell Death in L929 Cells"

    Article Title: Regulator of G-Protein Signaling 19 (RGS19) and Its Partner G?-Inhibiting Activity Polypeptide 3 (GNAI3) Are Required for zVAD-Induced Autophagy and Cell Death in L929 Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0094634

    Inhibition of ERK- or JNK- pathway blocks zVAD- but not TNF-induced cell death. ( A ) Inhibition of ERK- or JNK- pathway blocked zVAD-induced cell death. L929 cells were untreated or treated with ERK inhibitor PD98059 (100 µM), JNK inhibitor SP600125 (10 µM), p38 inhibitor SB203580 (10 µM), and PI3K inhibitor LY294002 (100 µM), respectively. Then the cells were treated with mock or zVAD (20 µM) for 24 h and cell viabilities were measured. ( B ) Inhibition of MAPKs does not block TNF-induced cell death. L929 cells were untreated or treated with PD98059 (100 µM), SP600125 (10 µM), p38 inhibitor SB203580 (10 µM), and LY294002 (100 µM). Then the cells were treated with mock or TNF (10 ng/ml) for 24 h and cell viabilities were measured. ( C ) zVAD had little effect on MAPKs’ activation. L929 cells were treated with zVAD or zVAD+LY294002 for 0, 0.5, 1, 2, 4 h, respectively. Cell lysates were subjected to western blot analysis with antibodies against p-ERK, ERK, p-JNK, JNK, p-p38 and p38. ( D ) Inhibition of zVAD-induced cell death has no effect on MAPKs’ activation. L929 cells were treated with zVAD or zVAD+Nec-1 for 0, 0.5, 1, 2, 4, 6 h, respectively. Cell lysates were subjected to western blot analysis with the indicated antibodies. ( E ) Inhibitors of MAPKs did not affect zVAD-induced LC3 modification. L929 cells were untreated or treated with PD98059 (100 µM), SP600125 (10 µM), SB203580 (10 µM), or LY294002 (100 µM). Then the cells were treated with mock or zVAD (20 µM) for 12 h and LC3 were analyzed by western blot. ( F ) Hypothetical pathway network of zVAD-induced cell death. The main pathways of zVAD-induced cell death are autophagy and autocrine of TNF. The induction of TNF by zVAD may depend on the collective effect of a number of pathways such as ERK, JNK, and autophagy. Mechanisms of zVAD-induced L929 cells could be different due to the variation of L929 sublines. **, p
    Figure Legend Snippet: Inhibition of ERK- or JNK- pathway blocks zVAD- but not TNF-induced cell death. ( A ) Inhibition of ERK- or JNK- pathway blocked zVAD-induced cell death. L929 cells were untreated or treated with ERK inhibitor PD98059 (100 µM), JNK inhibitor SP600125 (10 µM), p38 inhibitor SB203580 (10 µM), and PI3K inhibitor LY294002 (100 µM), respectively. Then the cells were treated with mock or zVAD (20 µM) for 24 h and cell viabilities were measured. ( B ) Inhibition of MAPKs does not block TNF-induced cell death. L929 cells were untreated or treated with PD98059 (100 µM), SP600125 (10 µM), p38 inhibitor SB203580 (10 µM), and LY294002 (100 µM). Then the cells were treated with mock or TNF (10 ng/ml) for 24 h and cell viabilities were measured. ( C ) zVAD had little effect on MAPKs’ activation. L929 cells were treated with zVAD or zVAD+LY294002 for 0, 0.5, 1, 2, 4 h, respectively. Cell lysates were subjected to western blot analysis with antibodies against p-ERK, ERK, p-JNK, JNK, p-p38 and p38. ( D ) Inhibition of zVAD-induced cell death has no effect on MAPKs’ activation. L929 cells were treated with zVAD or zVAD+Nec-1 for 0, 0.5, 1, 2, 4, 6 h, respectively. Cell lysates were subjected to western blot analysis with the indicated antibodies. ( E ) Inhibitors of MAPKs did not affect zVAD-induced LC3 modification. L929 cells were untreated or treated with PD98059 (100 µM), SP600125 (10 µM), SB203580 (10 µM), or LY294002 (100 µM). Then the cells were treated with mock or zVAD (20 µM) for 12 h and LC3 were analyzed by western blot. ( F ) Hypothetical pathway network of zVAD-induced cell death. The main pathways of zVAD-induced cell death are autophagy and autocrine of TNF. The induction of TNF by zVAD may depend on the collective effect of a number of pathways such as ERK, JNK, and autophagy. Mechanisms of zVAD-induced L929 cells could be different due to the variation of L929 sublines. **, p

    Techniques Used: Inhibition, Blocking Assay, Activation Assay, Western Blot, Modification

    13) Product Images from "Curcumin eliminates the inhibitory effect of advanced glycation end-products (AGEs) on gene expression of AGE receptor-1 in hepatic stellate cells in vitro"

    Article Title: Curcumin eliminates the inhibitory effect of advanced glycation end-products (AGEs) on gene expression of AGE receptor-1 in hepatic stellate cells in vitro

    Journal: Laboratory Investigation; a Journal of Technical Methods and Pathology

    doi: 10.1038/labinvest.2012.53

    The inhibition of ERK activity diminished the effect of AGEs and induced gene expression of AGE-R1 in cultured HSCs ( A B ) Serum-starved HSCs were treated with AGEs at indicated doses in serum-depleted media for 30 minutes with or without the pretreatment with curcumin (0–30 μM) for 1 hr. Whole cell extracts were prepared for analyzing levels of phosphorylated ERK by Western blotting analyses. Total ERK was used as an internal control for equal loading. Italic numbers beneath blots were fold changes (mean ± s. d., n=3) in the densities of the bands compared with the control without treatment in the blot, after normalization with the internal invariable control. Representatives were from three independent experiments. ( C D ) Serum-starved HSCs were pretreated with or without the selective ERK inhibitor PD98059 (0–20 μM) or curcumin (20 μM) for 1 hr prior to the exposure to AGEs (100 μg/ml) for additional 24 hr. Total RNA and whole cell extracts were prepared from the cells. ( C ) real-time PCR assays. Values were presented as mRNA fold changes (mean ± s. d., n=3). * p
    Figure Legend Snippet: The inhibition of ERK activity diminished the effect of AGEs and induced gene expression of AGE-R1 in cultured HSCs ( A B ) Serum-starved HSCs were treated with AGEs at indicated doses in serum-depleted media for 30 minutes with or without the pretreatment with curcumin (0–30 μM) for 1 hr. Whole cell extracts were prepared for analyzing levels of phosphorylated ERK by Western blotting analyses. Total ERK was used as an internal control for equal loading. Italic numbers beneath blots were fold changes (mean ± s. d., n=3) in the densities of the bands compared with the control without treatment in the blot, after normalization with the internal invariable control. Representatives were from three independent experiments. ( C D ) Serum-starved HSCs were pretreated with or without the selective ERK inhibitor PD98059 (0–20 μM) or curcumin (20 μM) for 1 hr prior to the exposure to AGEs (100 μg/ml) for additional 24 hr. Total RNA and whole cell extracts were prepared from the cells. ( C ) real-time PCR assays. Values were presented as mRNA fold changes (mean ± s. d., n=3). * p

    Techniques Used: Inhibition, Activity Assay, Expressing, Cell Culture, Western Blot, Real-time Polymerase Chain Reaction

    14) Product Images from "Brain-Derived Neurotrophic Factor Ameliorates Learning Deficits in a Rat Model of Alzheimer's Disease Induced by Aβ1-42"

    Article Title: Brain-Derived Neurotrophic Factor Ameliorates Learning Deficits in a Rat Model of Alzheimer's Disease Induced by Aβ1-42

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0122415

    Effect of intra-hippocampal injections of BDNF, ERK activator ceramide C6 and the ERK inhibitor PD98059 on spatial learning function in the rat model of Alzheimer's disease. (A) Representative swim traces of each group in the fifth training trial. (B) Escape latency and (C) swimming speed in each training trial were also analyzed. (D) The time spent in the target quadrant in the probe task. (E) The number of times crossing the platform in the probe task. (F) The total distance traveled in the open field test after the probe task. n = 8 each group. For panel B, * P
    Figure Legend Snippet: Effect of intra-hippocampal injections of BDNF, ERK activator ceramide C6 and the ERK inhibitor PD98059 on spatial learning function in the rat model of Alzheimer's disease. (A) Representative swim traces of each group in the fifth training trial. (B) Escape latency and (C) swimming speed in each training trial were also analyzed. (D) The time spent in the target quadrant in the probe task. (E) The number of times crossing the platform in the probe task. (F) The total distance traveled in the open field test after the probe task. n = 8 each group. For panel B, * P

    Techniques Used:

    15) Product Images from "Role of cocaine- and amphetamine-regulated transcript in estradiol-mediated neuroprotection"

    Article Title: Role of cocaine- and amphetamine-regulated transcript in estradiol-mediated neuroprotection

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

    doi: 10.1073/pnas.0602932103

    Mechanisms of neuroprotection by CART and regulation by estradiol. ( A ) Estradiol increases CREB binding to CART promoter DNA. EMSA in CART promoter DNA after incubation with brain nuclear extract at 3 h after MCAO (lane 1) was similar to that of a CRE sequence (+), eliminated by mutating the CRE site (−), and supershifted with an antibody against CREB (+ CREB AB, lanes 2–5), but not STAT3 (lane 6). The shift was stronger in estradiol-treated (lanes 3 and 5) compared with untreated animals (lanes 2 and 4). ( B ) CART increases the phosphorylation of ERK1/2 ( p -ERK) in primary cortical neurons. ERK activation by CART (0.2 nM) starts at 5 min (5′) after application, and it continues for at least 30 min (30′). Baseline (PD) and CART-induced (P+C) ERK phosphorylations were inhibited by MAPK inhibitor PD98059 (5 μM) and stimulated by FBS.
    Figure Legend Snippet: Mechanisms of neuroprotection by CART and regulation by estradiol. ( A ) Estradiol increases CREB binding to CART promoter DNA. EMSA in CART promoter DNA after incubation with brain nuclear extract at 3 h after MCAO (lane 1) was similar to that of a CRE sequence (+), eliminated by mutating the CRE site (−), and supershifted with an antibody against CREB (+ CREB AB, lanes 2–5), but not STAT3 (lane 6). The shift was stronger in estradiol-treated (lanes 3 and 5) compared with untreated animals (lanes 2 and 4). ( B ) CART increases the phosphorylation of ERK1/2 ( p -ERK) in primary cortical neurons. ERK activation by CART (0.2 nM) starts at 5 min (5′) after application, and it continues for at least 30 min (30′). Baseline (PD) and CART-induced (P+C) ERK phosphorylations were inhibited by MAPK inhibitor PD98059 (5 μM) and stimulated by FBS.

    Techniques Used: Binding Assay, Incubation, Sequencing, Activation Assay

    16) Product Images from "Calcitonin gene-related peptide protects rats from cerebral ischemia/reperfusion injury via a mechanism of action in the MAPK pathway"

    Article Title: Calcitonin gene-related peptide protects rats from cerebral ischemia/reperfusion injury via a mechanism of action in the MAPK pathway

    Journal: Biomedical Reports

    doi: 10.3892/br.2016.658

    Western blotting results of p-ERK/ERK in all the treatment groups. Compared to the MCAO group, the p-ERK expression level significantly increased in the brain tissues in the MCAO+CGRP group; whereas no significant change in the ERK expression was identified. Compared to the MCAO+CGRP group, the expression level of the p-ERK significantly decreased in the MCAO+CGRP+CGRP8–37, MCAO+CGRP+PD98059 and MCAO+CGRP+SB203580 groups; the largest reduction was evident in the MCAO+CGRP+PD98059 group, whereas no significant change in the expression level of the ERK protein was observed. The comparison between groups was considered to indicate significant differences, *P
    Figure Legend Snippet: Western blotting results of p-ERK/ERK in all the treatment groups. Compared to the MCAO group, the p-ERK expression level significantly increased in the brain tissues in the MCAO+CGRP group; whereas no significant change in the ERK expression was identified. Compared to the MCAO+CGRP group, the expression level of the p-ERK significantly decreased in the MCAO+CGRP+CGRP8–37, MCAO+CGRP+PD98059 and MCAO+CGRP+SB203580 groups; the largest reduction was evident in the MCAO+CGRP+PD98059 group, whereas no significant change in the expression level of the ERK protein was observed. The comparison between groups was considered to indicate significant differences, *P

    Techniques Used: Western Blot, Expressing

    17) Product Images from "Eya2 overexpression promotes the invasion of human astrocytoma through the regulation of ERK/MMP9 signaling"

    Article Title: Eya2 overexpression promotes the invasion of human astrocytoma through the regulation of ERK/MMP9 signaling

    Journal: International Journal of Molecular Medicine

    doi: 10.3892/ijmm.2017.3132

    Eyes absent (Eya) 2 interacts with Six1 and regulates ERK signaling. (A) ERK inhibitor, PD98059, blocked the promoting effect of Eya2 on A172 invasion. * P
    Figure Legend Snippet: Eyes absent (Eya) 2 interacts with Six1 and regulates ERK signaling. (A) ERK inhibitor, PD98059, blocked the promoting effect of Eya2 on A172 invasion. * P

    Techniques Used:

    18) Product Images from "The role of Lutheran/basal cell adhesion molecule in human bladder carcinogenesis"

    Article Title: The role of Lutheran/basal cell adhesion molecule in human bladder carcinogenesis

    Journal: Journal of Biomedical Science

    doi: 10.1186/s12929-017-0360-x

    The role of Erk phosphorylation in Lu/BCAM-laminin-related Rac/Rho activity, F-actin arrangement and adhesion of NIH-Lu 11 cells. ( A ) Phosphorylation of Erk in NIH-Lu11 cells after laminin treatment for different time periods were investigated using Western blotting. ( B ) The phosphorylation of Erk was evaluated after pretreatment with MEK1/2 inhibitor PD98059 for 1 h at various dosages. ( C ) F-actin distribution in NIH-Lu11 cells with or without laminin and in the presence or absence of PD98059 was labeled with Alexa Fluor™ 488-conjugated phalloidin. a : Cells without any treatment; b : Cells treated with laminin (0.2 μg/ml); c : Cells treated with laminin (0.2 μg/ml) and PD98059 (50 μM) Arrow : polymeric F-actin. ( D ) The quantitative data of ( C ) showed those cells with scattering F-actin distribution. ( E ) NIH-Lu11 cells were pretreated with PD98059 at various dosages in the presence of laminin. Activities of RhoA and Rac-1 were evaluated by GST-C21 and GST-PAK pull-down assay, respectively, followed by Western blotting. ( F ) The adhesion ability of NIH-Lu11 cells was evaluated by pretreating cells with PD98059 for 1 h followed by plating cells on 96-well plates pre-coated with laminin 10/11 or BSA. The adhesion ability of NIH-Lu11 cells was then measured. This experiment was repeated three times. *: p
    Figure Legend Snippet: The role of Erk phosphorylation in Lu/BCAM-laminin-related Rac/Rho activity, F-actin arrangement and adhesion of NIH-Lu 11 cells. ( A ) Phosphorylation of Erk in NIH-Lu11 cells after laminin treatment for different time periods were investigated using Western blotting. ( B ) The phosphorylation of Erk was evaluated after pretreatment with MEK1/2 inhibitor PD98059 for 1 h at various dosages. ( C ) F-actin distribution in NIH-Lu11 cells with or without laminin and in the presence or absence of PD98059 was labeled with Alexa Fluor™ 488-conjugated phalloidin. a : Cells without any treatment; b : Cells treated with laminin (0.2 μg/ml); c : Cells treated with laminin (0.2 μg/ml) and PD98059 (50 μM) Arrow : polymeric F-actin. ( D ) The quantitative data of ( C ) showed those cells with scattering F-actin distribution. ( E ) NIH-Lu11 cells were pretreated with PD98059 at various dosages in the presence of laminin. Activities of RhoA and Rac-1 were evaluated by GST-C21 and GST-PAK pull-down assay, respectively, followed by Western blotting. ( F ) The adhesion ability of NIH-Lu11 cells was evaluated by pretreating cells with PD98059 for 1 h followed by plating cells on 96-well plates pre-coated with laminin 10/11 or BSA. The adhesion ability of NIH-Lu11 cells was then measured. This experiment was repeated three times. *: p

    Techniques Used: Activity Assay, Western Blot, Labeling, Pull Down Assay

    19) Product Images from "Aberrant expression of NKL homeobox genes HMX2 and HMX3 interferes with cell differentiation in acute myeloid leukemia"

    Article Title: Aberrant expression of NKL homeobox genes HMX2 and HMX3 interferes with cell differentiation in acute myeloid leukemia

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0240120

    Regulation of HMX2 and HMX3 by KMT2A and ERK-signalling. (A) RQ-PCR analysis of EOL-1 (left) and MV4-11 (middle) treated for siRNA-mediated knockdown of KMT2A demonstrates raised expression levels of HMX2 and HMX3, indicating a repressive impact of KMT2A. This treatment resulted in enhanced expression of HMX3 in HL-60 cells which did not express HMX2 (right). Asterisks indicate calculated p-values obtained by t-Test analysis of controls (siCTR) and siRNA-targeted knockdown. (B) RQ-PCR analysis of KMT2A of EOL-1 cells treated for siRNA-mediated knockdown of HMX2 (left) and HMX3 (right) showed unaltered KMT2A expression levels, discounting any regulatory impact. (C) Quantification of KMT2A transcripts in AML cell lines and primary granulocytes showed low expression levels in EOL-1, MV4-11 and in eosinophils. (D) RQ-PCR analysis of HMX2 showed elevated expression levels in EOL-1 cells treated with PDGFRA-inhibitor dasatinib. Asterisks indicate calculated p-values obtained by t-Test analysis of controls (DMSO) and pharmacological treatments. (E) Treatment of EOL-1 cells with ERK-inhbitor PD98059 resulted in reduced levels of phospho-ERK as analyzed by Western blot (left), and in elevated transcript levels of HMX2 (middle) and HMX3 (right) as analyzed by RQ-PCR. (F) Treatment of EOL-1 cells with ERK-activator FLT3LG resulted in elevated levels of phosphorylated ERK (above) and in reduced transcript levels of HMX2 and HMX3 (below).
    Figure Legend Snippet: Regulation of HMX2 and HMX3 by KMT2A and ERK-signalling. (A) RQ-PCR analysis of EOL-1 (left) and MV4-11 (middle) treated for siRNA-mediated knockdown of KMT2A demonstrates raised expression levels of HMX2 and HMX3, indicating a repressive impact of KMT2A. This treatment resulted in enhanced expression of HMX3 in HL-60 cells which did not express HMX2 (right). Asterisks indicate calculated p-values obtained by t-Test analysis of controls (siCTR) and siRNA-targeted knockdown. (B) RQ-PCR analysis of KMT2A of EOL-1 cells treated for siRNA-mediated knockdown of HMX2 (left) and HMX3 (right) showed unaltered KMT2A expression levels, discounting any regulatory impact. (C) Quantification of KMT2A transcripts in AML cell lines and primary granulocytes showed low expression levels in EOL-1, MV4-11 and in eosinophils. (D) RQ-PCR analysis of HMX2 showed elevated expression levels in EOL-1 cells treated with PDGFRA-inhibitor dasatinib. Asterisks indicate calculated p-values obtained by t-Test analysis of controls (DMSO) and pharmacological treatments. (E) Treatment of EOL-1 cells with ERK-inhbitor PD98059 resulted in reduced levels of phospho-ERK as analyzed by Western blot (left), and in elevated transcript levels of HMX2 (middle) and HMX3 (right) as analyzed by RQ-PCR. (F) Treatment of EOL-1 cells with ERK-activator FLT3LG resulted in elevated levels of phosphorylated ERK (above) and in reduced transcript levels of HMX2 and HMX3 (below).

    Techniques Used: Polymerase Chain Reaction, Expressing, Western Blot

    20) Product Images from "Apigenin-induced apoptosis of leukemia cells is mediated by a bimodal and differentially regulated residue-specific phosphorylation of heat-shock protein-27"

    Article Title: Apigenin-induced apoptosis of leukemia cells is mediated by a bimodal and differentially regulated residue-specific phosphorylation of heat-shock protein-27

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2010.41

    Apigenin-induced ‘late' Hsp27 phosphorylation is ERK-independent. Lysates from THP-1 cells were treated with diluent (lane 1), or pretreated with diluent or 25 μ M PD98059 before the addition of 50 μ M apigenin for 6 h (lanes 2 and 3, respectively) and immunoblotted with anti-phospho-Hsp27-pS78, anti-phospho-Hsp27-pS82, anti-phospho-Hsp27-pS15, anti-phospho-ERK, anti-total-Hsp27, anti-total-ERK antibodies. The same membrane was immunoblotted with anti- β -Tubulin antibodies as loading control. Results are a representative of four independent experiments
    Figure Legend Snippet: Apigenin-induced ‘late' Hsp27 phosphorylation is ERK-independent. Lysates from THP-1 cells were treated with diluent (lane 1), or pretreated with diluent or 25 μ M PD98059 before the addition of 50 μ M apigenin for 6 h (lanes 2 and 3, respectively) and immunoblotted with anti-phospho-Hsp27-pS78, anti-phospho-Hsp27-pS82, anti-phospho-Hsp27-pS15, anti-phospho-ERK, anti-total-Hsp27, anti-total-ERK antibodies. The same membrane was immunoblotted with anti- β -Tubulin antibodies as loading control. Results are a representative of four independent experiments

    Techniques Used:

    21) Product Images from "HAb18G/CD147 cell-cell contacts confer resistance of a HEK293 subpopulation to anoikis in an E-cadherin-dependent manner"

    Article Title: HAb18G/CD147 cell-cell contacts confer resistance of a HEK293 subpopulation to anoikis in an E-cadherin-dependent manner

    Journal: BMC Cell Biology

    doi: 10.1186/1471-2121-11-27

    The suppression of anoikis in HEK293ar mediated by cell-cell contacts involves the PI3K/Akt pathway . A . The effect of the PI3K (phosphoinositide 3-kinase) inhibitor LY294002 (20, 50 μmol/l) or the ERK (extracellular signal-regulated kinase) inhibitor PD98059 (20, 50 μmol/l) on cell-cell contacts formation (n = 4-10). Magnification: × 200. B . The effect of signal pathway inhibitors treatment on the degree of cell aggregation (n = 4-10). The cells were counted in 4-10 independent sections (at least 300 nuclei/section). C . The effect of signal pathway inhibition on the survival of cells in suspension. The anoikis was determined with TUNEL assay kit. The apoptotic nuclei were counted in 4-10 independent sections (at least 500 nuclei/section). The concentration of both LY294002 (PI3K inhibitor) and PD98059 (ERK inhibitor) is 50 μmol/l. Magnification: ×200. D . The effect of signal pathway inhibitors LY294002 (0, 20, 50 μmol/l) or PD98059 (0, 20, 50 μmol/l) on cell number. It was evaluated with a CyQUANT ® NF Cell Proliferation Assay Kit (C35006, Invitrogen, Ltd) according to the manufacturer's protocol for the nonadherent cells. ** p
    Figure Legend Snippet: The suppression of anoikis in HEK293ar mediated by cell-cell contacts involves the PI3K/Akt pathway . A . The effect of the PI3K (phosphoinositide 3-kinase) inhibitor LY294002 (20, 50 μmol/l) or the ERK (extracellular signal-regulated kinase) inhibitor PD98059 (20, 50 μmol/l) on cell-cell contacts formation (n = 4-10). Magnification: × 200. B . The effect of signal pathway inhibitors treatment on the degree of cell aggregation (n = 4-10). The cells were counted in 4-10 independent sections (at least 300 nuclei/section). C . The effect of signal pathway inhibition on the survival of cells in suspension. The anoikis was determined with TUNEL assay kit. The apoptotic nuclei were counted in 4-10 independent sections (at least 500 nuclei/section). The concentration of both LY294002 (PI3K inhibitor) and PD98059 (ERK inhibitor) is 50 μmol/l. Magnification: ×200. D . The effect of signal pathway inhibitors LY294002 (0, 20, 50 μmol/l) or PD98059 (0, 20, 50 μmol/l) on cell number. It was evaluated with a CyQUANT ® NF Cell Proliferation Assay Kit (C35006, Invitrogen, Ltd) according to the manufacturer's protocol for the nonadherent cells. ** p

    Techniques Used: Inhibition, TUNEL Assay, Concentration Assay, CyQUANT Assay, Proliferation Assay

    22) Product Images from "A Novel Tumor Suppressor Function of Glycine N-Methyltransferase Is Independent of Its Catalytic Activity but Requires Nuclear Localization"

    Article Title: A Novel Tumor Suppressor Function of Glycine N-Methyltransferase Is Independent of Its Catalytic Activity but Requires Nuclear Localization

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0070062

    Cellular responses to GNMT expression. A. Distribution of GNMT-expressing cells ( right panel ) between cell cycle phases (propidium iodide staining) compared to control ( left panel ) GNMT-deficient cells. B . Assessment of DNA damage in GNMT expressing cells by the Comet assay. C . Apoptotic cells assessed by Annexin V/propidium iodide staining after GNMT expression ( bottom right quadrant , early apoptotic cells; upper right quadrant , late apoptotic cells); only green cells (expressing GFP-GNMT) were evaluated. D . Calculation of apoptotic cells from C. E . Activation of ERK phosphorylation in response to GNMT expression. F . zVAD-fmk, but not ERK inhibitor PD98059, partially rescues cells from the antiproliferative effect of GNMT (data for A549 cells are shown).
    Figure Legend Snippet: Cellular responses to GNMT expression. A. Distribution of GNMT-expressing cells ( right panel ) between cell cycle phases (propidium iodide staining) compared to control ( left panel ) GNMT-deficient cells. B . Assessment of DNA damage in GNMT expressing cells by the Comet assay. C . Apoptotic cells assessed by Annexin V/propidium iodide staining after GNMT expression ( bottom right quadrant , early apoptotic cells; upper right quadrant , late apoptotic cells); only green cells (expressing GFP-GNMT) were evaluated. D . Calculation of apoptotic cells from C. E . Activation of ERK phosphorylation in response to GNMT expression. F . zVAD-fmk, but not ERK inhibitor PD98059, partially rescues cells from the antiproliferative effect of GNMT (data for A549 cells are shown).

    Techniques Used: Expressing, Staining, Single Cell Gel Electrophoresis, Activation Assay

    23) Product Images from "Ghrelin Attenuates the Osteoblastic Differentiation of Vascular Smooth Muscle Cells through the ERK Pathway"

    Article Title: Ghrelin Attenuates the Osteoblastic Differentiation of Vascular Smooth Muscle Cells through the ERK Pathway

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0033126

    ERK signaling pathway mediated the inhibitory effect of ghrelin on osteoblastic differentiation of calcifying vascular smooth muscle cells (CVSMCs). (A) The expression and silencing of growth hormone secretagog receptor (GHSR) on CVSMCs. Cells were incubated with scramble siRNA or GHSR siRNA for 72 h. Total cellular protein was subjected to western blot analysis using anti-GHSR antibody. The anti-GHSR antibody identified a band at 44 kDa. β-actin was used as the control. (B) The activation of extracellular signal-related kinase (ERK) under the silencing of GHSR. Cells were incubated with scramble siRNA or GHSR siRNA for 72 h prior to treatment with 10−6 mol/L ghrelin for 30 min. Total proteins were subjected to western blotting and incubated with antibody against p-ERK and ERK. The representative results are shown. (C) The activation of ERK under PD98059. Cells were incubated with PD98059 (10 µM) for 2 h prior to treatment with 10−6 mol/L of ghrelin for 30 min. Total proteins were subjected to western blotting and incubated with antibody against p-ERK and ERK. The representative results are shown. (D, E, F) The decreased alkaline phosphatase (ALP) activity, Runx2 mRNA, and calcium deposition mediated by the GHSR/ERK pathway. Cells were incubated with PD98059 (10 µM) for 2 h prior to treatment with 10−6 mol/L of ghrelin. Cells were also treated with the scramble siRNA or GHSR siRNA in the presence of 10−6 mol/L of ghrelin. ALP activity, Rnux2 mRNA, and calcium deposition were measured. The bars represent the mean ±standard deviation (SD) ( n = 3).
    Figure Legend Snippet: ERK signaling pathway mediated the inhibitory effect of ghrelin on osteoblastic differentiation of calcifying vascular smooth muscle cells (CVSMCs). (A) The expression and silencing of growth hormone secretagog receptor (GHSR) on CVSMCs. Cells were incubated with scramble siRNA or GHSR siRNA for 72 h. Total cellular protein was subjected to western blot analysis using anti-GHSR antibody. The anti-GHSR antibody identified a band at 44 kDa. β-actin was used as the control. (B) The activation of extracellular signal-related kinase (ERK) under the silencing of GHSR. Cells were incubated with scramble siRNA or GHSR siRNA for 72 h prior to treatment with 10−6 mol/L ghrelin for 30 min. Total proteins were subjected to western blotting and incubated with antibody against p-ERK and ERK. The representative results are shown. (C) The activation of ERK under PD98059. Cells were incubated with PD98059 (10 µM) for 2 h prior to treatment with 10−6 mol/L of ghrelin for 30 min. Total proteins were subjected to western blotting and incubated with antibody against p-ERK and ERK. The representative results are shown. (D, E, F) The decreased alkaline phosphatase (ALP) activity, Runx2 mRNA, and calcium deposition mediated by the GHSR/ERK pathway. Cells were incubated with PD98059 (10 µM) for 2 h prior to treatment with 10−6 mol/L of ghrelin. Cells were also treated with the scramble siRNA or GHSR siRNA in the presence of 10−6 mol/L of ghrelin. ALP activity, Rnux2 mRNA, and calcium deposition were measured. The bars represent the mean ±standard deviation (SD) ( n = 3).

    Techniques Used: Expressing, Incubation, Western Blot, Activation Assay, ALP Assay, Activity Assay, Standard Deviation

    24) Product Images from "NF-kB and ERK-signaling pathways contribute to the gene expression induced by cag PAI-positive-Helicobacter pylori infection"

    Article Title: NF-kB and ERK-signaling pathways contribute to the gene expression induced by cag PAI-positive-Helicobacter pylori infection

    Journal: World Journal of Gastroenterology : WJG

    doi: 10.3748/wjg.v11.i39.6134

    Schematic representation of the distribution of genes affected by wild-type H pylori infection. The complete upregulated genes at 3 h after infection is represented by the circle as a whole. The expression of 367 genes (65%) of the 566 genes upregulated by wild type H pylori was suppressed by pre-incubation with APDC, an inhibitor of NF-kB. On the other hand, pre-incubation with PD98059, an inhibitor of ERK, suppressed the expression of 429 genes (76%) of the 566 genes upregulated by wild type H pylori . Expression of 475 of the 566 genes (84%) was induced under NF-kB and/or ERK signaling activation, whereas changes in the remaining 16% are NF-kB or ERK signaling independent.
    Figure Legend Snippet: Schematic representation of the distribution of genes affected by wild-type H pylori infection. The complete upregulated genes at 3 h after infection is represented by the circle as a whole. The expression of 367 genes (65%) of the 566 genes upregulated by wild type H pylori was suppressed by pre-incubation with APDC, an inhibitor of NF-kB. On the other hand, pre-incubation with PD98059, an inhibitor of ERK, suppressed the expression of 429 genes (76%) of the 566 genes upregulated by wild type H pylori . Expression of 475 of the 566 genes (84%) was induced under NF-kB and/or ERK signaling activation, whereas changes in the remaining 16% are NF-kB or ERK signaling independent.

    Techniques Used: Infection, Expressing, Incubation, Activation Assay

    25) Product Images from "The Critical Role of Membrane Cholesterol in Salmonella-Induced Autophagy in Intestinal Epithelial Cells"

    Article Title: The Critical Role of Membrane Cholesterol in Salmonella-Induced Autophagy in Intestinal Epithelial Cells

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms150712558

    The role of ERK or Akt on the Beclin 1 and LC3II proteins expression in Salmonella -infected Caco-2 cells. Caco-2 cells were uninfected (Con) or infected by wild-type S . typhimurium strain SL1344 for indicated times, in the presence or absence of PD98059 (PD) or LY294002 (LY). Immunoblots were performed on whole cell lysates with antibody to detect Beclin 1 and LC3II expression, or GAPDH for normalization of proteins. Representative immunoblots of Beclin 1 and LC3II proteins expression in Salmonella -infected Caco-2 cells in the presence of PD ( A ) or LY ( B ) are shown.
    Figure Legend Snippet: The role of ERK or Akt on the Beclin 1 and LC3II proteins expression in Salmonella -infected Caco-2 cells. Caco-2 cells were uninfected (Con) or infected by wild-type S . typhimurium strain SL1344 for indicated times, in the presence or absence of PD98059 (PD) or LY294002 (LY). Immunoblots were performed on whole cell lysates with antibody to detect Beclin 1 and LC3II expression, or GAPDH for normalization of proteins. Representative immunoblots of Beclin 1 and LC3II proteins expression in Salmonella -infected Caco-2 cells in the presence of PD ( A ) or LY ( B ) are shown.

    Techniques Used: Expressing, Infection, Western Blot

    26) Product Images from "RASAL2 down-regulation in ovarian cancer promotes epithelial-mesenchymal transition and metastasis"

    Article Title: RASAL2 down-regulation in ovarian cancer promotes epithelial-mesenchymal transition and metastasis

    Journal: Oncotarget

    doi:

    Tumor suppressor role of RASAL2 is Ras-ERK pathway-dependent To explore the functional effects of the Ras-ERK pathway following RASAL2 depletion, SK-OV-3, OVCAR3 and A2780 cells infected with shRASAL2-1 or -2 shRNA were treated with either the ERK pathway inhibitor PD98059 (10 μg/μl) or DMSO. (A) Western blot analysis of p-ERK, E-cadherin and vimentin expression following ERK inhibition. (B) SK-OV-3 cells expressing shRASAL2-1 or-2 shRNA were treated with PD98059 (10 μg/μl) or DMSO. Then, an anchorage-independent growth assay was performed. The graph indicates the relative number of colonies ± SD (n = 3). (C) Cell migration or invasion assays were also conducted on RASAL2 knockdown SK-OV-3 cells treated with either PD98059 or DMSO. All the data were normalized to the results of cells transfected with scramble-shRNA. The data are shown as the means ± SD (n = 3). (D) Representative graphs of SK-OV-3 cells in migration or invasion assays. (E) Immunofluorescence assay for the expression of E-cadherin or vimentin in RASAL2 knockdown SK-OV-3 cells treated with either PD98059 or DMSO. *, P
    Figure Legend Snippet: Tumor suppressor role of RASAL2 is Ras-ERK pathway-dependent To explore the functional effects of the Ras-ERK pathway following RASAL2 depletion, SK-OV-3, OVCAR3 and A2780 cells infected with shRASAL2-1 or -2 shRNA were treated with either the ERK pathway inhibitor PD98059 (10 μg/μl) or DMSO. (A) Western blot analysis of p-ERK, E-cadherin and vimentin expression following ERK inhibition. (B) SK-OV-3 cells expressing shRASAL2-1 or-2 shRNA were treated with PD98059 (10 μg/μl) or DMSO. Then, an anchorage-independent growth assay was performed. The graph indicates the relative number of colonies ± SD (n = 3). (C) Cell migration or invasion assays were also conducted on RASAL2 knockdown SK-OV-3 cells treated with either PD98059 or DMSO. All the data were normalized to the results of cells transfected with scramble-shRNA. The data are shown as the means ± SD (n = 3). (D) Representative graphs of SK-OV-3 cells in migration or invasion assays. (E) Immunofluorescence assay for the expression of E-cadherin or vimentin in RASAL2 knockdown SK-OV-3 cells treated with either PD98059 or DMSO. *, P

    Techniques Used: Functional Assay, Infection, shRNA, Western Blot, Expressing, Inhibition, Growth Assay, Migration, Transfection, Immunofluorescence

    27) Product Images from "Interferon-α Enhances 5?-Deoxy-5-Fluorouridine-Induced Apoptosis by ERK-Dependant Upregulation of Thymidine Phosphorylase"

    Article Title: Interferon-α Enhances 5?-Deoxy-5-Fluorouridine-Induced Apoptosis by ERK-Dependant Upregulation of Thymidine Phosphorylase

    Journal: BioMed Research International

    doi: 10.1155/2013/132793

    IFN- α upregulated the expression of TP partially by promoting ERK activation in gastric cancer cells. (a) MGC803 cells were preincubated with 20 μ mol/L ERK inhibitor PD98059 for 1 h followed by treatment with 1000 IU/mL of IFN- α or the combination of 1000 IU/mL IFN- α and 250 μ g/mL 5′-DFUR. Western blot analysis of the activated levels of ERK and the expression of TP. Data were means ± SD of three independent experiments. *Pretreated with PD98059 before IFN- α alone or IFN- α +5′-DFUR versus that untreated with PD98059 before IFN- α alone or IFN- α + 5′-DFUR, respectively, P
    Figure Legend Snippet: IFN- α upregulated the expression of TP partially by promoting ERK activation in gastric cancer cells. (a) MGC803 cells were preincubated with 20 μ mol/L ERK inhibitor PD98059 for 1 h followed by treatment with 1000 IU/mL of IFN- α or the combination of 1000 IU/mL IFN- α and 250 μ g/mL 5′-DFUR. Western blot analysis of the activated levels of ERK and the expression of TP. Data were means ± SD of three independent experiments. *Pretreated with PD98059 before IFN- α alone or IFN- α +5′-DFUR versus that untreated with PD98059 before IFN- α alone or IFN- α + 5′-DFUR, respectively, P

    Techniques Used: Expressing, Activation Assay, Western Blot

    Related Articles

    other:

    Article Title: Tanshinone IIA inhibits AGEs-induced proliferation and migration of cultured vascular smooth muscle cells by suppressing ERK1/2 MAPK signaling
    Article Snippet: The ERK1/2 inhibitor (PD 98059), p38 inhibitor (SB203580) anc FITC-conjugated monoclonal anti-α-smooth muscle actin antibody were obtained from Sigma Chemical Company (St. Louis, MO, USA).

    Inhibition:

    Article Title: Trichomonas vaginalis Induces Production of Proinflammatory Cytokines in Mouse Macrophages Through Activation of MAPK and NF-κB Pathways Partially Mediated by TLR2
    Article Snippet: .. In the inhibition experiment, WT PMϕ were pretreated with specific inhibitor of p38 (SB203580; 30 μM), ERK (PD98059; 40 μM) (Sigma-Aldrich, United States) for 1 h at 37°C with 5% CO2 and the viability of the macrophages was determined by trypan blue method ( > 95%). .. Then the PMϕ were co-incubated with T. vaginalis in cell culture medium containing 2% FBS.

    Cell Culture:

    Article Title: Glucose Induces Mouse β-Cell Proliferation via IRS2, MTOR, and Cyclin D2 but Not the Insulin Receptor
    Article Snippet: .. For proliferation, dispersed mouse islet cells were cultured for 72 h, with BrdU included the last 24 h. Rapamycin (10 nmol/L; LC Laboratories), wortmannin (100 nmol/L; Sigma), PI-103 (100 nmol/L, Selleck Chemicals), PD98059 (10 μmol/L; Calbiochem), and kinetin riboside (15 μmol/L; Sigma) were added 30 min before stimulation; hydroxy-2-naphthalenylmethylphosphonic acid (HNMPA) (10 μmol/L; Santa Cruz Biotechnology) was added 1 h before stimulation; or S961 (100 nmol/L; Phoenix Pharmaceuticals) was added 2 h before stimulation. .. Adenovirus (Ad-shIRS2, Ad-Cre, Ad-CMV-GFP-Cyclin-D2, Ad-shCyclin-D2, and Ad-shIR; Vector Biolabs) was added the day after islet trypsinization; multiplicity of infection (MOI) is per figure legends.

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    Millipore p42 44 mitogen activated protein kinase extracellular signal regulated kinase mapk erk kinase
    Effects of pan protein kinase C (PKC) inhibitor bisindolylmaleimide I (BIM) and mitogen-activated protein kinase–extracellular-signal-regulated kinase <t>(MAPK-ERK)</t> kinase (MEK) inhibitor PD98059 on the gene expression of EGR1 (A) and various growth factors and cytokines (B–I) by qRT-PCR with Taqman primers and the phosphorylation of EGFR (J) , MAPK-ERK (K) , and c-Jun N-terminal kinase (JNK) (L) by Luminex ® xMAP ® technology-based immunoassay. MSCs were stimulated with 10 nM EGF in the presence of DMSO (vehicle), BIM (5 μM), and PD98059 (10 μM) for 1 h (A–I) or an indicated time (J–L) , and total RNA (A–I) or protein (J–L) was harvested for further analysis [* P
    P42 44 Mitogen Activated Protein Kinase Extracellular Signal Regulated Kinase Mapk Erk Kinase, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 879 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Effects of pan protein kinase C (PKC) inhibitor bisindolylmaleimide I (BIM) and mitogen-activated protein kinase–extracellular-signal-regulated kinase (MAPK-ERK) kinase (MEK) inhibitor PD98059 on the gene expression of EGR1 (A) and various growth factors and cytokines (B–I) by qRT-PCR with Taqman primers and the phosphorylation of EGFR (J) , MAPK-ERK (K) , and c-Jun N-terminal kinase (JNK) (L) by Luminex ® xMAP ® technology-based immunoassay. MSCs were stimulated with 10 nM EGF in the presence of DMSO (vehicle), BIM (5 μM), and PD98059 (10 μM) for 1 h (A–I) or an indicated time (J–L) , and total RNA (A–I) or protein (J–L) was harvested for further analysis [* P

    Journal: Stem Cells and Development

    Article Title: EGFR Ligands Drive Multipotential Stromal Cells to Produce Multiple Growth Factors and Cytokines via Early Growth Response-1

    doi: 10.1089/scd.2011.0711

    Figure Lengend Snippet: Effects of pan protein kinase C (PKC) inhibitor bisindolylmaleimide I (BIM) and mitogen-activated protein kinase–extracellular-signal-regulated kinase (MAPK-ERK) kinase (MEK) inhibitor PD98059 on the gene expression of EGR1 (A) and various growth factors and cytokines (B–I) by qRT-PCR with Taqman primers and the phosphorylation of EGFR (J) , MAPK-ERK (K) , and c-Jun N-terminal kinase (JNK) (L) by Luminex ® xMAP ® technology-based immunoassay. MSCs were stimulated with 10 nM EGF in the presence of DMSO (vehicle), BIM (5 μM), and PD98059 (10 μM) for 1 h (A–I) or an indicated time (J–L) , and total RNA (A–I) or protein (J–L) was harvested for further analysis [* P

    Article Snippet: P42/44 mitogen-activated protein kinase–extracellular-signal-regulated kinase (MAPK-ERK) kinase (MEK) inhibitor PD98059 was from EMD Biosciences.

    Techniques: Expressing, Quantitative RT-PCR, Luminex

    The effect of various inhibitors on TGF-β and/ or TNF –α induced PAI-1 mRNA expression in a human granulosa cell line (HGrC1) (Fig. 3-a) HGrC1 cells were stimulated with TGF-β (1 ng/ml) or TNF-α (5 ng/ml) for 24 hrs. MAPK inhibitors, PD98059 (ERK inhibitor 25μM), SB202190 (p38MAPK inhibitor, 10μM), and SP600125 (JNK inhibitor, 10 μM) and SB431542, (inhibitor of activin receptor-like kinase (ALK)-5, 10 μM) were added 1hr before the treatment with TGF-β or TNF-α. (Fig. 3-b) HGrC1 cells were stimulated with TGF-β (1 ng/ml) and TNF-α (5 ng/ml) for 24 hrs. SB202190 (p38MAPK inhibitor, 10 μM) and/ or SB431542 (ALK-5 inhibitor, 10μM) were added 1hr before the treatment with TGF-β and TNF-α. Total RNA was extracted from the cells and subjected to real-time PCR to determine the PAI-1 mRNA levels. Data were normalized by GAPDH mRNA levels to show the relative abundance. Representative data from three different experiments were shown as the mean ± S.E.M relative to an adjusted value of 1.0 for the mean value of the control. *: P

    Journal: American journal of reproductive immunology (New York, N.Y. : 1989)

    Article Title: PAI-1 in granulosa cells is suppressed directly by statin and indirectly by suppressing TGF-β and TNF-α in mononuclear cells by insulin sensitizing drugs

    doi: 10.1111/aji.12669

    Figure Lengend Snippet: The effect of various inhibitors on TGF-β and/ or TNF –α induced PAI-1 mRNA expression in a human granulosa cell line (HGrC1) (Fig. 3-a) HGrC1 cells were stimulated with TGF-β (1 ng/ml) or TNF-α (5 ng/ml) for 24 hrs. MAPK inhibitors, PD98059 (ERK inhibitor 25μM), SB202190 (p38MAPK inhibitor, 10μM), and SP600125 (JNK inhibitor, 10 μM) and SB431542, (inhibitor of activin receptor-like kinase (ALK)-5, 10 μM) were added 1hr before the treatment with TGF-β or TNF-α. (Fig. 3-b) HGrC1 cells were stimulated with TGF-β (1 ng/ml) and TNF-α (5 ng/ml) for 24 hrs. SB202190 (p38MAPK inhibitor, 10 μM) and/ or SB431542 (ALK-5 inhibitor, 10μM) were added 1hr before the treatment with TGF-β and TNF-α. Total RNA was extracted from the cells and subjected to real-time PCR to determine the PAI-1 mRNA levels. Data were normalized by GAPDH mRNA levels to show the relative abundance. Representative data from three different experiments were shown as the mean ± S.E.M relative to an adjusted value of 1.0 for the mean value of the control. *: P

    Article Snippet: In some experiments, MAPK inhibitors, PD98059 (ERK inhibitor, 25μM, Calbiochem, San Diego, CA), SB202190 (p38MAPK inhibitor, 10μM, Calbiochem), and SP600125 (JNK inhibitor, 10μM, Calbiochem) and SB431542, (inhibitor of activin receptor-like kinase (ALK)-5, 10μM, Calbiochem) and simvastatin (up to 5 μM) were added 1hr before the treatment with TGF-β and/ or TNF-α

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    BMP-specific transactivation is improved with RAS/ERK inhibition. The BRE-Luc construct was used with and without pharmacologic inhibition of RAS/ERK with (A) PD98059 (5 μM) or after transfection with (B) DN KRAS. Cells were treated with 100 ng/mL

    Journal:

    Article Title: BMP-induced growth suppression in colon cancer cells is mediated by p21WAF1 stabilization and modulated by RAS/ERK

    doi: 10.1016/j.cellsig.2007.01.017

    Figure Lengend Snippet: BMP-specific transactivation is improved with RAS/ERK inhibition. The BRE-Luc construct was used with and without pharmacologic inhibition of RAS/ERK with (A) PD98059 (5 μM) or after transfection with (B) DN KRAS. Cells were treated with 100 ng/mL

    Article Snippet: In some assays, cells were pre-treated with PD98059 (an ERK inhibitor; Calbiochem, San Diego, CA) at a concentration of 5 μM for 30 min prior to 100 ng/ml of BMP2 treatment (R and D Systems, Minneapolis, MN).

    Techniques: Inhibition, Construct, Transfection

    Inhibition of RAS/ERK improves BMP2-induced growth suppression. Cells were treated with 100 ng/mL of BMP2 with or without PD98059 (5 μM) where indicated every 2 days, and cells were counted. Results are expressed as percent change in growth with

    Journal:

    Article Title: BMP-induced growth suppression in colon cancer cells is mediated by p21WAF1 stabilization and modulated by RAS/ERK

    doi: 10.1016/j.cellsig.2007.01.017

    Figure Lengend Snippet: Inhibition of RAS/ERK improves BMP2-induced growth suppression. Cells were treated with 100 ng/mL of BMP2 with or without PD98059 (5 μM) where indicated every 2 days, and cells were counted. Results are expressed as percent change in growth with

    Article Snippet: In some assays, cells were pre-treated with PD98059 (an ERK inhibitor; Calbiochem, San Diego, CA) at a concentration of 5 μM for 30 min prior to 100 ng/ml of BMP2 treatment (R and D Systems, Minneapolis, MN).

    Techniques: Inhibition

    BMP2 induces ERK activation above constitutively active levels, and RAS/ERK inhibition blocks both stimuli for ERK activation. Cells were treated with 100 ng/mL of BMP2 with or without PD98059 (5 μM) where indicated for up to 2 h, followed by

    Journal:

    Article Title: BMP-induced growth suppression in colon cancer cells is mediated by p21WAF1 stabilization and modulated by RAS/ERK

    doi: 10.1016/j.cellsig.2007.01.017

    Figure Lengend Snippet: BMP2 induces ERK activation above constitutively active levels, and RAS/ERK inhibition blocks both stimuli for ERK activation. Cells were treated with 100 ng/mL of BMP2 with or without PD98059 (5 μM) where indicated for up to 2 h, followed by

    Article Snippet: In some assays, cells were pre-treated with PD98059 (an ERK inhibitor; Calbiochem, San Diego, CA) at a concentration of 5 μM for 30 min prior to 100 ng/ml of BMP2 treatment (R and D Systems, Minneapolis, MN).

    Techniques: Activation Assay, Inhibition

    Effect of MAPK and NF-κB inhibitors on LPS-induced expression of pro-inflammatory mediators. Cells were pretreated with a specified concentration of theaflavin (50 µg/ml), PD98059 (ERK inhibitor; 20 µM), SP600125 (JNK inhibitor; 20 µM), SB203580 (p38 inhibitor; 20 µM), or Bay11-7082 (NF-κB inhibitor; 5 µM) and then stimulated with LPS (1 µg/ml) for the times indicated. Pretreatment with Bay11-7082 (A) markedly inhibited the LPS-induced expression of pro-inflammatory mediators, whereas pretreatment with either SB203580 or SP600125 had an inhibitory effect on the LPS-induced expression of IL-6, ICAM-1, or MCP-1, respectively (B).

    Journal: Chonnam Medical Journal

    Article Title: Theaflavin Inhibits LPS-Induced IL-6, MCP-1, and ICAM-1 Expression in Bone Marrow-Derived Macrophages Through the Blockade of NF-?B and MAPK Signaling Pathways

    doi: 10.4068/cmj.2011.47.2.104

    Figure Lengend Snippet: Effect of MAPK and NF-κB inhibitors on LPS-induced expression of pro-inflammatory mediators. Cells were pretreated with a specified concentration of theaflavin (50 µg/ml), PD98059 (ERK inhibitor; 20 µM), SP600125 (JNK inhibitor; 20 µM), SB203580 (p38 inhibitor; 20 µM), or Bay11-7082 (NF-κB inhibitor; 5 µM) and then stimulated with LPS (1 µg/ml) for the times indicated. Pretreatment with Bay11-7082 (A) markedly inhibited the LPS-induced expression of pro-inflammatory mediators, whereas pretreatment with either SB203580 or SP600125 had an inhibitory effect on the LPS-induced expression of IL-6, ICAM-1, or MCP-1, respectively (B).

    Article Snippet: PD98059 (extracellular signal-regulated kinase [ERK] inhibitor), SP600125 (c-Jun-N-terminal kinase [JNK] inhibitor), SB203580 (p38 MAPK inhibitor), and Bay11-7082 (NF-κB inhibitor) were purchased from Calbiochem (San Diego, CA, USA).

    Techniques: Expressing, Concentration Assay