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  • 99
    Vector Laboratories immedge hydrophobic barrier pen
    Immedge Hydrophobic Barrier Pen, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 123 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immedge hydrophobic barrier pen/product/Vector Laboratories
    Average 99 stars, based on 123 article reviews
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    94
    Thermo Fisher pap pen
    Pap Pen, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 277 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 277 article reviews
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    pap pen - by Bioz Stars, 2020-11
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    91
    Hologic Inc thinprep pap test
    Frequency of false-positive tests for ⩾CIN2 (samples with abnormal cytology that were not followed by a histological diagnosis of ⩾CIN2), by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: <t>ThinPrep</t> reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.
    Thinprep Pap Test, supplied by Hologic Inc, used in various techniques. Bioz Stars score: 91/100, based on 64 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/thinprep pap test/product/Hologic Inc
    Average 91 stars, based on 64 article reviews
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    99
    Millipore peroxidase anti peroxidase soluble complex antibody
    Frequency of false-positive tests for ⩾CIN2 (samples with abnormal cytology that were not followed by a histological diagnosis of ⩾CIN2), by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: <t>ThinPrep</t> reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.
    Peroxidase Anti Peroxidase Soluble Complex Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 610 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peroxidase anti peroxidase soluble complex antibody/product/Millipore
    Average 99 stars, based on 610 article reviews
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    peroxidase anti peroxidase soluble complex antibody - by Bioz Stars, 2020-11
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    99
    Millipore pap pen
    Frequency of false-positive tests for ⩾CIN2 (samples with abnormal cytology that were not followed by a histological diagnosis of ⩾CIN2), by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: <t>ThinPrep</t> reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.
    Pap Pen, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 294 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Agilent technologies pap pen
    Frequency of false-positive tests for ⩾CIN2 (samples with abnormal cytology that were not followed by a histological diagnosis of ⩾CIN2), by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: <t>ThinPrep</t> reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.
    Pap Pen, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 91/100, based on 119 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Stratagene pap 1 luc
    PG27 inhibited NF-κB and AP-1 activation induced by various stimuli. Human peripheral blood T cells at a concentration of 2 × 10 6 /mL were pretreated with various concentrations of PG27 for 2 h and then stimulated with PMA + ionomycin for 2 h (A) , CD3/CD28 for 6 h (B) or TNF-α for 6 h (C) . The nuclear extracts were prepared and analyzed for both NF-κB and AP-1 DNA-binding activity by EMSA. As a control, the DNA-binding activity of Oct-1 was measured (C) . In (D) , before adding the radiolabeled oligonucleotides to the reaction mixture, the nuclear extracts were preincubated with 5 μl of the indicated mAb for 30 min. The asterisk indicates the supershifted bands. In (E) , T cells at a concentration of 1 × 10 6 /mL were mixed with <t>pNF-κB-Luc</t> or <t>pAP-1-Luc</t> reporter plasmids and transfection reagents. The transfection was performed using an Amaxa Nucleofector according to the manufacturer’s instructions. After transfection for 48 h, the cells were aliquoted equally for the individual conditions and pretreated with various concentrations of PG27 for 2 h. After stimulation with TNF-α for another 18 h, cells were collected and total cell lysates were analyzed for luciferase activity. Cell survival was determined by trypan blue exclusion assays. Representative data of at least 3 independent experiments are shown.
    Pap 1 Luc, supplied by Stratagene, used in various techniques. Bioz Stars score: 89/100, based on 192 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Agilent technologies rabbit pap
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Rabbit Pap, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 88 stars, based on 81 article reviews
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    93
    Abcam pap pen
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Pap Pen, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 87 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Research Products International pap pen
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Pap Pen, supplied by Research Products International, used in various techniques. Bioz Stars score: 90/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 71 article reviews
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    91
    Boehringer Mannheim chod pap
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Chod Pap, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 91/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Becton Dickinson surepath pap test
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Surepath Pap Test, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 88/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Becton Dickinson surepath liquid based pap test
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Surepath Liquid Based Pap Test, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 88/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore peroxidase anti peroxidase pap antibody
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Peroxidase Anti Peroxidase Pap Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 87 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Ted Pella pap pen
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Pap Pen, supplied by Ted Pella, used in various techniques. Bioz Stars score: 90/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore anti pap antibody
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Anti Pap Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Bio/Data pap 4 aggregometer
    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in <t>Naf1p-depleted</t> cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit <t>PAP.</t> The remaining proteins were detected as described in previous figure legends.
    Pap 4 Aggregometer, supplied by Bio/Data, used in various techniques. Bioz Stars score: 88/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Stratagene pap 1 luciferase reporter plasmid
    Candidate MAPK phosphorylation sites confer PDGF responsiveness to the c-Fos TAD. (A) Schematic representation of c-Fos primary structure with emphasis on the major functional domains and the relative location of the four conserved sites that follow the consensus motif for MAPK phosphorylation in the C-terminal TAD (above). bZIP, region that comprises the leucine zipper and DBD; N- and C-TAD, N-terminal and C-terminal TADs, respectively. Details are shown for known c-Fos sequences from diverse species, showing the conservation of all four potential MAPK phosphorylation sites (below). Note that Thr-325, Thr-331, and Ser-374 lie within sequence motifs that are also highly conserved. (B) Effect of mutations in potential MAPK phosphorylation sites on the basal activity and inducibility by PDGF of the c-Fos TAD. Where indicated, cells were transfected with pGal4-FosTAD or pGal4-c-FosTAD-m (2 ng/well each) along with pGal4-luc, pRL-null, and MEKEE+ERK2 (0.5 μg each) (right panel). Cells were serum starved and stimulated with PDGF (20 ng/ml) or FBS (10%) (left panel) for 4 h before reading firefly and Renilla luciferase activities. Total lysates from Gal4c-FosTAD- or Gal4-c-FosTAD-m-overexpressing cells were analyzed by Western blotting using anti-Gal4 DBD antibodies (inset). (C) Effect of mutations in MAPK sites on the c-Fos activation of AP-1 transcription. NIH 3T3 fibroblasts were transfected with <t>pAP-1-Luc,</t> pRL-null, and 1 μg (right panel) or increasing concentrations (left panel) of pCEFL-AU5-c-Fos or pCEFL-AU5-c-Fos-m. Cells were incubated overnight in the absence of serum and then stimulated with PDGF for 4 h before measuring dual luciferase activities. Total lysates of c-Fos- or c-Fos-m-overexpressing cells were analyzed by Western blotting using anti-AU5 antibodies (left panel, inset). MEKEE and ERK2 were cotransfected at 0.5 μg each (right panel). Reporter assay data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. All values are the average ± standard deviation of triplicate samples from a typical experiment. Similar results were obtained in three additional experiments.
    Pap 1 Luciferase Reporter Plasmid, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Randox chod pap
    Candidate MAPK phosphorylation sites confer PDGF responsiveness to the c-Fos TAD. (A) Schematic representation of c-Fos primary structure with emphasis on the major functional domains and the relative location of the four conserved sites that follow the consensus motif for MAPK phosphorylation in the C-terminal TAD (above). bZIP, region that comprises the leucine zipper and DBD; N- and C-TAD, N-terminal and C-terminal TADs, respectively. Details are shown for known c-Fos sequences from diverse species, showing the conservation of all four potential MAPK phosphorylation sites (below). Note that Thr-325, Thr-331, and Ser-374 lie within sequence motifs that are also highly conserved. (B) Effect of mutations in potential MAPK phosphorylation sites on the basal activity and inducibility by PDGF of the c-Fos TAD. Where indicated, cells were transfected with pGal4-FosTAD or pGal4-c-FosTAD-m (2 ng/well each) along with pGal4-luc, pRL-null, and MEKEE+ERK2 (0.5 μg each) (right panel). Cells were serum starved and stimulated with PDGF (20 ng/ml) or FBS (10%) (left panel) for 4 h before reading firefly and Renilla luciferase activities. Total lysates from Gal4c-FosTAD- or Gal4-c-FosTAD-m-overexpressing cells were analyzed by Western blotting using anti-Gal4 DBD antibodies (inset). (C) Effect of mutations in MAPK sites on the c-Fos activation of AP-1 transcription. NIH 3T3 fibroblasts were transfected with <t>pAP-1-Luc,</t> pRL-null, and 1 μg (right panel) or increasing concentrations (left panel) of pCEFL-AU5-c-Fos or pCEFL-AU5-c-Fos-m. Cells were incubated overnight in the absence of serum and then stimulated with PDGF for 4 h before measuring dual luciferase activities. Total lysates of c-Fos- or c-Fos-m-overexpressing cells were analyzed by Western blotting using anti-AU5 antibodies (left panel, inset). MEKEE and ERK2 were cotransfected at 0.5 μg each (right panel). Reporter assay data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. All values are the average ± standard deviation of triplicate samples from a typical experiment. Similar results were obtained in three additional experiments.
    Chod Pap, supplied by Randox, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Bio/Data pap 4 platelet aggregometer
    Candidate MAPK phosphorylation sites confer PDGF responsiveness to the c-Fos TAD. (A) Schematic representation of c-Fos primary structure with emphasis on the major functional domains and the relative location of the four conserved sites that follow the consensus motif for MAPK phosphorylation in the C-terminal TAD (above). bZIP, region that comprises the leucine zipper and DBD; N- and C-TAD, N-terminal and C-terminal TADs, respectively. Details are shown for known c-Fos sequences from diverse species, showing the conservation of all four potential MAPK phosphorylation sites (below). Note that Thr-325, Thr-331, and Ser-374 lie within sequence motifs that are also highly conserved. (B) Effect of mutations in potential MAPK phosphorylation sites on the basal activity and inducibility by PDGF of the c-Fos TAD. Where indicated, cells were transfected with pGal4-FosTAD or pGal4-c-FosTAD-m (2 ng/well each) along with pGal4-luc, pRL-null, and MEKEE+ERK2 (0.5 μg each) (right panel). Cells were serum starved and stimulated with PDGF (20 ng/ml) or FBS (10%) (left panel) for 4 h before reading firefly and Renilla luciferase activities. Total lysates from Gal4c-FosTAD- or Gal4-c-FosTAD-m-overexpressing cells were analyzed by Western blotting using anti-Gal4 DBD antibodies (inset). (C) Effect of mutations in MAPK sites on the c-Fos activation of AP-1 transcription. NIH 3T3 fibroblasts were transfected with <t>pAP-1-Luc,</t> pRL-null, and 1 μg (right panel) or increasing concentrations (left panel) of pCEFL-AU5-c-Fos or pCEFL-AU5-c-Fos-m. Cells were incubated overnight in the absence of serum and then stimulated with PDGF for 4 h before measuring dual luciferase activities. Total lysates of c-Fos- or c-Fos-m-overexpressing cells were analyzed by Western blotting using anti-AU5 antibodies (left panel, inset). MEKEE and ERK2 were cotransfected at 0.5 μg each (right panel). Reporter assay data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. All values are the average ± standard deviation of triplicate samples from a typical experiment. Similar results were obtained in three additional experiments.
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    Frequency of false-positive tests for ⩾CIN2 (samples with abnormal cytology that were not followed by a histological diagnosis of ⩾CIN2), by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: ThinPrep reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.

    Journal: British Journal of Cancer

    Article Title: Cervical histology after routine ThinPrep or SurePath liquid-based cytology and computer-assisted reading in Denmark

    doi: 10.1038/bjc.2015.339

    Figure Lengend Snippet: Frequency of false-positive tests for ⩾CIN2 (samples with abnormal cytology that were not followed by a histological diagnosis of ⩾CIN2), by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: ThinPrep reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.

    Article Snippet: Odense laboratory started using ThinPrep technology in phase 2 when conventional cytology was replaced by LBC using ThinPrep Pap test in T3000 processor (Hologic).

    Techniques:

    Frequency of histologically confirmed ⩾CIN2, by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: ThinPrep reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.

    Journal: British Journal of Cancer

    Article Title: Cervical histology after routine ThinPrep or SurePath liquid-based cytology and computer-assisted reading in Denmark

    doi: 10.1038/bjc.2015.339

    Figure Lengend Snippet: Frequency of histologically confirmed ⩾CIN2, by laboratory and phase. Roskilde: manually read conventional cytology in all phases. Hvidovre and Hillerød: SurePath/FocalPoint reading and liquid-based cytology technologies. Odense: ThinPrep reading and liquid-based cytology technologies. ○, 23–29 years; □, 30–44 years; ◊, 45–59 years. Phases as described in Table 1 . CPH M, Copenhagen Municipality.

    Article Snippet: Odense laboratory started using ThinPrep technology in phase 2 when conventional cytology was replaced by LBC using ThinPrep Pap test in T3000 processor (Hologic).

    Techniques:

    PG27 inhibited NF-κB and AP-1 activation induced by various stimuli. Human peripheral blood T cells at a concentration of 2 × 10 6 /mL were pretreated with various concentrations of PG27 for 2 h and then stimulated with PMA + ionomycin for 2 h (A) , CD3/CD28 for 6 h (B) or TNF-α for 6 h (C) . The nuclear extracts were prepared and analyzed for both NF-κB and AP-1 DNA-binding activity by EMSA. As a control, the DNA-binding activity of Oct-1 was measured (C) . In (D) , before adding the radiolabeled oligonucleotides to the reaction mixture, the nuclear extracts were preincubated with 5 μl of the indicated mAb for 30 min. The asterisk indicates the supershifted bands. In (E) , T cells at a concentration of 1 × 10 6 /mL were mixed with pNF-κB-Luc or pAP-1-Luc reporter plasmids and transfection reagents. The transfection was performed using an Amaxa Nucleofector according to the manufacturer’s instructions. After transfection for 48 h, the cells were aliquoted equally for the individual conditions and pretreated with various concentrations of PG27 for 2 h. After stimulation with TNF-α for another 18 h, cells were collected and total cell lysates were analyzed for luciferase activity. Cell survival was determined by trypan blue exclusion assays. Representative data of at least 3 independent experiments are shown.

    Journal: Journal of Translational Medicine

    Article Title: Differential immunomodulatory effects by Tripterygium wilfordii Hook f-derived refined extract PG27 and its purified component PG490 (triptolide) in human peripheral blood T cells: potential therapeutics for arthritis and possible mechanisms explaining in part Chinese herbal theory “Junn-Chenn-Zuou-SS”

    doi: 10.1186/1479-5876-11-294

    Figure Lengend Snippet: PG27 inhibited NF-κB and AP-1 activation induced by various stimuli. Human peripheral blood T cells at a concentration of 2 × 10 6 /mL were pretreated with various concentrations of PG27 for 2 h and then stimulated with PMA + ionomycin for 2 h (A) , CD3/CD28 for 6 h (B) or TNF-α for 6 h (C) . The nuclear extracts were prepared and analyzed for both NF-κB and AP-1 DNA-binding activity by EMSA. As a control, the DNA-binding activity of Oct-1 was measured (C) . In (D) , before adding the radiolabeled oligonucleotides to the reaction mixture, the nuclear extracts were preincubated with 5 μl of the indicated mAb for 30 min. The asterisk indicates the supershifted bands. In (E) , T cells at a concentration of 1 × 10 6 /mL were mixed with pNF-κB-Luc or pAP-1-Luc reporter plasmids and transfection reagents. The transfection was performed using an Amaxa Nucleofector according to the manufacturer’s instructions. After transfection for 48 h, the cells were aliquoted equally for the individual conditions and pretreated with various concentrations of PG27 for 2 h. After stimulation with TNF-α for another 18 h, cells were collected and total cell lysates were analyzed for luciferase activity. Cell survival was determined by trypan blue exclusion assays. Representative data of at least 3 independent experiments are shown.

    Article Snippet: In brief, primary T cells were mixed with 5 μg of the reporter plasmid pNF-κB-luciferase (Luc) or pAP-1-Luc (Stratagene, La Jolla, CA) in 100 μL of the provided electroporation buffer.

    Techniques: Activation Assay, Concentration Assay, Binding Assay, Activity Assay, Transfection, Luciferase

    PG490 inhibited both NF-κB and AP-1 DNA-binding and transcriptional activity. T cells were pretreated with various concentrations of PG490 (A) for 2 h and then stimulated with TNF-α (B) or CD3/CD28 (C) for 6 h. The nuclear extracts were analyzed for both NF-κB and AP-1 DNA-binding activity by EMSA. In (D) , T cells were pretreated with PG490 for 2 h or left untreated, and then stimulated with TNF-α for various lengths of time as indicated. After washing, cell pellets were collected and cytoplasmic extracts were analyzed for the protein levels of IκBα and β-actin by Western blotting. In (E) , T cells were mixed together with pNF-κB-Luc or pAP-1-Luc reporter plasmids and the transfection procedures were performed as described for Figure 2 . After electroporation for 48 h, the cells were aliquoted equally and pretreated with various concentrations of PG490 for 2 h. After stimulation with TNF-α for another 18 h, cells were collected and analyzed for luciferase activity. Representative data of at least 3 independent experiments are shown.

    Journal: Journal of Translational Medicine

    Article Title: Differential immunomodulatory effects by Tripterygium wilfordii Hook f-derived refined extract PG27 and its purified component PG490 (triptolide) in human peripheral blood T cells: potential therapeutics for arthritis and possible mechanisms explaining in part Chinese herbal theory “Junn-Chenn-Zuou-SS”

    doi: 10.1186/1479-5876-11-294

    Figure Lengend Snippet: PG490 inhibited both NF-κB and AP-1 DNA-binding and transcriptional activity. T cells were pretreated with various concentrations of PG490 (A) for 2 h and then stimulated with TNF-α (B) or CD3/CD28 (C) for 6 h. The nuclear extracts were analyzed for both NF-κB and AP-1 DNA-binding activity by EMSA. In (D) , T cells were pretreated with PG490 for 2 h or left untreated, and then stimulated with TNF-α for various lengths of time as indicated. After washing, cell pellets were collected and cytoplasmic extracts were analyzed for the protein levels of IκBα and β-actin by Western blotting. In (E) , T cells were mixed together with pNF-κB-Luc or pAP-1-Luc reporter plasmids and the transfection procedures were performed as described for Figure 2 . After electroporation for 48 h, the cells were aliquoted equally and pretreated with various concentrations of PG490 for 2 h. After stimulation with TNF-α for another 18 h, cells were collected and analyzed for luciferase activity. Representative data of at least 3 independent experiments are shown.

    Article Snippet: In brief, primary T cells were mixed with 5 μg of the reporter plasmid pNF-κB-luciferase (Luc) or pAP-1-Luc (Stratagene, La Jolla, CA) in 100 μL of the provided electroporation buffer.

    Techniques: Binding Assay, Activity Assay, Western Blot, Transfection, Electroporation, Luciferase

    Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in Naf1p-depleted cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit PAP. The remaining proteins were detected as described in previous figure legends.

    Journal: Molecular and Cellular Biology

    Article Title: Naf1p, an Essential Nucleoplasmic Factor Specifically Required for Accumulation of Box H/ACA Small Nucleolar RNPs †

    doi: 10.1128/MCB.22.20.7053-7065.2002

    Figure Lengend Snippet: Analysis of steady-state levels of H/ACA snoRNP components and of the snR44 host gene mRNA in Naf1p-depleted cells. GAL :: zz - naf1 (lanes 1 to 6) or GAL :: naf1 / CBF5 - TAP (lanes 7 to 12) cells were grown in a medium containing galactose (gal), raffinose, and sucrose, were washed, and shifted to a medium containing glucose (glu). Cell aliquots were collected from the cultures grown in galactose, raffinose, and sucrose (lanes 1 and 7) and after 6 (lanes 2 and 8), 12 (lanes 3 and 9), 24 (lanes 4 and 10), 48 (lanes 5 and 11), and 72 (lanes 6 and 12) h of growth in glucose-containing medium. Total RNAs and proteins were extracted from these samples for Northern (A) and Western (B) blot analysis. A large set of RNAs was detected by use of complementary oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify RNA levels. Values indicated are percentages of the figures obtained for RNAs originating from cells grown on galactose, raffinose, and sucrose. Cbf5p-TAP was detected using rabbit PAP. The remaining proteins were detected as described in previous figure legends.

    Article Snippet: Naf1p-ZZ and Cbf5p-TAP were detected using rabbit PAP (Dako) diluted 10,000-fold.

    Techniques: Northern Blot, Western Blot

    Analysis of the interactions between Naf1p-ZZ and H/ACA snoRNP components. Total extracts were produced in native conditions from yeast cells expressing either free ZZ tag (lanes 1 to 3), ZZ-Nop1p (lanes 4 to 6), Cbf5p-ZZ (lanes 7 to 9), or Naf1p-ZZ (lanes 10 to 12). Immunoprecipitation experiments were carried out using IgG-Sepharose beads in a buffer containing either 150 mM (lanes 2, 5, 8, and 11) or 500 mM (lanes 3, 6, 9, and 12) KOAc. After precipitation and being washed, beads were separated in two equal fractions. (A) Western blot analysis. Beads from one set of fractions were resuspended in protein-denaturing buffer. Aliquots of the resulting supernatants (lanes 2, 3, 5, 6, 8, 9, 11, and 12) and 1/20 of the corresponding amount of total proteins from the input extract (T and lanes 1, 4, 7, and 10) were submitted to SDS-polyacrylamide gel electrophoresis. Proteins were transferred to cellulose membranes. Tagged proteins were detected by use of rabbit PAP, Nsr1p by a monoclonal antibody, and Nop1p, Gar1p, Nhp2p, and Nop10p by polyclonal sera. Northern blot (B) and analysis (C) of [ 32 P]pCp-labeled RNAs. RNAs retained on the beads of the second set of fractions were purified. Aliquots of precipitated RNAs (lanes 2, 3, 5, 6, 8, 9, 11, and 12) and 1/10 of the corresponding amount of total RNAs from the input extract (T and lanes 1, 4, 7, and 10) were submitted to denaturing 6% polyacrylamide gel electrophoresis. In panel B, separated RNAs were transferred to nylon membranes, and various H/ACA and C/D snoRNAs were detected by hybridization with specific oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify snoRNA levels. The amounts of RNAs precipitated, expressed as percentages of input RNA levels, are indicated in the table on the right. In panel C, RNAs were 3′ end labeled with [ 32 P]pCp and separated on a 6% sequencing gel. M, molecular weight markers (pBR322 digested with Hae III and Taq I). Positions of RNAs inferred from their size are indicated.

    Journal: Molecular and Cellular Biology

    Article Title: Naf1p, an Essential Nucleoplasmic Factor Specifically Required for Accumulation of Box H/ACA Small Nucleolar RNPs †

    doi: 10.1128/MCB.22.20.7053-7065.2002

    Figure Lengend Snippet: Analysis of the interactions between Naf1p-ZZ and H/ACA snoRNP components. Total extracts were produced in native conditions from yeast cells expressing either free ZZ tag (lanes 1 to 3), ZZ-Nop1p (lanes 4 to 6), Cbf5p-ZZ (lanes 7 to 9), or Naf1p-ZZ (lanes 10 to 12). Immunoprecipitation experiments were carried out using IgG-Sepharose beads in a buffer containing either 150 mM (lanes 2, 5, 8, and 11) or 500 mM (lanes 3, 6, 9, and 12) KOAc. After precipitation and being washed, beads were separated in two equal fractions. (A) Western blot analysis. Beads from one set of fractions were resuspended in protein-denaturing buffer. Aliquots of the resulting supernatants (lanes 2, 3, 5, 6, 8, 9, 11, and 12) and 1/20 of the corresponding amount of total proteins from the input extract (T and lanes 1, 4, 7, and 10) were submitted to SDS-polyacrylamide gel electrophoresis. Proteins were transferred to cellulose membranes. Tagged proteins were detected by use of rabbit PAP, Nsr1p by a monoclonal antibody, and Nop1p, Gar1p, Nhp2p, and Nop10p by polyclonal sera. Northern blot (B) and analysis (C) of [ 32 P]pCp-labeled RNAs. RNAs retained on the beads of the second set of fractions were purified. Aliquots of precipitated RNAs (lanes 2, 3, 5, 6, 8, 9, 11, and 12) and 1/10 of the corresponding amount of total RNAs from the input extract (T and lanes 1, 4, 7, and 10) were submitted to denaturing 6% polyacrylamide gel electrophoresis. In panel B, separated RNAs were transferred to nylon membranes, and various H/ACA and C/D snoRNAs were detected by hybridization with specific oligonucleotide probes. Phosphorimager scans of the Northern blots were used to quantify snoRNA levels. The amounts of RNAs precipitated, expressed as percentages of input RNA levels, are indicated in the table on the right. In panel C, RNAs were 3′ end labeled with [ 32 P]pCp and separated on a 6% sequencing gel. M, molecular weight markers (pBR322 digested with Hae III and Taq I). Positions of RNAs inferred from their size are indicated.

    Article Snippet: Naf1p-ZZ and Cbf5p-TAP were detected using rabbit PAP (Dako) diluted 10,000-fold.

    Techniques: Produced, Expressing, Immunoprecipitation, Western Blot, Polyacrylamide Gel Electrophoresis, Northern Blot, Labeling, Purification, Hybridization, Sequencing, Molecular Weight

    Candidate MAPK phosphorylation sites confer PDGF responsiveness to the c-Fos TAD. (A) Schematic representation of c-Fos primary structure with emphasis on the major functional domains and the relative location of the four conserved sites that follow the consensus motif for MAPK phosphorylation in the C-terminal TAD (above). bZIP, region that comprises the leucine zipper and DBD; N- and C-TAD, N-terminal and C-terminal TADs, respectively. Details are shown for known c-Fos sequences from diverse species, showing the conservation of all four potential MAPK phosphorylation sites (below). Note that Thr-325, Thr-331, and Ser-374 lie within sequence motifs that are also highly conserved. (B) Effect of mutations in potential MAPK phosphorylation sites on the basal activity and inducibility by PDGF of the c-Fos TAD. Where indicated, cells were transfected with pGal4-FosTAD or pGal4-c-FosTAD-m (2 ng/well each) along with pGal4-luc, pRL-null, and MEKEE+ERK2 (0.5 μg each) (right panel). Cells were serum starved and stimulated with PDGF (20 ng/ml) or FBS (10%) (left panel) for 4 h before reading firefly and Renilla luciferase activities. Total lysates from Gal4c-FosTAD- or Gal4-c-FosTAD-m-overexpressing cells were analyzed by Western blotting using anti-Gal4 DBD antibodies (inset). (C) Effect of mutations in MAPK sites on the c-Fos activation of AP-1 transcription. NIH 3T3 fibroblasts were transfected with pAP-1-Luc, pRL-null, and 1 μg (right panel) or increasing concentrations (left panel) of pCEFL-AU5-c-Fos or pCEFL-AU5-c-Fos-m. Cells were incubated overnight in the absence of serum and then stimulated with PDGF for 4 h before measuring dual luciferase activities. Total lysates of c-Fos- or c-Fos-m-overexpressing cells were analyzed by Western blotting using anti-AU5 antibodies (left panel, inset). MEKEE and ERK2 were cotransfected at 0.5 μg each (right panel). Reporter assay data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. All values are the average ± standard deviation of triplicate samples from a typical experiment. Similar results were obtained in three additional experiments.

    Journal: Molecular and Cellular Biology

    Article Title: Phosphorylation of the Carboxyl-Terminal Transactivation Domain of c-Fos by Extracellular Signal-Regulated Kinase Mediates the Transcriptional Activation of AP-1 and Cellular Transformation Induced by Platelet-Derived Growth Factor

    doi: 10.1128/MCB.23.19.7030-7043.2003

    Figure Lengend Snippet: Candidate MAPK phosphorylation sites confer PDGF responsiveness to the c-Fos TAD. (A) Schematic representation of c-Fos primary structure with emphasis on the major functional domains and the relative location of the four conserved sites that follow the consensus motif for MAPK phosphorylation in the C-terminal TAD (above). bZIP, region that comprises the leucine zipper and DBD; N- and C-TAD, N-terminal and C-terminal TADs, respectively. Details are shown for known c-Fos sequences from diverse species, showing the conservation of all four potential MAPK phosphorylation sites (below). Note that Thr-325, Thr-331, and Ser-374 lie within sequence motifs that are also highly conserved. (B) Effect of mutations in potential MAPK phosphorylation sites on the basal activity and inducibility by PDGF of the c-Fos TAD. Where indicated, cells were transfected with pGal4-FosTAD or pGal4-c-FosTAD-m (2 ng/well each) along with pGal4-luc, pRL-null, and MEKEE+ERK2 (0.5 μg each) (right panel). Cells were serum starved and stimulated with PDGF (20 ng/ml) or FBS (10%) (left panel) for 4 h before reading firefly and Renilla luciferase activities. Total lysates from Gal4c-FosTAD- or Gal4-c-FosTAD-m-overexpressing cells were analyzed by Western blotting using anti-Gal4 DBD antibodies (inset). (C) Effect of mutations in MAPK sites on the c-Fos activation of AP-1 transcription. NIH 3T3 fibroblasts were transfected with pAP-1-Luc, pRL-null, and 1 μg (right panel) or increasing concentrations (left panel) of pCEFL-AU5-c-Fos or pCEFL-AU5-c-Fos-m. Cells were incubated overnight in the absence of serum and then stimulated with PDGF for 4 h before measuring dual luciferase activities. Total lysates of c-Fos- or c-Fos-m-overexpressing cells were analyzed by Western blotting using anti-AU5 antibodies (left panel, inset). MEKEE and ERK2 were cotransfected at 0.5 μg each (right panel). Reporter assay data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. All values are the average ± standard deviation of triplicate samples from a typical experiment. Similar results were obtained in three additional experiments.

    Article Snippet: The pAP-1 luciferase reporter plasmid was obtained from Stratagene.

    Techniques: Functional Assay, Sequencing, Activity Assay, Transfection, Luciferase, Western Blot, Activation Assay, Incubation, Reporter Assay, Standard Deviation

    JNK and ERK pathways mediate AP-1 activation by PDGF and serum. NIH 3T3 cells were transfected with pAP-1-Luc and pRL-null, cultured under serum-free conditions, and pretreated for 30 min with inhibitors for each MAPK pathway (U0126, SP600125, and SB203580; 10 μM each) before PDGF (20 ng/ml) or FBS (10%) stimulation. Dual luciferase activities were determined 4 h after treatment, as described in Materials and Methods. The data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. Values are the average ± standard deviation of triplicate samples from a typical experiment. Nearly identical results were obtained in three additional experiments.

    Journal: Molecular and Cellular Biology

    Article Title: Phosphorylation of the Carboxyl-Terminal Transactivation Domain of c-Fos by Extracellular Signal-Regulated Kinase Mediates the Transcriptional Activation of AP-1 and Cellular Transformation Induced by Platelet-Derived Growth Factor

    doi: 10.1128/MCB.23.19.7030-7043.2003

    Figure Lengend Snippet: JNK and ERK pathways mediate AP-1 activation by PDGF and serum. NIH 3T3 cells were transfected with pAP-1-Luc and pRL-null, cultured under serum-free conditions, and pretreated for 30 min with inhibitors for each MAPK pathway (U0126, SP600125, and SB203580; 10 μM each) before PDGF (20 ng/ml) or FBS (10%) stimulation. Dual luciferase activities were determined 4 h after treatment, as described in Materials and Methods. The data represent the firefly luciferase activity normalized by Renilla luciferase activity present in each sample, expressed as absolute counts. Values are the average ± standard deviation of triplicate samples from a typical experiment. Nearly identical results were obtained in three additional experiments.

    Article Snippet: The pAP-1 luciferase reporter plasmid was obtained from Stratagene.

    Techniques: Activation Assay, Transfection, Cell Culture, Luciferase, Activity Assay, Standard Deviation