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  • 99
    Thermo Fisher n2 supplement
    N2 Supplement, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 8491 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore n acetyl l cysteine
    HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM <t>NAC</t> for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and <t>DAPI</t> (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p
    N Acetyl L Cysteine, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cold Spring Harbor Laboratory Press n y cold spring harbor laboratory press
    HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM <t>NAC</t> for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and <t>DAPI</t> (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p
    N Y Cold Spring Harbor Laboratory Press, supplied by Cold Spring Harbor Laboratory Press, used in various techniques. Bioz Stars score: 92/100, based on 13865 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare hybond n membrane
    HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM <t>NAC</t> for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and <t>DAPI</t> (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p
    Hybond N Membrane, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 19468 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore n hydroxysuccinimide nhs
    HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM <t>NAC</t> for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and <t>DAPI</t> (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p
    N Hydroxysuccinimide Nhs, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2803 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore n ethylmaleimide
    HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM <t>NAC</t> for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and <t>DAPI</t> (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p
    N Ethylmaleimide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5325 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc n cadherin
    Long non-coding RNA HOXD-AS1 regulates epithelial-mesenchymal transition and stem cell formation in colorectal cancer cells. (A) Knockdown of HOXD-AS1 increased <t>E-cadherin</t> expression and reduced Vimentin expression in HCT116 cell. Magnification, ×200. (B) RT-qPCR analysis demonstrated that knockdown of HOXD-AS1 decreased the expression levels of Vimentin, N-cadherin, Slug and Snail, and increased the expression of E-cadherin, α-catenin and β-catenin in HCT116 cells ( * P
    N Cadherin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 5180 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam n cadherin
    Association of four epithelial-mesenchymal transition-a ssociated markers with overall survival. Kaplan-Meier overall survival curves stratified by the expression of (A) <t>E-cadherin,</t> (B) N-cadherin, (C) β-catenin and (D) ZEB2. P-values were calculated using the log-rank test. ZEB2, zinc finger E-box binding homeobox 2.
    N Cadherin, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 3492 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher sulfo nhs ss biotin
    Association of four epithelial-mesenchymal transition-a ssociated markers with overall survival. Kaplan-Meier overall survival curves stratified by the expression of (A) <t>E-cadherin,</t> (B) N-cadherin, (C) β-catenin and (D) ZEB2. P-values were calculated using the log-rank test. ZEB2, zinc finger E-box binding homeobox 2.
    Sulfo Nhs Ss Biotin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4097 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Springer-Verlag n y springer verlag
    Association of four epithelial-mesenchymal transition-a ssociated markers with overall survival. Kaplan-Meier overall survival curves stratified by the expression of (A) <t>E-cadherin,</t> (B) N-cadherin, (C) β-catenin and (D) ZEB2. P-values were calculated using the log-rank test. ZEB2, zinc finger E-box binding homeobox 2.
    N Y Springer Verlag, supplied by Springer-Verlag, used in various techniques. Bioz Stars score: 92/100, based on 1051 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore nmda
    TNF is produced by MSC and contributes to MSC CM-mediated neuroprotection against glutamate excitotoxicity. ( A ) <t>DIV</t> 9 neurons (N) were pre-treated with high glucose DMEM medium alone (hgDMEM) or MSC CM without or with etanercept (100 ng/ml) (24 h), then left untreated or challenged with <t>NMDA</t> (50 μM) supplemented with glycine (10 μM) (24 h), and death was measured at DIV 11 by Hoechst staining. Etanercept treatment consistently resulted in a small but significant increase in NMDA-induced excitotoxicity, as measured by fold changes in proportions of cells with pyknotic nuclei compared to those in cells treated with MSC CM alone ( Ai and ii , arrows show pyknotic nuclei). Neuron death is represented as fold differences compared to measurements in untreated cultures ( Ai ). Representative fields from each culture are shown in the photographs ( Aii ). ( B ) TNF-induced cytotoxicity of L929 fibroblasts was measured in the presence of 1 μg/ml emetine, using increasing amounts of recombinant human TNF (rhTNF) (1, 10, 100 and 1000 pg/ml) added to non-conditioned hgDMEM or MSC CM without or with etanercept (200 ng/ml). MSC CM consistently induced more cytotoxicity than non-conditioned hgDMEM at each concentration of added rhTNF used, demonstrating that MSC CM contains TNF bioactivity (estimated between 0.15–0.24 U/ml). Etanercept inhibited cytotoxicity in all preparations showing that cytotoxicity was specifically induced by TNF. Scale bars 50 μM. Results shown are means ± SEM of triplicate samples from one representative of three independent experiments. * p
    Nmda, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1815 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs peptide n glycosidase f
    The  N -glycan on ZIKV prM is important for the virus life cycle. ( a ) Schematic diagram of experiments. ( b ) Representative picture of ZsGreen expression from four variants of ZIKV RNA transfected into Vero B4 cells. The monitoring was performed as scheduled in  Figure 3 a . Scale bar = 20 µm. ( c ) Virus egress kinetics by qRT-PCR, depicted as copy number of ZIKV NS5 RNA in 100 µL of harvested supernatant, as scheduled in  Figure 3 a . Mean values and standard deviations are shown from three independent experiments. ( d ) Representative picture of the plaque-forming ability of harvested viruses. The ZIKV strains MR766 and BeH819015 (approximately, 100 plaque-forming units) were used as positive controls. Respectively, virus titer was measured using plaque assay and the average of virus titer and standard deviations are shown from two independent experiments. ( e ) Confirmation of presence/absence of the  N -glycan sites in the prM and E proteins. Vero B4 cells were infected with supernatant from day 6 ( Figure 3 a ). Three days after infection, the cell lysate was harvested and used for prM and E protein detection by Western blotting, with either absence or presence of peptide N-glycosidase F (PNGase F) treatment. The ZIKV strains MR766 (absence of  N -glycan in E) and BeH819015 (presence of  N -glycan in E) were used as controls.
    Peptide N Glycosidase F, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 92/100, based on 2435 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore n 3 dimethylaminopropyl n ethylcarbodiimide hydrochloride
    The  N -glycan on ZIKV prM is important for the virus life cycle. ( a ) Schematic diagram of experiments. ( b ) Representative picture of ZsGreen expression from four variants of ZIKV RNA transfected into Vero B4 cells. The monitoring was performed as scheduled in  Figure 3 a . Scale bar = 20 µm. ( c ) Virus egress kinetics by qRT-PCR, depicted as copy number of ZIKV NS5 RNA in 100 µL of harvested supernatant, as scheduled in  Figure 3 a . Mean values and standard deviations are shown from three independent experiments. ( d ) Representative picture of the plaque-forming ability of harvested viruses. The ZIKV strains MR766 and BeH819015 (approximately, 100 plaque-forming units) were used as positive controls. Respectively, virus titer was measured using plaque assay and the average of virus titer and standard deviations are shown from two independent experiments. ( e ) Confirmation of presence/absence of the  N -glycan sites in the prM and E proteins. Vero B4 cells were infected with supernatant from day 6 ( Figure 3 a ). Three days after infection, the cell lysate was harvested and used for prM and E protein detection by Western blotting, with either absence or presence of peptide N-glycosidase F (PNGase F) treatment. The ZIKV strains MR766 (absence of  N -glycan in E) and BeH819015 (presence of  N -glycan in E) were used as controls.
    N 3 Dimethylaminopropyl N Ethylcarbodiimide Hydrochloride, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 913 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore n dimethylformamide
    The  N -glycan on ZIKV prM is important for the virus life cycle. ( a ) Schematic diagram of experiments. ( b ) Representative picture of ZsGreen expression from four variants of ZIKV RNA transfected into Vero B4 cells. The monitoring was performed as scheduled in  Figure 3 a . Scale bar = 20 µm. ( c ) Virus egress kinetics by qRT-PCR, depicted as copy number of ZIKV NS5 RNA in 100 µL of harvested supernatant, as scheduled in  Figure 3 a . Mean values and standard deviations are shown from three independent experiments. ( d ) Representative picture of the plaque-forming ability of harvested viruses. The ZIKV strains MR766 and BeH819015 (approximately, 100 plaque-forming units) were used as positive controls. Respectively, virus titer was measured using plaque assay and the average of virus titer and standard deviations are shown from two independent experiments. ( e ) Confirmation of presence/absence of the  N -glycan sites in the prM and E proteins. Vero B4 cells were infected with supernatant from day 6 ( Figure 3 a ). Three days after infection, the cell lysate was harvested and used for prM and E protein detection by Western blotting, with either absence or presence of peptide N-glycosidase F (PNGase F) treatment. The ZIKV strains MR766 (absence of  N -glycan in E) and BeH819015 (presence of  N -glycan in E) were used as controls.
    N Dimethylformamide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1271 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM NAC for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and DAPI (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p

    Journal: Nature Communications

    Article Title: Nuclear lactate dehydrogenase A senses ROS to produce α-hydroxybutyrate for HPV-induced cervical tumor growth

    doi: 10.1038/s41467-018-06841-7

    Figure Lengend Snippet: HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM NAC for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and DAPI (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p

    Article Snippet: Hydrogen peroxide solution (H2 O2 ) (Sigma, 323381), N-acetyl cysteine (NAC) (Sigma, A7250), DAPI (Sigma, D9542), sodium pyruvate (Sigma, P5280), sodium (L) lactate solution (Sangon Biotech, A604046), sodium 2-ketobutyrate (Sigma, K0875), sodium 2-hydroxybutyrate (Santa Cruz, sc-258161), NADH (Sigma, N4505), EPZ004777 (Selleck, S7353), DPIC (Selleck, S8639), 50% glutaraldehyde solution (Sangon Biotech, A600875), and ML385 (MCE, HY-100523) were commercially obtained.

    Techniques: Translocation Assay, Immunohistochemistry, Stable Transfection, Expressing, Plasmid Preparation, Staining, Flow Cytometry, Cytometry, Two Tailed Test

    Long non-coding RNA HOXD-AS1 regulates epithelial-mesenchymal transition and stem cell formation in colorectal cancer cells. (A) Knockdown of HOXD-AS1 increased E-cadherin expression and reduced Vimentin expression in HCT116 cell. Magnification, ×200. (B) RT-qPCR analysis demonstrated that knockdown of HOXD-AS1 decreased the expression levels of Vimentin, N-cadherin, Slug and Snail, and increased the expression of E-cadherin, α-catenin and β-catenin in HCT116 cells ( * P

    Journal: International Journal of Oncology

    Article Title: Long non-coding RNA HOXD-AS1 promotes tumor progression and predicts poor prognosis in colorectal cancer

    doi: 10.3892/ijo.2018.4400

    Figure Lengend Snippet: Long non-coding RNA HOXD-AS1 regulates epithelial-mesenchymal transition and stem cell formation in colorectal cancer cells. (A) Knockdown of HOXD-AS1 increased E-cadherin expression and reduced Vimentin expression in HCT116 cell. Magnification, ×200. (B) RT-qPCR analysis demonstrated that knockdown of HOXD-AS1 decreased the expression levels of Vimentin, N-cadherin, Slug and Snail, and increased the expression of E-cadherin, α-catenin and β-catenin in HCT116 cells ( * P

    Article Snippet: The following antibodies were used in the present study: E-cadherin (#3199S) and N-cadherin (#14215S) (both from Cell Signaling Technology, Inc., Danvers, MA, USA).

    Techniques: Expressing, Quantitative RT-PCR

    Association of four epithelial-mesenchymal transition-a ssociated markers with overall survival. Kaplan-Meier overall survival curves stratified by the expression of (A) E-cadherin, (B) N-cadherin, (C) β-catenin and (D) ZEB2. P-values were calculated using the log-rank test. ZEB2, zinc finger E-box binding homeobox 2.

    Journal: Oncology Letters

    Article Title: Role of epithelial-mesenchymal transition markers E-cadherin, N-cadherin, β-catenin and ZEB2 in laryngeal squamous cell carcinoma

    doi: 10.3892/ol.2018.7751

    Figure Lengend Snippet: Association of four epithelial-mesenchymal transition-a ssociated markers with overall survival. Kaplan-Meier overall survival curves stratified by the expression of (A) E-cadherin, (B) N-cadherin, (C) β-catenin and (D) ZEB2. P-values were calculated using the log-rank test. ZEB2, zinc finger E-box binding homeobox 2.

    Article Snippet: Sections were subsequently incubated with primary antibodies against E-cadherin (mouse monoclonal; cat. no., ab1416), N-cadherin (rabbit polyclonal; cat. no., ab18203), β-catenin (rabbit monoclonal; cat. no., ab32572), and ZEB2 (rabbit polyclonal; cat. no., ab138222; all Abcam, Cambridge, UK) overnight at 4°C.

    Techniques: Expressing, Binding Assay

    TNF is produced by MSC and contributes to MSC CM-mediated neuroprotection against glutamate excitotoxicity. ( A ) DIV 9 neurons (N) were pre-treated with high glucose DMEM medium alone (hgDMEM) or MSC CM without or with etanercept (100 ng/ml) (24 h), then left untreated or challenged with NMDA (50 μM) supplemented with glycine (10 μM) (24 h), and death was measured at DIV 11 by Hoechst staining. Etanercept treatment consistently resulted in a small but significant increase in NMDA-induced excitotoxicity, as measured by fold changes in proportions of cells with pyknotic nuclei compared to those in cells treated with MSC CM alone ( Ai and ii , arrows show pyknotic nuclei). Neuron death is represented as fold differences compared to measurements in untreated cultures ( Ai ). Representative fields from each culture are shown in the photographs ( Aii ). ( B ) TNF-induced cytotoxicity of L929 fibroblasts was measured in the presence of 1 μg/ml emetine, using increasing amounts of recombinant human TNF (rhTNF) (1, 10, 100 and 1000 pg/ml) added to non-conditioned hgDMEM or MSC CM without or with etanercept (200 ng/ml). MSC CM consistently induced more cytotoxicity than non-conditioned hgDMEM at each concentration of added rhTNF used, demonstrating that MSC CM contains TNF bioactivity (estimated between 0.15–0.24 U/ml). Etanercept inhibited cytotoxicity in all preparations showing that cytotoxicity was specifically induced by TNF. Scale bars 50 μM. Results shown are means ± SEM of triplicate samples from one representative of three independent experiments. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Mesenchymal Stem Cell Protection of Neurons against Glutamate Excitotoxicity Involves Reduction of NMDA-Triggered Calcium Responses and Surface GluR1, and Is Partly Mediated by TNF

    doi: 10.3390/ijms19030651

    Figure Lengend Snippet: TNF is produced by MSC and contributes to MSC CM-mediated neuroprotection against glutamate excitotoxicity. ( A ) DIV 9 neurons (N) were pre-treated with high glucose DMEM medium alone (hgDMEM) or MSC CM without or with etanercept (100 ng/ml) (24 h), then left untreated or challenged with NMDA (50 μM) supplemented with glycine (10 μM) (24 h), and death was measured at DIV 11 by Hoechst staining. Etanercept treatment consistently resulted in a small but significant increase in NMDA-induced excitotoxicity, as measured by fold changes in proportions of cells with pyknotic nuclei compared to those in cells treated with MSC CM alone ( Ai and ii , arrows show pyknotic nuclei). Neuron death is represented as fold differences compared to measurements in untreated cultures ( Ai ). Representative fields from each culture are shown in the photographs ( Aii ). ( B ) TNF-induced cytotoxicity of L929 fibroblasts was measured in the presence of 1 μg/ml emetine, using increasing amounts of recombinant human TNF (rhTNF) (1, 10, 100 and 1000 pg/ml) added to non-conditioned hgDMEM or MSC CM without or with etanercept (200 ng/ml). MSC CM consistently induced more cytotoxicity than non-conditioned hgDMEM at each concentration of added rhTNF used, demonstrating that MSC CM contains TNF bioactivity (estimated between 0.15–0.24 U/ml). Etanercept inhibited cytotoxicity in all preparations showing that cytotoxicity was specifically induced by TNF. Scale bars 50 μM. Results shown are means ± SEM of triplicate samples from one representative of three independent experiments. * p

    Article Snippet: Excitotoxic death was induced in DIV 10 neurons by exposure to 50 μM NMDA (Sigma-Aldrich, St. Louis, MO, USA; M3262) supplemented with 10 μM glycine for 24 h. The NMDAR antagonist MK801 was added to culture medium at 10 μM.

    Techniques: Produced, Staining, Recombinant, Concentration Assay

    The  N -glycan on ZIKV prM is important for the virus life cycle. ( a ) Schematic diagram of experiments. ( b ) Representative picture of ZsGreen expression from four variants of ZIKV RNA transfected into Vero B4 cells. The monitoring was performed as scheduled in  Figure 3 a . Scale bar = 20 µm. ( c ) Virus egress kinetics by qRT-PCR, depicted as copy number of ZIKV NS5 RNA in 100 µL of harvested supernatant, as scheduled in  Figure 3 a . Mean values and standard deviations are shown from three independent experiments. ( d ) Representative picture of the plaque-forming ability of harvested viruses. The ZIKV strains MR766 and BeH819015 (approximately, 100 plaque-forming units) were used as positive controls. Respectively, virus titer was measured using plaque assay and the average of virus titer and standard deviations are shown from two independent experiments. ( e ) Confirmation of presence/absence of the  N -glycan sites in the prM and E proteins. Vero B4 cells were infected with supernatant from day 6 ( Figure 3 a ). Three days after infection, the cell lysate was harvested and used for prM and E protein detection by Western blotting, with either absence or presence of peptide N-glycosidase F (PNGase F) treatment. The ZIKV strains MR766 (absence of  N -glycan in E) and BeH819015 (presence of  N -glycan in E) were used as controls.

    Journal: Viruses

    Article Title: N-glycosylation in the Pre-Membrane Protein Is Essential for the Zika Virus Life Cycle

    doi: 10.3390/v12090925

    Figure Lengend Snippet: The N -glycan on ZIKV prM is important for the virus life cycle. ( a ) Schematic diagram of experiments. ( b ) Representative picture of ZsGreen expression from four variants of ZIKV RNA transfected into Vero B4 cells. The monitoring was performed as scheduled in Figure 3 a . Scale bar = 20 µm. ( c ) Virus egress kinetics by qRT-PCR, depicted as copy number of ZIKV NS5 RNA in 100 µL of harvested supernatant, as scheduled in Figure 3 a . Mean values and standard deviations are shown from three independent experiments. ( d ) Representative picture of the plaque-forming ability of harvested viruses. The ZIKV strains MR766 and BeH819015 (approximately, 100 plaque-forming units) were used as positive controls. Respectively, virus titer was measured using plaque assay and the average of virus titer and standard deviations are shown from two independent experiments. ( e ) Confirmation of presence/absence of the N -glycan sites in the prM and E proteins. Vero B4 cells were infected with supernatant from day 6 ( Figure 3 a ). Three days after infection, the cell lysate was harvested and used for prM and E protein detection by Western blotting, with either absence or presence of peptide N-glycosidase F (PNGase F) treatment. The ZIKV strains MR766 (absence of N -glycan in E) and BeH819015 (presence of N -glycan in E) were used as controls.

    Article Snippet: Glycosidase Treatment In order to confirm the absence or presence of an N-glycan in the prM and E proteins, peptide N-glycosidase F (PNGase F; NEB, Ipswich, MA, USA) treatment was carried out using Vero B4 cell lysates that were either: (1) infected by different ZIKV constructs or (2) transfected by different ZIKV prME expression plasmids.

    Techniques: Expressing, Transfection, Quantitative RT-PCR, Plaque Assay, Infection, Western Blot

    The lack of N -glycan on the pre-membrane (prM) or/and E protein caused impairment in the E protein expression and secretion. ( a ) Confirmation of absence/presence of N -glycosylation in the prM- and E proteins expressed from constructed plasmids. For the Western blotting, proteins were stained with anti-ZIKV E -, anti-ZIKV prM- or anti-β actin protein antibody ( b ) Representative Western blot picture of E- and β-actin protein expression in harvested cell lysate and cell culture supernatant from three independent experiments. ( c ) Quantification of E protein expression with Image J. To normalize the E protein expression in the cell lysate, the expression level of E protein was divided by the expression level of β-actin. To normalize the E protein expression in the supernatant, the expression level of E protein from the supernatant was divided by the expression level of E protein from the cell lysate. The experiment was repeated three times, average and SD are shown. Statistical significance was determined by two-tailed t-test. p = p value. GFP = pcDNA3.1-GFP vector; WT clone = pcDNA3.1-prME vectors with wild-type ZIKV prM-E genes; N69Q = pcDNA3.1-prME vector with a mutated N -glycosylation site in prM; N154Q = pcDNA3.1-prME vector with a mutated N -glycosylation site in E; N69Q/N154Q = pcDNA3.1-prME vector with mutated N -glycosylation sites in prM and E; PNGase F = Peptide:N-glycosidase F.

    Journal: Viruses

    Article Title: N-glycosylation in the Pre-Membrane Protein Is Essential for the Zika Virus Life Cycle

    doi: 10.3390/v12090925

    Figure Lengend Snippet: The lack of N -glycan on the pre-membrane (prM) or/and E protein caused impairment in the E protein expression and secretion. ( a ) Confirmation of absence/presence of N -glycosylation in the prM- and E proteins expressed from constructed plasmids. For the Western blotting, proteins were stained with anti-ZIKV E -, anti-ZIKV prM- or anti-β actin protein antibody ( b ) Representative Western blot picture of E- and β-actin protein expression in harvested cell lysate and cell culture supernatant from three independent experiments. ( c ) Quantification of E protein expression with Image J. To normalize the E protein expression in the cell lysate, the expression level of E protein was divided by the expression level of β-actin. To normalize the E protein expression in the supernatant, the expression level of E protein from the supernatant was divided by the expression level of E protein from the cell lysate. The experiment was repeated three times, average and SD are shown. Statistical significance was determined by two-tailed t-test. p = p value. GFP = pcDNA3.1-GFP vector; WT clone = pcDNA3.1-prME vectors with wild-type ZIKV prM-E genes; N69Q = pcDNA3.1-prME vector with a mutated N -glycosylation site in prM; N154Q = pcDNA3.1-prME vector with a mutated N -glycosylation site in E; N69Q/N154Q = pcDNA3.1-prME vector with mutated N -glycosylation sites in prM and E; PNGase F = Peptide:N-glycosidase F.

    Article Snippet: Glycosidase Treatment In order to confirm the absence or presence of an N-glycan in the prM and E proteins, peptide N-glycosidase F (PNGase F; NEB, Ipswich, MA, USA) treatment was carried out using Vero B4 cell lysates that were either: (1) infected by different ZIKV constructs or (2) transfected by different ZIKV prME expression plasmids.

    Techniques: Expressing, Construct, Western Blot, Staining, Cell Culture, Two Tailed Test, Plasmid Preparation