ferryl iron Search Results


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  • 99
    Thermo Fisher edta
    Digestion of T4gt by <t>SauUSI</t> in NEB buffers 1–4, in the presence of <t>EDTA,</t> or in the absence of metal ions (depleted from enzyme preparation). ( A ) Lanes 1–4, SauUSI digestion in NEB buffers 1 to 4. Lanes 5 and 6, 150 and 200 mM NaCl in a buffer containing 20 mM Tris–HCl, pH 8.0, 1 mM DTT, 10 mM MgCl 2 . Lane 7, SauUSI digestion in the NTD buffer (50 mM N aCl, 20 mM T ris–HCl, pH 8.0, 1 mM D TT), plus 10 mM EDTA. Lane 8, same as lane 7, except EDTA was left out, no additional metal ions were added to the buffer. Lane 9, T4gt DNA incubated with metal ion-depleted SauUSI in the NTD buffer without additional metal ions. Lane 10, T4gt DNA digested with metal ion-depleted SauUSI in buffer 4. Lane 11, same as lane 10, but supplemented with 10 mM EDTA. (B) SauUSI digestion of modified DNA mixed with unmodified DNA. Lanes 1–6, SauUSI digestion of DNAs. The “–” and “+” on top of pUC indicate unmodified or modified pUC19 by Dcm methylase, respectively. Lane 11, DpnI digestion of pUC19.
    Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 16222 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore superoxide dismutase
    Concentration-response curves showing the changes in tone induced by MnTMPyP on phenylephrine-contracted, endothelium-containing rings of rat aorta (control) and the effects of pretreatment with Cu/Zn superoxide <t>dismutase</t> (SOD, 250 u ml −1 , 30 min) on these changes. Each point is the mean±s.e.mean of 5–11 observations. * P
    Superoxide Dismutase, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1493 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore superoxide dismutase sod
    Effect of pure and Zn-doped TiO 2 NPs on superoxide <t>dismutase</t> <t>(SOD)</t> and heme oxygenase 1 (HO-1) genes in MCF-7 cells. ( a ) Western blot analysis of SOD1 (CuZn-SOD), SOD2 (Mn-SOD) and HO-1 protein levels. Cells were treated with 200 μg/ml pure and Zn-doped TiO 2 NPs for 6 h. Cells not exposed to NPs served as a negative control. The treated and untreated cells were lysed in RIPA buffer and cell extract subjected to western blots with anti-SOD1, anti-SOD2 anti-HO-1 antibodies. The β-actin blot is a loading control. ( b ) Protein levels were also analyzed by desitometric analysis using AlphaEase TM FC StandAlone V.4.0.0 software. Results are expressed as a fold change over the control group. ( c ) SOD enzyme activity in MCF-7 cells after exposure to pure and Zn-doped TiO 2 NPs. Cells were treated with 200 μg/ml of pure and Zn-doped TiO 2 NPs as well as pure Zn NPs for 6 h. SOD activity was expressed in terms of U/ml. ( d ) SOD enzyme extract attenuates Zn-doped TiO 2 NPs induced cytotoxicity. Cells were treated with 200 μg/ml of Zn-doped TiO 2 NPs in the presence or absence of SOD enzyme extract. Data represented are mean ± SD of three identical experiments made in three replicate. *Significant difference as compared to the control (p
    Superoxide Dismutase Sod, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 896 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore mgcl2
    Effect of pure and Zn-doped TiO 2 NPs on superoxide <t>dismutase</t> <t>(SOD)</t> and heme oxygenase 1 (HO-1) genes in MCF-7 cells. ( a ) Western blot analysis of SOD1 (CuZn-SOD), SOD2 (Mn-SOD) and HO-1 protein levels. Cells were treated with 200 μg/ml pure and Zn-doped TiO 2 NPs for 6 h. Cells not exposed to NPs served as a negative control. The treated and untreated cells were lysed in RIPA buffer and cell extract subjected to western blots with anti-SOD1, anti-SOD2 anti-HO-1 antibodies. The β-actin blot is a loading control. ( b ) Protein levels were also analyzed by desitometric analysis using AlphaEase TM FC StandAlone V.4.0.0 software. Results are expressed as a fold change over the control group. ( c ) SOD enzyme activity in MCF-7 cells after exposure to pure and Zn-doped TiO 2 NPs. Cells were treated with 200 μg/ml of pure and Zn-doped TiO 2 NPs as well as pure Zn NPs for 6 h. SOD activity was expressed in terms of U/ml. ( d ) SOD enzyme extract attenuates Zn-doped TiO 2 NPs induced cytotoxicity. Cells were treated with 200 μg/ml of Zn-doped TiO 2 NPs in the presence or absence of SOD enzyme extract. Data represented are mean ± SD of three identical experiments made in three replicate. *Significant difference as compared to the control (p
    Mgcl2, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 50653 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore x gal
    Effect of pure and Zn-doped TiO 2 NPs on superoxide <t>dismutase</t> <t>(SOD)</t> and heme oxygenase 1 (HO-1) genes in MCF-7 cells. ( a ) Western blot analysis of SOD1 (CuZn-SOD), SOD2 (Mn-SOD) and HO-1 protein levels. Cells were treated with 200 μg/ml pure and Zn-doped TiO 2 NPs for 6 h. Cells not exposed to NPs served as a negative control. The treated and untreated cells were lysed in RIPA buffer and cell extract subjected to western blots with anti-SOD1, anti-SOD2 anti-HO-1 antibodies. The β-actin blot is a loading control. ( b ) Protein levels were also analyzed by desitometric analysis using AlphaEase TM FC StandAlone V.4.0.0 software. Results are expressed as a fold change over the control group. ( c ) SOD enzyme activity in MCF-7 cells after exposure to pure and Zn-doped TiO 2 NPs. Cells were treated with 200 μg/ml of pure and Zn-doped TiO 2 NPs as well as pure Zn NPs for 6 h. SOD activity was expressed in terms of U/ml. ( d ) SOD enzyme extract attenuates Zn-doped TiO 2 NPs induced cytotoxicity. Cells were treated with 200 μg/ml of Zn-doped TiO 2 NPs in the presence or absence of SOD enzyme extract. Data represented are mean ± SD of three identical experiments made in three replicate. *Significant difference as compared to the control (p
    X Gal, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3365 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore 2 pyridyl 5 6 diphenyl 1
    Chemical structures of 3-(2-pyridyl)-5,6-di(2-furyl)-1,2,4-triazine-5′,5″-disulfonic acid disodium salt (ferene: L1) (left) and <t>3-(2-pyridyl)-5,6-diphenyl-1,2,4-triazine-4′,4″-disulfonic</t> acid sodium salt (ferrozine: L2) (right).
    2 Pyridyl 5 6 Diphenyl 1, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore triton x 100
    TEM images of the IO nanostructures obtained in the Lα phase of Triton X-45 in water: ( A , B ) 50 wt % Triton X-45, 1 mmol FeCl 3  (( A ): froth, ( B ): gel); ( C , D ) 50 wt % Triton X-45, 2 mmol FeCl 3  (( C ): froth, ( D ): gel); ( E , F ) 20 wt % Triton X-45, 1 mmol FeCl 3  (( E ): froth, ( F ): gel); ( G , H ) 50 wt % Triton X-45, 1 mmol Fe(acac) 3  (( G ): froth, ( H ): gel).
    Triton X 100, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 65173 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore potassium ferrocyanide
    TEM images of the IO nanostructures obtained in the Lα phase of Triton X-45 in water: ( A , B ) 50 wt % Triton X-45, 1 mmol FeCl 3  (( A ): froth, ( B ): gel); ( C , D ) 50 wt % Triton X-45, 2 mmol FeCl 3  (( C ): froth, ( D ): gel); ( E , F ) 20 wt % Triton X-45, 1 mmol FeCl 3  (( E ): froth, ( F ): gel); ( G , H ) 50 wt % Triton X-45, 1 mmol Fe(acac) 3  (( G ): froth, ( H ): gel).
    Potassium Ferrocyanide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1314 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore potassium ferricyanide
    TEM images of the IO nanostructures obtained in the Lα phase of Triton X-45 in water: ( A , B ) 50 wt % Triton X-45, 1 mmol FeCl 3  (( A ): froth, ( B ): gel); ( C , D ) 50 wt % Triton X-45, 2 mmol FeCl 3  (( C ): froth, ( D ): gel); ( E , F ) 20 wt % Triton X-45, 1 mmol FeCl 3  (( E ): froth, ( F ): gel); ( G , H ) 50 wt % Triton X-45, 1 mmol Fe(acac) 3  (( G ): froth, ( H ): gel).
    Potassium Ferricyanide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1558 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore transferrin
    Tryptophan fluorescence quenching spectra of <t>transferrin</t> (5 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations of Zr-K 1:2 (0–5 µM). The insert shows a plot of F 0 /F versus the POM concentration. (Right) Derived Stern-Volmer plot used to calculate the association constant.
    Transferrin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8257 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore pbs
    Tryptophan fluorescence quenching spectra of <t>transferrin</t> (5 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations of Zr-K 1:2 (0–5 µM). The insert shows a plot of F 0 /F versus the POM concentration. (Right) Derived Stern-Volmer plot used to calculate the association constant.
    Pbs, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 34240 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher x gal
    Tryptophan fluorescence quenching spectra of <t>transferrin</t> (5 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations of Zr-K 1:2 (0–5 µM). The insert shows a plot of F 0 /F versus the POM concentration. (Right) Derived Stern-Volmer plot used to calculate the association constant.
    X Gal, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1472 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher imdm
    Tryptophan fluorescence quenching spectra of <t>transferrin</t> (5 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations of Zr-K 1:2 (0–5 µM). The insert shows a plot of F 0 /F versus the POM concentration. (Right) Derived Stern-Volmer plot used to calculate the association constant.
    Imdm, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 7962 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Lonestar Heart sofosbuvir
    <t>Sofosbuvir</t>
    Sofosbuvir, supplied by Lonestar Heart, used in various techniques. Bioz Stars score: 90/100, based on 135 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher calcein am
    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in <t>calcein</t> release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles
    Calcein Am, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9277 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore sodium deoxycholate
    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in <t>calcein</t> release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles
    Sodium Deoxycholate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 18429 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher phosphate buffered saline
    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in <t>calcein</t> release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles
    Phosphate Buffered Saline, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 34842 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Altamira bioespeleo consultoria ambiental
    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in <t>calcein</t> release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles
    Bioespeleo Consultoria Ambiental, supplied by Altamira, used in various techniques. Bioz Stars score: 98/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore glutaraldehyde
    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in <t>calcein</t> release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles
    Glutaraldehyde, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 9219 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Thermo Fisher cryostat
    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in <t>calcein</t> release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles
    Cryostat, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 3604 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher insulin transferrin selenium
    Endocrine cell formation requires LSD1 activity during a short window in early pancreatic development. a Schematic of the human embryonic stem cell (hESC) differentiation protocol to the endocrine cell stage (EN) and experimental plan for LSD1 inhibition. b Immunofluorescent staining for pancreatic hormones insulin (INS), glucagon (GCG) and somatostatin (SST) or PDX1 and NKX6.1 in control EN cells compared to EN cells with early (LSD1i early ) and late (LSD1i late ) LSD1 inhibition (representative images, n = 10 independent differentiations). Scale bar, 50 µm. c qRT-PCR analysis for INS , GCG and SST in control, LSD1i early and LSD1i late EN cells. Data are shown as mean ± S.E.M. ( n = 3 replicates from independent differentiations with n = 3 technical replicates per sample; source data are provided as a Source Data file). P = 7.93 e−4, 1.42 e−2, 2.32 e−4, 8.71 e−4, 3.5 e−2, and 1.52 e−3, respectively, Student’s t -test, 2 sided. d Flow cytometry analysis at EN stage for NKX6.1, PDX1 and INS comparing control, LSD1i early and LSD1i late cells. Isotype control for each antibody is shown in red and target protein staining in green. Percentage of cells expressing each protein is indicated (representative experiment, n = 2 independent differentiations). D, day; AA, activin A; ITS, <t>insulin-transferrin-selenium;</t> TGFBi, TGFβ R1 kinase inhibitor; KC, KAAD-cyclopamine; KGF, keratinocyte growth factor; RA, retinoic acid; EGF, epidermal growth factor; ES, human embryonic stem cells; DE, definitive endoderm; GT, primitive gut tube; PP1, early pancreatic progenitors; PP2, late pancreatic progenitors; EN, endocrine cell stage; FSC-A, forward scatter area.
    Insulin Transferrin Selenium, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3832 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore imac select affinity gel
    Zinc inhibits <t>IFN-λ3:IFNLR1</t> binding. ( a ) To ascertain the cellular location of zinc inhibition following ZnSO 4 treatment, Huh-7 cells were pre-treated for 24 h with 50 μM ZnSO 4 , washed thoroughly, and then treated with IFN-λ3 ±50 μM ZnSO 4 for 15 min. STAT1 phosphorylation was significantly inhibited only when IFN-λ3 was administered in the presence of zinc, suggesting that zinc inhibits IFN-λ3 signalling at the receptor. ( b ) To identify cytokine zinc binding, 200 ng of IFN-α or IFN-λ3 were added to a zinc loaded <t>IMAC-affinity</t> resin for 2 h, after which bound protein was examined by SDS–PAGE. Dimeric forms of IFN-α and IFN-λ3 bound the zinc resin, as did monomeric IFN-λ3. ( c ) Using protein G beads, Co-IP was performed on Huh-7 cell lysates using recombinant IFN-λ3 alone or with the addition of 50 μM ZnSO 4 . Co-IP of both IFN-λ3 (66% reduction) and IFNLR1 (40% reduction) was reduced in the presence of zinc, when IFNLR1 and IFN-λ3 were immunoprecipitated respectively, demonstrating a direct inhibition of receptor:cytokine interaction by zinc. ( d ) Co-IP studies were confirmed using proximity ligation assays to examine the interaction of IFN-λ3 and IFNLR1 in the presence of zinc in situ . Confocal microscopy of IFN-λ3 treated Huh-7 cells demonstrated a reduction in fluorescent signals (red fluorescent spots), indicative of IFNLR1:IFN-λ3 interaction (within 40 nm). No signal was observed within the negative control assay lacking the primary IFN-λ3 antibody (1° Ab) or lacking the addition of IFN-λ3. ( e ) Proximity ligation signals per cell were quantified using ImageJ software, demonstrating a 50% decrease in IFNLR1:IFN-λ3 interactions per cell (Mann–Whitney test). ( d ) Scale bars, 10 μm. Data are representative of two independent experiments, *** P
    Imac Select Affinity Gel, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ferring Pharmaceuticals degarelix
    Relationship between total Sunshine payment amount and total Medicare reimbursement for <t>degarelix</t> and denosumab. Scatter plot of total Sunshine payment amount vs. total Medicare reimbursement in the log scale. Red line represents fitted linear prediction.
    Degarelix, supplied by Ferring Pharmaceuticals, used in various techniques. Bioz Stars score: 89/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cayman Chemical superoxide dismutase assay kit
    Real-time polymerase chain reaction expression of manganese superoxide <t>dismutase</t> in HLE-B3 cells. HLE-B3 cells were incubated with 1 μM 17β-E 2 for 0, 1.5, 3, 6, 12, and 24 h. The expression of MnSOD mRNA was analyzed by quantitative real-time PCR. According to the two-way ANOVA, there were no statistically significant changes in MnSOD mRNA at any time point after estrogen treatment compared to the control (untreated). Data are expressed as mean±SD values. p
    Superoxide Dismutase Assay Kit, supplied by Cayman Chemical, used in various techniques. Bioz Stars score: 93/100, based on 810 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore tris
    Real-time polymerase chain reaction expression of manganese superoxide <t>dismutase</t> in HLE-B3 cells. HLE-B3 cells were incubated with 1 μM 17β-E 2 for 0, 1.5, 3, 6, 12, and 24 h. The expression of MnSOD mRNA was analyzed by quantitative real-time PCR. According to the two-way ANOVA, there were no statistically significant changes in MnSOD mRNA at any time point after estrogen treatment compared to the control (untreated). Data are expressed as mean±SD values. p
    Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 38479 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Digestion of T4gt by SauUSI in NEB buffers 1–4, in the presence of EDTA, or in the absence of metal ions (depleted from enzyme preparation). ( A ) Lanes 1–4, SauUSI digestion in NEB buffers 1 to 4. Lanes 5 and 6, 150 and 200 mM NaCl in a buffer containing 20 mM Tris–HCl, pH 8.0, 1 mM DTT, 10 mM MgCl 2 . Lane 7, SauUSI digestion in the NTD buffer (50 mM N aCl, 20 mM T ris–HCl, pH 8.0, 1 mM D TT), plus 10 mM EDTA. Lane 8, same as lane 7, except EDTA was left out, no additional metal ions were added to the buffer. Lane 9, T4gt DNA incubated with metal ion-depleted SauUSI in the NTD buffer without additional metal ions. Lane 10, T4gt DNA digested with metal ion-depleted SauUSI in buffer 4. Lane 11, same as lane 10, but supplemented with 10 mM EDTA. (B) SauUSI digestion of modified DNA mixed with unmodified DNA. Lanes 1–6, SauUSI digestion of DNAs. The “–” and “+” on top of pUC indicate unmodified or modified pUC19 by Dcm methylase, respectively. Lane 11, DpnI digestion of pUC19.

    Journal: Nucleic Acids Research

    Article Title: A type IV modification-dependent restriction enzyme SauUSI from Staphylococcus aureus subsp. aureus USA300

    doi: 10.1093/nar/gkr098

    Figure Lengend Snippet: Digestion of T4gt by SauUSI in NEB buffers 1–4, in the presence of EDTA, or in the absence of metal ions (depleted from enzyme preparation). ( A ) Lanes 1–4, SauUSI digestion in NEB buffers 1 to 4. Lanes 5 and 6, 150 and 200 mM NaCl in a buffer containing 20 mM Tris–HCl, pH 8.0, 1 mM DTT, 10 mM MgCl 2 . Lane 7, SauUSI digestion in the NTD buffer (50 mM N aCl, 20 mM T ris–HCl, pH 8.0, 1 mM D TT), plus 10 mM EDTA. Lane 8, same as lane 7, except EDTA was left out, no additional metal ions were added to the buffer. Lane 9, T4gt DNA incubated with metal ion-depleted SauUSI in the NTD buffer without additional metal ions. Lane 10, T4gt DNA digested with metal ion-depleted SauUSI in buffer 4. Lane 11, same as lane 10, but supplemented with 10 mM EDTA. (B) SauUSI digestion of modified DNA mixed with unmodified DNA. Lanes 1–6, SauUSI digestion of DNAs. The “–” and “+” on top of pUC indicate unmodified or modified pUC19 by Dcm methylase, respectively. Lane 11, DpnI digestion of pUC19.

    Article Snippet: To remove the divalent metal ions bound by the purified SauUSI, the enzyme was supplemented with 20 mM EDTA and then dialyzed against a buffer (50 mM NaCl, 20 mM Tris–HCl, pH 8, 1 mM DTT) for 48 h at 4°C using a dialysis cassette (10 000 Da MWCO; Thermo Scientific Pierce).

    Techniques: Incubation, Modification

    Concentration-response curves showing the changes in tone induced by MnTMPyP on phenylephrine-contracted, endothelium-containing rings of rat aorta (control) and the effects of pretreatment with Cu/Zn superoxide dismutase (SOD, 250 u ml −1 , 30 min) on these changes. Each point is the mean±s.e.mean of 5–11 observations. * P

    Journal: British Journal of Pharmacology

    Article Title: Effects of superoxide dismutase mimetics on the activity of nitric oxide in rat aorta

    doi: 10.1038/sj.bjp.0702670

    Figure Lengend Snippet: Concentration-response curves showing the changes in tone induced by MnTMPyP on phenylephrine-contracted, endothelium-containing rings of rat aorta (control) and the effects of pretreatment with Cu/Zn superoxide dismutase (SOD, 250 u ml −1 , 30 min) on these changes. Each point is the mean±s.e.mean of 5–11 observations. * P

    Article Snippet: 4,5-dihydroxy-1,3-benzene-disulphonic acid (tiron), 4-hydroxy 2,2,6,6-tetramethylpiperidine-1-oxyl (tempol), phenylephrine hydrochloride, and superoxide dismutase (Cu/Zn-containing enzyme from bovine erythrocytes) were obtained from Sigma (Poole, U.K.).

    Techniques: Concentration Assay

    Concentration-response curves showing that the relaxation induced by MnTMPyP on phenylephrine-contracted, endothelium-denuded rings of rat aorta (control) was unaffected by pretreatment with Cu/Zn superoxide dismutase (SOD, 250 u ml −1 , 30 min). Each point is the mean±s.e.mean of eight observations.

    Journal: British Journal of Pharmacology

    Article Title: Effects of superoxide dismutase mimetics on the activity of nitric oxide in rat aorta

    doi: 10.1038/sj.bjp.0702670

    Figure Lengend Snippet: Concentration-response curves showing that the relaxation induced by MnTMPyP on phenylephrine-contracted, endothelium-denuded rings of rat aorta (control) was unaffected by pretreatment with Cu/Zn superoxide dismutase (SOD, 250 u ml −1 , 30 min). Each point is the mean±s.e.mean of eight observations.

    Article Snippet: 4,5-dihydroxy-1,3-benzene-disulphonic acid (tiron), 4-hydroxy 2,2,6,6-tetramethylpiperidine-1-oxyl (tempol), phenylephrine hydrochloride, and superoxide dismutase (Cu/Zn-containing enzyme from bovine erythrocytes) were obtained from Sigma (Poole, U.K.).

    Techniques: Concentration Assay

    Effect of pure and Zn-doped TiO 2 NPs on superoxide dismutase (SOD) and heme oxygenase 1 (HO-1) genes in MCF-7 cells. ( a ) Western blot analysis of SOD1 (CuZn-SOD), SOD2 (Mn-SOD) and HO-1 protein levels. Cells were treated with 200 μg/ml pure and Zn-doped TiO 2 NPs for 6 h. Cells not exposed to NPs served as a negative control. The treated and untreated cells were lysed in RIPA buffer and cell extract subjected to western blots with anti-SOD1, anti-SOD2 anti-HO-1 antibodies. The β-actin blot is a loading control. ( b ) Protein levels were also analyzed by desitometric analysis using AlphaEase TM FC StandAlone V.4.0.0 software. Results are expressed as a fold change over the control group. ( c ) SOD enzyme activity in MCF-7 cells after exposure to pure and Zn-doped TiO 2 NPs. Cells were treated with 200 μg/ml of pure and Zn-doped TiO 2 NPs as well as pure Zn NPs for 6 h. SOD activity was expressed in terms of U/ml. ( d ) SOD enzyme extract attenuates Zn-doped TiO 2 NPs induced cytotoxicity. Cells were treated with 200 μg/ml of Zn-doped TiO 2 NPs in the presence or absence of SOD enzyme extract. Data represented are mean ± SD of three identical experiments made in three replicate. *Significant difference as compared to the control (p

    Journal: Scientific Reports

    Article Title: Role of Zn doping in oxidative stress mediated cytotoxicity of TiO2 nanoparticles in human breast cancer MCF-7 cells

    doi: 10.1038/srep30196

    Figure Lengend Snippet: Effect of pure and Zn-doped TiO 2 NPs on superoxide dismutase (SOD) and heme oxygenase 1 (HO-1) genes in MCF-7 cells. ( a ) Western blot analysis of SOD1 (CuZn-SOD), SOD2 (Mn-SOD) and HO-1 protein levels. Cells were treated with 200 μg/ml pure and Zn-doped TiO 2 NPs for 6 h. Cells not exposed to NPs served as a negative control. The treated and untreated cells were lysed in RIPA buffer and cell extract subjected to western blots with anti-SOD1, anti-SOD2 anti-HO-1 antibodies. The β-actin blot is a loading control. ( b ) Protein levels were also analyzed by desitometric analysis using AlphaEase TM FC StandAlone V.4.0.0 software. Results are expressed as a fold change over the control group. ( c ) SOD enzyme activity in MCF-7 cells after exposure to pure and Zn-doped TiO 2 NPs. Cells were treated with 200 μg/ml of pure and Zn-doped TiO 2 NPs as well as pure Zn NPs for 6 h. SOD activity was expressed in terms of U/ml. ( d ) SOD enzyme extract attenuates Zn-doped TiO 2 NPs induced cytotoxicity. Cells were treated with 200 μg/ml of Zn-doped TiO 2 NPs in the presence or absence of SOD enzyme extract. Data represented are mean ± SD of three identical experiments made in three replicate. *Significant difference as compared to the control (p

    Article Snippet: N-acetyl cysteine (NAC), 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazoliumbromide (MTT), 2, 7-dichlorofluorescin diacetate (DCFH-DA), buthionine sulphoximine (BSO), 5,5-dithiobis-(2-nitrobenzoic acid) (DTNB), reduced glutathione (GSH), superoxide dismutase (SOD) and O-phthalaldehyde (OPT) was purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: Western Blot, Negative Control, Software, Activity Assay

    Chemical structures of 3-(2-pyridyl)-5,6-di(2-furyl)-1,2,4-triazine-5′,5″-disulfonic acid disodium salt (ferene: L1) (left) and 3-(2-pyridyl)-5,6-diphenyl-1,2,4-triazine-4′,4″-disulfonic acid sodium salt (ferrozine: L2) (right).

    Journal: Bioinorganic Chemistry and Applications

    Article Title: Synthesis, Characterization, and BSA-Binding Studies of Novel Sulfonated Zinc-Triazine Complexes

    doi: 10.1155/2018/7563820

    Figure Lengend Snippet: Chemical structures of 3-(2-pyridyl)-5,6-di(2-furyl)-1,2,4-triazine-5′,5″-disulfonic acid disodium salt (ferene: L1) (left) and 3-(2-pyridyl)-5,6-diphenyl-1,2,4-triazine-4′,4″-disulfonic acid sodium salt (ferrozine: L2) (right).

    Article Snippet: All chemicals (zinc chloride (3-(2-pyridyl)-5,6-di(2-furyl)-1,2,4-triazine-5′,5″-disulfonic acid disodium salt (ferene/L1) and 3-(2-pyridyl)-5,6-diphenyl-1,2,4-triazine-4′,4″-disulfonic acid sodium salt (ferrozine/L2)), methanol, diethyl ether, ethanol, bovine serum albumin (BSA), tris-HCl buffer (tris(hydroxymethyl)-aminomethane), sodium chloride (NaCl), and analytical grade water) were obtained from Sigma-Aldrich.

    Techniques:

    TEM images of the IO nanostructures obtained in the Lα phase of Triton X-45 in water: ( A , B ) 50 wt % Triton X-45, 1 mmol FeCl 3  (( A ): froth, ( B ): gel); ( C , D ) 50 wt % Triton X-45, 2 mmol FeCl 3  (( C ): froth, ( D ): gel); ( E , F ) 20 wt % Triton X-45, 1 mmol FeCl 3  (( E ): froth, ( F ): gel); ( G , H ) 50 wt % Triton X-45, 1 mmol Fe(acac) 3  (( G ): froth, ( H ): gel).

    Journal: Nanomaterials

    Article Title: Synthesis of Distinct Iron Oxide Nanomaterial Shapes Using Lyotropic Liquid Crystal Solvents

    doi: 10.3390/nano7080211

    Figure Lengend Snippet: TEM images of the IO nanostructures obtained in the Lα phase of Triton X-45 in water: ( A , B ) 50 wt % Triton X-45, 1 mmol FeCl 3 (( A ): froth, ( B ): gel); ( C , D ) 50 wt % Triton X-45, 2 mmol FeCl 3 (( C ): froth, ( D ): gel); ( E , F ) 20 wt % Triton X-45, 1 mmol FeCl 3 (( E ): froth, ( F ): gel); ( G , H ) 50 wt % Triton X-45, 1 mmol Fe(acac) 3 (( G ): froth, ( H ): gel).

    Article Snippet: Materials and Methods Iron(III) chloride hexahydrate (FeCl3 ·6H2 O, 98%), iron(III) acetylacetonate (Fe(acac)3 , 97%,), sodium borohydride (NaBH4 , 98%), cetyltrimethylammonium bromide (CTAB, ≥99%), Triton™ X-100 (laboratory grade), and Triton™ X-45, Brij® C10 were purchased from Sigma-Aldrich (St. Louis, MO, US)and used as such for synthesis.

    Techniques: Transmission Electron Microscopy

    Transmission electron microscopy (TEM) images of previously synthesized IO nanostructures: ( A ) polyhedral nanobricks prepared by co-precipitation of Fe(III)- and Fe(II)-precursors (2:1 ratio) in the LLC phases (lamellar and hexagonal columnar) of Triton X-100 or Triton X-45 in H 2 O [ 46 ]. Using TEM tomography the height of the nanobricks was determined to be ~5 nm. Reproduced from Ref. [ 46 ] with permission from The Royal Society of Chemistry; ( B ) Large nanosheets (lateral dimensions up to several micron) prepared in the Col h  LLC phase formed by Triton X-100 in water using the reduction/hydrolysis method feature heights of 5 or 10 nm (inset shows higher resolution) [ 47 ]. Reproduced from Ref. [ 47 ] with permission from The Royal Society of Chemistry.

    Journal: Nanomaterials

    Article Title: Synthesis of Distinct Iron Oxide Nanomaterial Shapes Using Lyotropic Liquid Crystal Solvents

    doi: 10.3390/nano7080211

    Figure Lengend Snippet: Transmission electron microscopy (TEM) images of previously synthesized IO nanostructures: ( A ) polyhedral nanobricks prepared by co-precipitation of Fe(III)- and Fe(II)-precursors (2:1 ratio) in the LLC phases (lamellar and hexagonal columnar) of Triton X-100 or Triton X-45 in H 2 O [ 46 ]. Using TEM tomography the height of the nanobricks was determined to be ~5 nm. Reproduced from Ref. [ 46 ] with permission from The Royal Society of Chemistry; ( B ) Large nanosheets (lateral dimensions up to several micron) prepared in the Col h LLC phase formed by Triton X-100 in water using the reduction/hydrolysis method feature heights of 5 or 10 nm (inset shows higher resolution) [ 47 ]. Reproduced from Ref. [ 47 ] with permission from The Royal Society of Chemistry.

    Article Snippet: Materials and Methods Iron(III) chloride hexahydrate (FeCl3 ·6H2 O, 98%), iron(III) acetylacetonate (Fe(acac)3 , 97%,), sodium borohydride (NaBH4 , 98%), cetyltrimethylammonium bromide (CTAB, ≥99%), Triton™ X-100 (laboratory grade), and Triton™ X-45, Brij® C10 were purchased from Sigma-Aldrich (St. Louis, MO, US)and used as such for synthesis.

    Techniques: Transmission Assay, Electron Microscopy, Transmission Electron Microscopy, Synthesized

    TEM images of the IO nanostructures obtained in the Lα phase of Triton X-100 in water (70 wt % Triton X-100): the reaction was performed at 3 °C and both gel and froth fraction contain the same product (see images in ( A – C )).

    Journal: Nanomaterials

    Article Title: Synthesis of Distinct Iron Oxide Nanomaterial Shapes Using Lyotropic Liquid Crystal Solvents

    doi: 10.3390/nano7080211

    Figure Lengend Snippet: TEM images of the IO nanostructures obtained in the Lα phase of Triton X-100 in water (70 wt % Triton X-100): the reaction was performed at 3 °C and both gel and froth fraction contain the same product (see images in ( A – C )).

    Article Snippet: Materials and Methods Iron(III) chloride hexahydrate (FeCl3 ·6H2 O, 98%), iron(III) acetylacetonate (Fe(acac)3 , 97%,), sodium borohydride (NaBH4 , 98%), cetyltrimethylammonium bromide (CTAB, ≥99%), Triton™ X-100 (laboratory grade), and Triton™ X-45, Brij® C10 were purchased from Sigma-Aldrich (St. Louis, MO, US)and used as such for synthesis.

    Techniques: Transmission Electron Microscopy

    Tryptophan fluorescence quenching spectra of transferrin (5 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations of Zr-K 1:2 (0–5 µM). The insert shows a plot of F 0 /F versus the POM concentration. (Right) Derived Stern-Volmer plot used to calculate the association constant.

    Journal: Molecules

    Article Title: Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates

    doi: 10.3390/molecules25153472

    Figure Lengend Snippet: Tryptophan fluorescence quenching spectra of transferrin (5 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations of Zr-K 1:2 (0–5 µM). The insert shows a plot of F 0 /F versus the POM concentration. (Right) Derived Stern-Volmer plot used to calculate the association constant.

    Article Snippet: Transferrin, glycine, ammonium persulfate, tetramethylammonium chloride, tetrabutylammonium hydroxide, zirconyl chloride octahydrate, zirconium(IV) chloride, sodium phosphate dibasic and deuterium oxide were bought from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques: Fluorescence, Concentration Assay, Derivative Assay

    31 P-NMR of Zr-WD 1:2 (2 mM) incubated in the presence of transferrin (20 µM) in phosphate buffer (10 mM, pH 7.4) at 60 °C. Incubation times are shown in the figure. The Zr-WD 1:2 structure (−14.11 and −9.548 ppm) remains largely stable over time.

    Journal: Molecules

    Article Title: Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates

    doi: 10.3390/molecules25153472

    Figure Lengend Snippet: 31 P-NMR of Zr-WD 1:2 (2 mM) incubated in the presence of transferrin (20 µM) in phosphate buffer (10 mM, pH 7.4) at 60 °C. Incubation times are shown in the figure. The Zr-WD 1:2 structure (−14.11 and −9.548 ppm) remains largely stable over time.

    Article Snippet: Transferrin, glycine, ammonium persulfate, tetramethylammonium chloride, tetrabutylammonium hydroxide, zirconyl chloride octahydrate, zirconium(IV) chloride, sodium phosphate dibasic and deuterium oxide were bought from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques: Nuclear Magnetic Resonance, Incubation

    SDS-Page gel featuring intact transferrin (lane 1), transferrin incubated in phosphate buffer (lanes 2–3), and transferrin incubated in buffer solutions containing different metal-substituted POMs (lanes 5–10). The samples in this gel were incubated for 3 days.

    Journal: Molecules

    Article Title: Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates

    doi: 10.3390/molecules25153472

    Figure Lengend Snippet: SDS-Page gel featuring intact transferrin (lane 1), transferrin incubated in phosphate buffer (lanes 2–3), and transferrin incubated in buffer solutions containing different metal-substituted POMs (lanes 5–10). The samples in this gel were incubated for 3 days.

    Article Snippet: Transferrin, glycine, ammonium persulfate, tetramethylammonium chloride, tetrabutylammonium hydroxide, zirconyl chloride octahydrate, zirconium(IV) chloride, sodium phosphate dibasic and deuterium oxide were bought from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques: SDS Page, Incubation

    CD spectra of transferrin (7 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations (0–10 µM) of Zr-WD 1:2 .

    Journal: Molecules

    Article Title: Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates

    doi: 10.3390/molecules25153472

    Figure Lengend Snippet: CD spectra of transferrin (7 µM) in phosphate buffer (10 mM, pH 7.4) with increasing concentrations (0–10 µM) of Zr-WD 1:2 .

    Article Snippet: Transferrin, glycine, ammonium persulfate, tetramethylammonium chloride, tetrabutylammonium hydroxide, zirconyl chloride octahydrate, zirconium(IV) chloride, sodium phosphate dibasic and deuterium oxide were bought from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques:

    SDS-Page gel featuring intact transferrin (lane 1), transferrin incubated in phosphate buffer (lanes 2–3), and transferrin incubated in buffer solutions containing control samples. The samples were incubated for 7 days.

    Journal: Molecules

    Article Title: Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates

    doi: 10.3390/molecules25153472

    Figure Lengend Snippet: SDS-Page gel featuring intact transferrin (lane 1), transferrin incubated in phosphate buffer (lanes 2–3), and transferrin incubated in buffer solutions containing control samples. The samples were incubated for 7 days.

    Article Snippet: Transferrin, glycine, ammonium persulfate, tetramethylammonium chloride, tetrabutylammonium hydroxide, zirconyl chloride octahydrate, zirconium(IV) chloride, sodium phosphate dibasic and deuterium oxide were bought from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques: SDS Page, Incubation

    Sofosbuvir

    Journal: World Journal of Hepatology

    Article Title: Psychiatric and substance use disorders co-morbidities and hepatitis C: Diagnostic and treatment implications

    doi: 10.4254/wjh.v7.i15.1921

    Figure Lengend Snippet: Sofosbuvir

    Article Snippet: Sofosbuvir and ledipasvir fi xed-dose combination with and without ribavirin in treatment-naive and previously treated patients with genotype 1 hepatitis C virus infection (LONESTAR): an open-label, randomized, phase 2 trial.

    Techniques:

    Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in calcein release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles

    Journal: Biomaterials

    Article Title: The manipulation of natural killer cells to target tumor sites using magnetic nanoparticles

    doi: 10.1016/j.biomaterials.2012.04.041

    Figure Lengend Snippet: Cytotoxicity assays. (a) NK-92MI cells (effector, E) were the transfected with nanoparticles (0, 5, and 20 μg Fe/mL) and then cytotoxicity was tested in calcein release assays using RPMI8226 cells (target, T) with different ratios of E. (b) Nanoparticles

    Article Snippet: One microliter of 10 mM calcein-AM solution (Invitrogen, C1430) was added to 106 target cells in 2 mL RPMI-1640/10% fetal bovine serum (FBS) and incubated at 37 °C in 5% CO2 for 60 min. Target cells were then washed twice with RPMI-1640/10% FBS and resuspended in the same medium.

    Techniques: Transfection

    Endocrine cell formation requires LSD1 activity during a short window in early pancreatic development. a Schematic of the human embryonic stem cell (hESC) differentiation protocol to the endocrine cell stage (EN) and experimental plan for LSD1 inhibition. b Immunofluorescent staining for pancreatic hormones insulin (INS), glucagon (GCG) and somatostatin (SST) or PDX1 and NKX6.1 in control EN cells compared to EN cells with early (LSD1i early ) and late (LSD1i late ) LSD1 inhibition (representative images, n = 10 independent differentiations). Scale bar, 50 µm. c qRT-PCR analysis for INS , GCG and SST in control, LSD1i early and LSD1i late EN cells. Data are shown as mean ± S.E.M. ( n = 3 replicates from independent differentiations with n = 3 technical replicates per sample; source data are provided as a Source Data file). P = 7.93 e−4, 1.42 e−2, 2.32 e−4, 8.71 e−4, 3.5 e−2, and 1.52 e−3, respectively, Student’s t -test, 2 sided. d Flow cytometry analysis at EN stage for NKX6.1, PDX1 and INS comparing control, LSD1i early and LSD1i late cells. Isotype control for each antibody is shown in red and target protein staining in green. Percentage of cells expressing each protein is indicated (representative experiment, n = 2 independent differentiations). D, day; AA, activin A; ITS, insulin-transferrin-selenium; TGFBi, TGFβ R1 kinase inhibitor; KC, KAAD-cyclopamine; KGF, keratinocyte growth factor; RA, retinoic acid; EGF, epidermal growth factor; ES, human embryonic stem cells; DE, definitive endoderm; GT, primitive gut tube; PP1, early pancreatic progenitors; PP2, late pancreatic progenitors; EN, endocrine cell stage; FSC-A, forward scatter area.

    Journal: Nature Communications

    Article Title: LSD1-mediated enhancer silencing attenuates retinoic acid signalling during pancreatic endocrine cell development

    doi: 10.1038/s41467-020-16017-x

    Figure Lengend Snippet: Endocrine cell formation requires LSD1 activity during a short window in early pancreatic development. a Schematic of the human embryonic stem cell (hESC) differentiation protocol to the endocrine cell stage (EN) and experimental plan for LSD1 inhibition. b Immunofluorescent staining for pancreatic hormones insulin (INS), glucagon (GCG) and somatostatin (SST) or PDX1 and NKX6.1 in control EN cells compared to EN cells with early (LSD1i early ) and late (LSD1i late ) LSD1 inhibition (representative images, n = 10 independent differentiations). Scale bar, 50 µm. c qRT-PCR analysis for INS , GCG and SST in control, LSD1i early and LSD1i late EN cells. Data are shown as mean ± S.E.M. ( n = 3 replicates from independent differentiations with n = 3 technical replicates per sample; source data are provided as a Source Data file). P = 7.93 e−4, 1.42 e−2, 2.32 e−4, 8.71 e−4, 3.5 e−2, and 1.52 e−3, respectively, Student’s t -test, 2 sided. d Flow cytometry analysis at EN stage for NKX6.1, PDX1 and INS comparing control, LSD1i early and LSD1i late cells. Isotype control for each antibody is shown in red and target protein staining in green. Percentage of cells expressing each protein is indicated (representative experiment, n = 2 independent differentiations). D, day; AA, activin A; ITS, insulin-transferrin-selenium; TGFBi, TGFβ R1 kinase inhibitor; KC, KAAD-cyclopamine; KGF, keratinocyte growth factor; RA, retinoic acid; EGF, epidermal growth factor; ES, human embryonic stem cells; DE, definitive endoderm; GT, primitive gut tube; PP1, early pancreatic progenitors; PP2, late pancreatic progenitors; EN, endocrine cell stage; FSC-A, forward scatter area.

    Article Snippet: Other added components included FBS (HyClone), B-27® supplement (Life Technologies), Insulin-Transferrin-Selenium (ITS; Life Technologies), TGFβ R1 kinase inhibitor IV (EMD Bioscience), KAAD-Cyclopamine (KC; Toronto Research Chemicals), and the retinoic receptor agonist TTNPB (RA; Sigma Aldrich).

    Techniques: Activity Assay, Inhibition, Staining, Quantitative RT-PCR, Flow Cytometry, Expressing

    Zinc inhibits IFN-λ3:IFNLR1 binding. ( a ) To ascertain the cellular location of zinc inhibition following ZnSO 4 treatment, Huh-7 cells were pre-treated for 24 h with 50 μM ZnSO 4 , washed thoroughly, and then treated with IFN-λ3 ±50 μM ZnSO 4 for 15 min. STAT1 phosphorylation was significantly inhibited only when IFN-λ3 was administered in the presence of zinc, suggesting that zinc inhibits IFN-λ3 signalling at the receptor. ( b ) To identify cytokine zinc binding, 200 ng of IFN-α or IFN-λ3 were added to a zinc loaded IMAC-affinity resin for 2 h, after which bound protein was examined by SDS–PAGE. Dimeric forms of IFN-α and IFN-λ3 bound the zinc resin, as did monomeric IFN-λ3. ( c ) Using protein G beads, Co-IP was performed on Huh-7 cell lysates using recombinant IFN-λ3 alone or with the addition of 50 μM ZnSO 4 . Co-IP of both IFN-λ3 (66% reduction) and IFNLR1 (40% reduction) was reduced in the presence of zinc, when IFNLR1 and IFN-λ3 were immunoprecipitated respectively, demonstrating a direct inhibition of receptor:cytokine interaction by zinc. ( d ) Co-IP studies were confirmed using proximity ligation assays to examine the interaction of IFN-λ3 and IFNLR1 in the presence of zinc in situ . Confocal microscopy of IFN-λ3 treated Huh-7 cells demonstrated a reduction in fluorescent signals (red fluorescent spots), indicative of IFNLR1:IFN-λ3 interaction (within 40 nm). No signal was observed within the negative control assay lacking the primary IFN-λ3 antibody (1° Ab) or lacking the addition of IFN-λ3. ( e ) Proximity ligation signals per cell were quantified using ImageJ software, demonstrating a 50% decrease in IFNLR1:IFN-λ3 interactions per cell (Mann–Whitney test). ( d ) Scale bars, 10 μm. Data are representative of two independent experiments, *** P

    Journal: Nature Communications

    Article Title: Zinc is a potent and specific inhibitor of IFN-λ3 signalling

    doi: 10.1038/ncomms15245

    Figure Lengend Snippet: Zinc inhibits IFN-λ3:IFNLR1 binding. ( a ) To ascertain the cellular location of zinc inhibition following ZnSO 4 treatment, Huh-7 cells were pre-treated for 24 h with 50 μM ZnSO 4 , washed thoroughly, and then treated with IFN-λ3 ±50 μM ZnSO 4 for 15 min. STAT1 phosphorylation was significantly inhibited only when IFN-λ3 was administered in the presence of zinc, suggesting that zinc inhibits IFN-λ3 signalling at the receptor. ( b ) To identify cytokine zinc binding, 200 ng of IFN-α or IFN-λ3 were added to a zinc loaded IMAC-affinity resin for 2 h, after which bound protein was examined by SDS–PAGE. Dimeric forms of IFN-α and IFN-λ3 bound the zinc resin, as did monomeric IFN-λ3. ( c ) Using protein G beads, Co-IP was performed on Huh-7 cell lysates using recombinant IFN-λ3 alone or with the addition of 50 μM ZnSO 4 . Co-IP of both IFN-λ3 (66% reduction) and IFNLR1 (40% reduction) was reduced in the presence of zinc, when IFNLR1 and IFN-λ3 were immunoprecipitated respectively, demonstrating a direct inhibition of receptor:cytokine interaction by zinc. ( d ) Co-IP studies were confirmed using proximity ligation assays to examine the interaction of IFN-λ3 and IFNLR1 in the presence of zinc in situ . Confocal microscopy of IFN-λ3 treated Huh-7 cells demonstrated a reduction in fluorescent signals (red fluorescent spots), indicative of IFNLR1:IFN-λ3 interaction (within 40 nm). No signal was observed within the negative control assay lacking the primary IFN-λ3 antibody (1° Ab) or lacking the addition of IFN-λ3. ( e ) Proximity ligation signals per cell were quantified using ImageJ software, demonstrating a 50% decrease in IFNLR1:IFN-λ3 interactions per cell (Mann–Whitney test). ( d ) Scale bars, 10 μm. Data are representative of two independent experiments, *** P

    Article Snippet: Zinc binding assays To examine the ability of IFN-α or IFN-λ3 to bind zinc, IMAC-Select affinity gel (Sigma-Aldrich) was used according to the manufacturer's instructions.

    Techniques: Binding Assay, Inhibition, SDS Page, Co-Immunoprecipitation Assay, Recombinant, Immunoprecipitation, Ligation, In Situ, Confocal Microscopy, Negative Control, Software, MANN-WHITNEY

    Relationship between total Sunshine payment amount and total Medicare reimbursement for degarelix and denosumab. Scatter plot of total Sunshine payment amount vs. total Medicare reimbursement in the log scale. Red line represents fitted linear prediction.

    Journal: Urology practice

    Article Title: The Relationship of Industry Payments to Prescribing Behavior: A Study of Degarelix and Denosumab

    doi: 10.1016/j.urpr.2016.03.007

    Figure Lengend Snippet: Relationship between total Sunshine payment amount and total Medicare reimbursement for degarelix and denosumab. Scatter plot of total Sunshine payment amount vs. total Medicare reimbursement in the log scale. Red line represents fitted linear prediction.

    Article Snippet: Degarelix, a gonadotropin-releasing hormone (GnRH) antagonist manufactured by Ferring Pharmaceuticals, was U.S. Food and Drug Administration (FDA) approved in 2008 for the treatment of advanced prostate cancer.

    Techniques:

    Real-time polymerase chain reaction expression of manganese superoxide dismutase in HLE-B3 cells. HLE-B3 cells were incubated with 1 μM 17β-E 2 for 0, 1.5, 3, 6, 12, and 24 h. The expression of MnSOD mRNA was analyzed by quantitative real-time PCR. According to the two-way ANOVA, there were no statistically significant changes in MnSOD mRNA at any time point after estrogen treatment compared to the control (untreated). Data are expressed as mean±SD values. p

    Journal: Molecular Vision

    Article Title: Mitochondrial superoxide dismutase activation with 17 ?-estradiol-treated human lens epithelial cells

    doi:

    Figure Lengend Snippet: Real-time polymerase chain reaction expression of manganese superoxide dismutase in HLE-B3 cells. HLE-B3 cells were incubated with 1 μM 17β-E 2 for 0, 1.5, 3, 6, 12, and 24 h. The expression of MnSOD mRNA was analyzed by quantitative real-time PCR. According to the two-way ANOVA, there were no statistically significant changes in MnSOD mRNA at any time point after estrogen treatment compared to the control (untreated). Data are expressed as mean±SD values. p

    Article Snippet: The supernatant was evaluated for MnSOD activity evaluation using a Superoxide Dismutase Assay kit (#706002; Cayman Chemicals Inc., Ann Arbor, MI) according to the manufacturer's protocol.

    Techniques: Real-time Polymerase Chain Reaction, Expressing, Incubation

    Reverse transcriptase polymerase chain reaction expression of manganese superoxide dismutase in HLE-B3 cells. Total RNA was extracted from confluent HLE-B3 cells and subjected to RT–PCR for MnSOD. The cDNA product yielded one band at the correct predicted molecular weight (199 bp). The authenticity of PCR products was verified by DNA sequencing and a BLAST search of the sequence (refer to Methods).

    Journal: Molecular Vision

    Article Title: Mitochondrial superoxide dismutase activation with 17 ?-estradiol-treated human lens epithelial cells

    doi:

    Figure Lengend Snippet: Reverse transcriptase polymerase chain reaction expression of manganese superoxide dismutase in HLE-B3 cells. Total RNA was extracted from confluent HLE-B3 cells and subjected to RT–PCR for MnSOD. The cDNA product yielded one band at the correct predicted molecular weight (199 bp). The authenticity of PCR products was verified by DNA sequencing and a BLAST search of the sequence (refer to Methods).

    Article Snippet: The supernatant was evaluated for MnSOD activity evaluation using a Superoxide Dismutase Assay kit (#706002; Cayman Chemicals Inc., Ann Arbor, MI) according to the manufacturer's protocol.

    Techniques: Polymerase Chain Reaction, Expressing, Reverse Transcription Polymerase Chain Reaction, Molecular Weight, DNA Sequencing, Sequencing

    Western blot analysis of manganese superoxide dismutase expression in HLE-B3 cells. Total cell lysates were collected from HLE-B3 cells grown in 0.5% serum and stimulated by exposure to 1 μM 17β-E 2 for 0, 1.5, 3, 6, 12, and 24 h. There was no change in the expression of MnSOD at any of the time points. The time points at 0 and 24* hours did not receive estrogen.

    Journal: Molecular Vision

    Article Title: Mitochondrial superoxide dismutase activation with 17 ?-estradiol-treated human lens epithelial cells

    doi:

    Figure Lengend Snippet: Western blot analysis of manganese superoxide dismutase expression in HLE-B3 cells. Total cell lysates were collected from HLE-B3 cells grown in 0.5% serum and stimulated by exposure to 1 μM 17β-E 2 for 0, 1.5, 3, 6, 12, and 24 h. There was no change in the expression of MnSOD at any of the time points. The time points at 0 and 24* hours did not receive estrogen.

    Article Snippet: The supernatant was evaluated for MnSOD activity evaluation using a Superoxide Dismutase Assay kit (#706002; Cayman Chemicals Inc., Ann Arbor, MI) according to the manufacturer's protocol.

    Techniques: Western Blot, Expressing