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  • 99
    Millipore dimethyl sulfoxide dmso
    N-cadherin homotypic binding promotes α3β4-myc nAChRs localization at the edges of the cell-cell contact. A) Schematic drawing of two contacting cells showing the areas of the cell surface in which α3β4-myc nAChRs and N-cadherin pixel area was measured in 2×2 µm regions placed at the center (red) and at each of the edges of the cell-cell contact (orange). The average of the two measurements of the edges was used for analysis, and the sum of the measurements at the center and edges at the cell-cell contact was considered 100%. B) Analysis of the percentage of α3β4-myc nAChRs pixel area distribution between the center and the edges of cell-cell contacts in cell junctions mediated by mEGFP (n = 24), N-cadherin (n = 22), N-cadherin-Δ-β-catenin (n = 25), and N-cadherin-Δ-cyto (n = 27). C) Analysis of the effect of inhibitors of actin polymerization <t>(LAT-A</t> 10 µM, n = 21; and CTCH-D 2 µM, n = 16), RhoA (RhoA Inh 1 µg/ml, n = 21), and ROCK (Y27632 10 µM, n = 21) on α3β4-myc nAChRs density at the contact and edges of N-cadherin-mediated cell-cell contacts. Cells treated with <t>DMSO</t> (10 µl/ml, n = 20) were used as controls. D) Analysis of the percentage distribution of N-cadherin and N-cadherin-deleted proteins between the cell-cell contact and the edges of contact zone. E) Analysis of the effect of DMSO, LAT-A, CTCH-D, RhoA Inh, and Y27632 on N-cadherin density at the contact zone and at the edges of cell-cell contacts. Values in B, C, D, and E represent the mean ± SEM of each experimental group. One-way ANOVA of pixel density in cell-cell contacts and the edges of the contact in B and C, p
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    Cell Signaling Technology Inc dimethyl sulfoxide dmso
    Reactivity of nAbs and non-nAbs to HIV-1 Env on the surface of latently infected T cells after provirus reactivation. ACH-2 cells were incubated with <t>PMA</t> (10 ng/ml) plus ionomycin (1 μg/ml) or <t>DMSO</t> for 24 h. Supernatants were subjected to HIV-1
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    Amresco dimethyl sulfoxide dmso
    ME1 and 6PGD formed hetero-oligomers to promote 6PGD enzymatic activity. A , lysates from U2OS cells transfected with ME1 siRNA or control siRNA were treated with <t>DMSO</t> or the cross-linker DSS. Cell lysates were then prepared and analyzed by Western blotting. B , lysates from U2OS cells stably expressing ME1 or control vector were treated with DMSO or DSS. The mixtures were subjected to Western blotting analysis. C , 293T cells were transfected with GST-6PGD and <t>FLAG-ME1</t> as indicated. Cell lysates were treated with DMSO or DSS, and analyzed by Western blotting. D , malic enzyme activity of purified FLAG-ME1 after being incubated with His peptide or His-6PGD proteins at different mole ratio as indicated ( top ). The protein expression was visualized by Coomassie Blue staining ( bottom ). Data are the means ± S.D. ( n = 3 independent experiments). E , activity of purified wild-type FLAG-6PGD, FLAG-6PGD mut1 (G10I, L11N, A12K, V13K, M14K, G15I), or FLAG-6PGD mut2 (H187N and D188L) protein in presence or absence of ME1 protein ( top ). Protein expression was analyzed by Coomassie Blue staining ( bottom ). Data are the means ± S.D. ( n = 3 independent experiments). F , 293T cells were transfected with FLAG-ME1 and eGFP-6PGD, eGFP-6PGD mut1 , or eGFP-6PGD mut2 as indicated. Cell lysates were immunoprecipitated with anti-FLAG antibody. Input and immunoprecipitates were analyzed by Western blotting. G , 293T cells were transfected with FLAG-ME1 and eGFP-6PGD, eGFP-6PGD K76R , or eGFP-6PGD K294R as indicated. Cell lysates were immunoprecipitated with anti-FLAG antibody and analyzed by Western blotting. H , purified FLAG-6PGD, FLAG-6PGD K76R , and FLAG-6PGD K294R proteins were incubated with either FLAG-ME1 or FLAG peptide as indicated. 6PGD activity was measured ( top ), and purified proteins were analyzed by Coomassie Blue staining ( bottom ). All results are representative of three independent experiments.
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    Avantor dimethyl sulfoxide dmso
    Controlling TC-83 induced ROS response in microglial cells decreases inflammatory burden. (a) Experimental workflow indicating HMC3 cells were pre-treated for 2h with 0.1% <t>DMSO,</t> 1μM BAY 11–7082 (BAY-82), or 100pM <t>mitoquinone</t> mesylate (MitoQ) prior to inoculation with TC-83 (MOI:2). Levels of the pro-inflammatory cytokines (b) IL-1α, (c) IL-1β, (d), IL-6 and (e) IL-8 produced by HMC3 cells as the direct result of TC-83 infection were measured at 1, 2, and 6hpi. The quantitative data are depicted as the means of three biologically independent experiments ± SD. * p
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    Duchefa dimethyl sulfoxide dmso
    Controlling TC-83 induced ROS response in microglial cells decreases inflammatory burden. (a) Experimental workflow indicating HMC3 cells were pre-treated for 2h with 0.1% <t>DMSO,</t> 1μM BAY 11–7082 (BAY-82), or 100pM <t>mitoquinone</t> mesylate (MitoQ) prior to inoculation with TC-83 (MOI:2). Levels of the pro-inflammatory cytokines (b) IL-1α, (c) IL-1β, (d), IL-6 and (e) IL-8 produced by HMC3 cells as the direct result of TC-83 infection were measured at 1, 2, and 6hpi. The quantitative data are depicted as the means of three biologically independent experiments ± SD. * p
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    Fisher Scientific dimethyl sulfoxide dmso
    Comparison of <t>CFZ</t> and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and <t>DMSO</t> (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.
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    J&K Scientific dimethyl sulfoxide dmso
    Comparison of <t>CFZ</t> and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and <t>DMSO</t> (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.
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    Merck & Co dimethyl sulfoxide dmso
    The combination of <t>LCRF‐0006</t> and bortezomib synergistically increases MM tumor response in vivo. A, Schematic representation of treatment regimen. C57BL/KaLwRij mice with established MM (day 14 post‐5TGM1 cell injection) were treated with LCRF‐0006 (100 mg/kg) and bortezomib (0.5 mg/kg) (LCRF‐0006 + bortezomib), LCRF‐0006 and <t>DMSO</t> vehicle (LCRF‐0006), 2‐HP‐b‐CD vehicle and bortezomib (bortezomib) or 2‐HP‐b‐CD and DMSO vehicles (vehicles) i.p., as per treatment regimen. B, Tumor burden was assessed at day 14, 21 and 28 by BLI. Graph depicts mean ± SEM. n = 5‐6 mice/treatment group. *** P
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    Merck KGaA dimethyl sulfoxide dmso
    SEM image of PVA nanofiber (a) before and after solvent vapor treatment with (b) <t>DMF,</t> (c) methanol, and (d) <t>DMSO</t> at a temperature of 40 °C for 8 h, and (e) Young's modulus and tensile strength of PVA nanofiber mats with various solvent types at a temperature of 40 °C for 4 h.
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    Nacalai dimethyl sulfoxide dmso
    Effects of <t>S42</t> or DHT on atrogin1, MuRF1 , Igf1 expression on C2C12 myotubes. C2C12 myotubes were incubated with 1–10 µM of S42 or 100 nM of DHT or appropriate vehicle <t>(DMSO)</t> for 24 h. (A), (B), (C) Comparison of mRNA expression levels of atrogin1 , MuRF1 and Igf1 relative to those of Gapdh , respectively are shown. Data are expressed as mean ± SE of triplicate samples. In statistical comparisons, the data of treated groups with DHT or S42 were compared with that of untreated group. *P
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    Thermo Fisher dimethyl sulfoxide dmso
    Inhibition of <t>TMZ-induced</t> G2 arrest by Rsv leads to mitotic catastrophe. U87 cells were treated with Rsv 30 μM, TMZ 100 μM or RT for 24, 38 and 48 h, followed by fixation and DAPI staining. (A) representative images of nuclei from cells treated with <t>DMSO</t> (control), Rsv for 38 h or RT for 48 h. Double arrows point to fragmented/irregular nuclei; single arrow points to micronuclei; double arrowheads point to enlarged nuclei; Scale bar: 6 μm; (B) representative visible and fluorescent images of nuclei from untreated cells showing a normal mitosis (i and ii) ; an abnormal chromosome condensation and mitosis, with cellular enlargement, in a cell treated with RT for 48 h (iii and iv) ; and a triple mitosis in a cell treated with Rsv for 48 h (v and vi) and. Scale bar: 10 μm; (C) direct counting of the percentage of nuclei presenting normal (top), irregular (mid) or large phenotype (bottom); *p
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    FUJIFILM dimethyl sulfoxide dmso
    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, <t>DEX,</t> and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and <t>DMSO</t> were assigned a value of 1.
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    Sangon Biotech dimethyl sulfoxide dmso
    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, <t>DEX,</t> and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and <t>DMSO</t> were assigned a value of 1.
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    Finar Limited dimethyl sulfoxide dmso
    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, <t>DEX,</t> and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and <t>DMSO</t> were assigned a value of 1.
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    Kanto Chemical dimethyl sulfoxide dmso
    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, <t>DEX,</t> and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and <t>DMSO</t> were assigned a value of 1.
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    Tedia dimethyl sulfoxide dmso
    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, <t>DEX,</t> and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and <t>DMSO</t> were assigned a value of 1.
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    AG Scientific dimethyl sulfoxide dmso
    PLK1 phosphorylates BEX4 and regulates its subcellular localization during mitosis. a HeLa cells were transfected with shLuc, shBEX4, shCDK1, or shPLK1 and cultured in the presence of nocodazole (200 ng/ml) for 16 h. The cells were collected by shake-off, then lysed and immunoblotted with anti-PLK1, anti-CDK1, anti-BEX4, and anti-β-actin. Expression levels relative to respective controls are shown below the blots. b HeLa cells were transfected with control shLuc or PLK1-targeting shRNA, cultured on coverslips for 24 h and stained with anti-aurora A (Aur A), anti-BEX4, and DAPI. The metaphase cells were then analyzed. Scale bars represent 5 μm. c HeLa cells were cultured on coverslips for 24 h, then treated with BI2536 (300 nmol/l; a selective PLK1 inhibitor) or <t>DMSO</t> as the control. At 2 h post-treatment, the cells were fixed with 4% paraformaldehyde and stained with anti-BEX4 and anti-aurora A (Aur A) antibodies. DNA was visualized by DAPI staining. The insets show magnified images of centrosomes. Scale bars represent 5 μm. d HeLa cells were transfected with shLuc or shPLK1. At 36 h after transfection, the cells were treated with cycloheximide (CHX) for the indicated times and then subjected to immunoblotting with anti-BEX4, anti-PLK1, and anti-actin antibodies. e , f All serine (S) and threonine (T) residues in human BEX4 protein. HeLa cells were transfected with GFP-fused BEX4 mutant constructs with serine and/or threonine substituted with alanine (S3A, T29A, S35A, T94A, or T107A), or a BEX4 wild-type construct. The expression of each BEX4 expression construct was analyzed by immunoblotting using anti-GFP, anti-BEX4, and anti-actin antibodies ( e ). Cells were fixed with 4% paraformaldehyde and stained with anti-GFP and anti-aurora A (Aur A) antibodies. DNA was visualized by DAPI staining ( f ). The insets show magnified images of the centrosomes. Scale bars represent 5 μm
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    HiMedia Laboratories dimethyl sulfoxide dmso
    The in-vitro cytotoxicity of different NPs measured by <t>MTT</t> assay. (a) The cytotoxic effect of AgFeO 2 (Bio) and FeO 2 NPs synthesised by green co-reduction using A. blitum leaves extract and AgFeO 2 (Che) and FeO 2 NPs synthesised by chemical co-reduction precipitation method using NaBH 4 on non-cancerous human embryonic kidney cell lines (HEK 293 T) after 24 h of treatment were evaluated by mitochondrial activity using the MTT assay. The bar graph represents the mean value of three replicates where cells were treated 20 μg of NPs and cells treated with 10% <t>DMSO</t> were considered as control. (b) HEK 293 T cells treated with different NPs after 24 h incubation. HEK 293 T cells untreated (left panel) and the cells treated with 20 μg of Ag-FeO 2 (middle panel) and with 20 μg of FeO 2 (right panel). Magnification: 20 × . One-way ANOVAs were performed to evaluate significance comparing the both NPs to the control. A value of p
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    Valiant dimethyl sulfoxide dmso
    HDACs regulate the DNA damage response MCF-7 cells were treated with vehicle <t>(DMSO)</t> or vorinostat (Vor.) for 48 hours before adding <t>epirubicin</t> (0.5 μM) for an additional 0-8 hours. Total cell lysate was processed for western blotting examining the activation and stabilization of p53 due to increasing lengths of exposure to epirubicin (A.), and the concentration effect of vorinostat (B.). (C.) Cells grown on glass coverslips were treated as in (A.) before fixation, and immunofluorescence imaging of FITC-p53 and DAPI (D.). (E.) Cells treated as in (A.) were analyzed for induction of p21 and acetylation of histone H4 by western blotting. (E.) Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) analysis for the induction of GADD45A and RRM2B normalized to β-glucuronidase ( h.Gus ) for total RNA in cells treated as in (A). (*p
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    Applichem dimethyl sulfoxide dmso
    Effect of testosterone on probasin, Oat1- and Oat3-promoter activity. OK cells were either transfected with pSG5 or <t>pSG5-rAR,</t> and rAR expression and cellular localization were analyzed using immunofluorescence staining (green color rAR, blue color DAPI staining; excitation wavelength 488 nm and 365 nm) (1A). Promoter constructs of rat probasin, Oat1 and Oat3, and the expression vector for rAR were transiently transfected into OK cells (1B and 1C). Cells were cultured 43 h with either 100 nM testosterone (black bars) or with 0.0003% <t>DMSO</t> as control (white bars) (1B and 1C). Luciferase activity was measured and firefly luciferase was normalized to Renilla luciferase. Data are reported as the fold increase presented as mean ± S.E.M.; n = 4; n.s.: not significant; ***: p
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    Accustandard Inc dimethyl sulfoxide dmso
    <t>TCDD-induced</t> binding of AHR to putative DRE sites in PTPN6 promoter Nuclear protein was isolated from HepG2 cells treated with vehicle (VH, 0.01% <t>DMSO)</t> or TCDD (T, 30nM), incubated with 32 P -labeled A) or unlabeled B) consensus DRE and four DRE oligomers in PTPN6 promoter (indicated by the position relative to transcription start site). A) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, dried and autoradiographed. B) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, transferred to nitrocellulose, and probed with anti-AHR antibody. Arrow indicates specific binding of AHR to DRE oligomers. Results are representative of more than two independent experiments.
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    Junsei Chemical dimethyl sulfoxide dmso
    <t>TCDD-induced</t> binding of AHR to putative DRE sites in PTPN6 promoter Nuclear protein was isolated from HepG2 cells treated with vehicle (VH, 0.01% <t>DMSO)</t> or TCDD (T, 30nM), incubated with 32 P -labeled A) or unlabeled B) consensus DRE and four DRE oligomers in PTPN6 promoter (indicated by the position relative to transcription start site). A) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, dried and autoradiographed. B) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, transferred to nitrocellulose, and probed with anti-AHR antibody. Arrow indicates specific binding of AHR to DRE oligomers. Results are representative of more than two independent experiments.
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    Carl Roth GmbH dimethyl sulfoxide dmso
    ( A ) SEC elugram of <t>AMCA-PLGA;</t> the black line indicates the refractive index of the PLGA expressed as relative units (RIU), and the gray line indicates the ultraviolet absorption by AMCA at 350 nm expressed as relative milli-units (mAU). ( B ) Stability studies via fluorescence intensity measurements of AMCA-PLGA in <t>DMSO</t> for > 120 hours at 4°C (solid line, crosses), 20°C (dotted line, triangles) and 37°C (broken line, circles). Data are expressed as ratios of I/I 0 and shown as the mean ± SD of three independent experiments. Abbreviations: AMCA-PLGA, 7-amino-4-methyl-3-coumarinylacetic acid-poly( d,l -lactide-co-glycolide); DMSO, dimethyl sulfoxide; mAU, milli-absorption unit; PLGA, poly( d,l -lactide-co-glycolide); RIU, refractive index unit; SD, standard deviation; SEC, size exclusion chromatography.
    Dimethyl Sulfoxide Dmso, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 92/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    EM Science Inc dimethyl sulfoxide dmso
    ( A ) SEC elugram of <t>AMCA-PLGA;</t> the black line indicates the refractive index of the PLGA expressed as relative units (RIU), and the gray line indicates the ultraviolet absorption by AMCA at 350 nm expressed as relative milli-units (mAU). ( B ) Stability studies via fluorescence intensity measurements of AMCA-PLGA in <t>DMSO</t> for > 120 hours at 4°C (solid line, crosses), 20°C (dotted line, triangles) and 37°C (broken line, circles). Data are expressed as ratios of I/I 0 and shown as the mean ± SD of three independent experiments. Abbreviations: AMCA-PLGA, 7-amino-4-methyl-3-coumarinylacetic acid-poly( d,l -lactide-co-glycolide); DMSO, dimethyl sulfoxide; mAU, milli-absorption unit; PLGA, poly( d,l -lactide-co-glycolide); RIU, refractive index unit; SD, standard deviation; SEC, size exclusion chromatography.
    Dimethyl Sulfoxide Dmso, supplied by EM Science Inc, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    dimethyl sulfoxide dmso - by Bioz Stars, 2020-08
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    Fisher Bioreagents dimethyl sulfoxide dmso
    ( A ) SEC elugram of <t>AMCA-PLGA;</t> the black line indicates the refractive index of the PLGA expressed as relative units (RIU), and the gray line indicates the ultraviolet absorption by AMCA at 350 nm expressed as relative milli-units (mAU). ( B ) Stability studies via fluorescence intensity measurements of AMCA-PLGA in <t>DMSO</t> for > 120 hours at 4°C (solid line, crosses), 20°C (dotted line, triangles) and 37°C (broken line, circles). Data are expressed as ratios of I/I 0 and shown as the mean ± SD of three independent experiments. Abbreviations: AMCA-PLGA, 7-amino-4-methyl-3-coumarinylacetic acid-poly( d,l -lactide-co-glycolide); DMSO, dimethyl sulfoxide; mAU, milli-absorption unit; PLGA, poly( d,l -lactide-co-glycolide); RIU, refractive index unit; SD, standard deviation; SEC, size exclusion chromatography.
    Dimethyl Sulfoxide Dmso, supplied by Fisher Bioreagents, used in various techniques. Bioz Stars score: 92/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dimethyl sulfoxide dmso/product/Fisher Bioreagents
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    Image Search Results


    N-cadherin homotypic binding promotes α3β4-myc nAChRs localization at the edges of the cell-cell contact. A) Schematic drawing of two contacting cells showing the areas of the cell surface in which α3β4-myc nAChRs and N-cadherin pixel area was measured in 2×2 µm regions placed at the center (red) and at each of the edges of the cell-cell contact (orange). The average of the two measurements of the edges was used for analysis, and the sum of the measurements at the center and edges at the cell-cell contact was considered 100%. B) Analysis of the percentage of α3β4-myc nAChRs pixel area distribution between the center and the edges of cell-cell contacts in cell junctions mediated by mEGFP (n = 24), N-cadherin (n = 22), N-cadherin-Δ-β-catenin (n = 25), and N-cadherin-Δ-cyto (n = 27). C) Analysis of the effect of inhibitors of actin polymerization (LAT-A 10 µM, n = 21; and CTCH-D 2 µM, n = 16), RhoA (RhoA Inh 1 µg/ml, n = 21), and ROCK (Y27632 10 µM, n = 21) on α3β4-myc nAChRs density at the contact and edges of N-cadherin-mediated cell-cell contacts. Cells treated with DMSO (10 µl/ml, n = 20) were used as controls. D) Analysis of the percentage distribution of N-cadherin and N-cadherin-deleted proteins between the cell-cell contact and the edges of contact zone. E) Analysis of the effect of DMSO, LAT-A, CTCH-D, RhoA Inh, and Y27632 on N-cadherin density at the contact zone and at the edges of cell-cell contacts. Values in B, C, D, and E represent the mean ± SEM of each experimental group. One-way ANOVA of pixel density in cell-cell contacts and the edges of the contact in B and C, p

    Journal: PLoS ONE

    Article Title: Cell Surface Localization of ?3?4 Nicotinic Acetylcholine Receptors Is Regulated by N-Cadherin Homotypic Binding and Actomyosin Contractility

    doi: 10.1371/journal.pone.0062435

    Figure Lengend Snippet: N-cadherin homotypic binding promotes α3β4-myc nAChRs localization at the edges of the cell-cell contact. A) Schematic drawing of two contacting cells showing the areas of the cell surface in which α3β4-myc nAChRs and N-cadherin pixel area was measured in 2×2 µm regions placed at the center (red) and at each of the edges of the cell-cell contact (orange). The average of the two measurements of the edges was used for analysis, and the sum of the measurements at the center and edges at the cell-cell contact was considered 100%. B) Analysis of the percentage of α3β4-myc nAChRs pixel area distribution between the center and the edges of cell-cell contacts in cell junctions mediated by mEGFP (n = 24), N-cadherin (n = 22), N-cadherin-Δ-β-catenin (n = 25), and N-cadherin-Δ-cyto (n = 27). C) Analysis of the effect of inhibitors of actin polymerization (LAT-A 10 µM, n = 21; and CTCH-D 2 µM, n = 16), RhoA (RhoA Inh 1 µg/ml, n = 21), and ROCK (Y27632 10 µM, n = 21) on α3β4-myc nAChRs density at the contact and edges of N-cadherin-mediated cell-cell contacts. Cells treated with DMSO (10 µl/ml, n = 20) were used as controls. D) Analysis of the percentage distribution of N-cadherin and N-cadherin-deleted proteins between the cell-cell contact and the edges of contact zone. E) Analysis of the effect of DMSO, LAT-A, CTCH-D, RhoA Inh, and Y27632 on N-cadherin density at the contact zone and at the edges of cell-cell contacts. Values in B, C, D, and E represent the mean ± SEM of each experimental group. One-way ANOVA of pixel density in cell-cell contacts and the edges of the contact in B and C, p

    Article Snippet: Reagents: Alexa Fluor 488 Phalloidin (Molecular Probes, Invitrogen); cell permeable C3 transferase (RhoA Inhibitor I Cytoskeleton CT04, Denver, CO); Rho associated kinase (ROCK) inhibitor Y27632 (Cytoskeleton CN06); latrunculin A (LAT-A) (Sigma L5163); cytochalasin D (CTCH-D) (Sigma C8273); dimethyl sulfoxide (DMSO) (Sigma D2650); acetylcholine (Sigma A2661); and epibatidine (Sigma E1145).

    Techniques: Binding Assay

    ROCK regulates N-cadherin-mediate α3β4-myc nAChRs distribution on the cell surface. CHO cells expressing N-cadherin and α3β4-myc nAChRs were treated with DMSO (10 µl/ml) or with the indicated drugs: LAT-A 10 µM, CTCH-D 2 µM, RhoA Inh 1 µg/ml, and the ROCK inhibitor Y27632 10 µM. A) Effect of pharmacological treatments on α3β4-myc nAChRs density at N-cadherin-mediated cell-cell contacts as compared to cell-cell contacts between untreated cells expressing mEGFP and α3β4-myc nAChRs (100%) (mEGFP, n = 24; DMSO, n = 20; LAT-A, n = 21; CTCH-D, n = 15; RhoA Inh, n = 21; and Y27632, n = 21). B) Ratio between α3β4-myc nAChRs pixel area within cell-cell contacts and contact-free cell membrane in N-cadherin-mediated cell-cell contacts treated with the indicated drugs as compared to cell-cell contacts between cells expressing mEGFP (100%). C) N-cadherin pixel area within the cell-cell contact compared to untreated cells (100%). Values represent the mean ± SEM of each experimental group. One-way ANOVA in A and B, p

    Journal: PLoS ONE

    Article Title: Cell Surface Localization of ?3?4 Nicotinic Acetylcholine Receptors Is Regulated by N-Cadherin Homotypic Binding and Actomyosin Contractility

    doi: 10.1371/journal.pone.0062435

    Figure Lengend Snippet: ROCK regulates N-cadherin-mediate α3β4-myc nAChRs distribution on the cell surface. CHO cells expressing N-cadherin and α3β4-myc nAChRs were treated with DMSO (10 µl/ml) or with the indicated drugs: LAT-A 10 µM, CTCH-D 2 µM, RhoA Inh 1 µg/ml, and the ROCK inhibitor Y27632 10 µM. A) Effect of pharmacological treatments on α3β4-myc nAChRs density at N-cadherin-mediated cell-cell contacts as compared to cell-cell contacts between untreated cells expressing mEGFP and α3β4-myc nAChRs (100%) (mEGFP, n = 24; DMSO, n = 20; LAT-A, n = 21; CTCH-D, n = 15; RhoA Inh, n = 21; and Y27632, n = 21). B) Ratio between α3β4-myc nAChRs pixel area within cell-cell contacts and contact-free cell membrane in N-cadherin-mediated cell-cell contacts treated with the indicated drugs as compared to cell-cell contacts between cells expressing mEGFP (100%). C) N-cadherin pixel area within the cell-cell contact compared to untreated cells (100%). Values represent the mean ± SEM of each experimental group. One-way ANOVA in A and B, p

    Article Snippet: Reagents: Alexa Fluor 488 Phalloidin (Molecular Probes, Invitrogen); cell permeable C3 transferase (RhoA Inhibitor I Cytoskeleton CT04, Denver, CO); Rho associated kinase (ROCK) inhibitor Y27632 (Cytoskeleton CN06); latrunculin A (LAT-A) (Sigma L5163); cytochalasin D (CTCH-D) (Sigma C8273); dimethyl sulfoxide (DMSO) (Sigma D2650); acetylcholine (Sigma A2661); and epibatidine (Sigma E1145).

    Techniques: Expressing

    Reactivity of nAbs and non-nAbs to HIV-1 Env on the surface of latently infected T cells after provirus reactivation. ACH-2 cells were incubated with PMA (10 ng/ml) plus ionomycin (1 μg/ml) or DMSO for 24 h. Supernatants were subjected to HIV-1

    Journal: Journal of Virology

    Article Title: Blockage of CD59 Function Restores Activities of Neutralizing and Nonneutralizing Antibodies in Triggering Antibody-Dependent Complement-Mediated Lysis of HIV-1 Virions and Provirus-Activated Latently Infected Cells

    doi: 10.1128/JVI.01614-15

    Figure Lengend Snippet: Reactivity of nAbs and non-nAbs to HIV-1 Env on the surface of latently infected T cells after provirus reactivation. ACH-2 cells were incubated with PMA (10 ng/ml) plus ionomycin (1 μg/ml) or DMSO for 24 h. Supernatants were subjected to HIV-1

    Article Snippet: ACH-2 cells treated or untreated with phorbol 12-myristate 13-acetate (PMA; 10 ng/ml)/ionomycin (1 μg/ml) or dimethyl sulfoxide (DMSO) for 24 h were lysed in 1× cell lysis buffer (Cell Signaling Technology, Danvers, MA) plus 1× protease inhibitor cocktail (Sigma-Aldrich).

    Techniques: Infection, Incubation

    ME1 and 6PGD formed hetero-oligomers to promote 6PGD enzymatic activity. A , lysates from U2OS cells transfected with ME1 siRNA or control siRNA were treated with DMSO or the cross-linker DSS. Cell lysates were then prepared and analyzed by Western blotting. B , lysates from U2OS cells stably expressing ME1 or control vector were treated with DMSO or DSS. The mixtures were subjected to Western blotting analysis. C , 293T cells were transfected with GST-6PGD and FLAG-ME1 as indicated. Cell lysates were treated with DMSO or DSS, and analyzed by Western blotting. D , malic enzyme activity of purified FLAG-ME1 after being incubated with His peptide or His-6PGD proteins at different mole ratio as indicated ( top ). The protein expression was visualized by Coomassie Blue staining ( bottom ). Data are the means ± S.D. ( n = 3 independent experiments). E , activity of purified wild-type FLAG-6PGD, FLAG-6PGD mut1 (G10I, L11N, A12K, V13K, M14K, G15I), or FLAG-6PGD mut2 (H187N and D188L) protein in presence or absence of ME1 protein ( top ). Protein expression was analyzed by Coomassie Blue staining ( bottom ). Data are the means ± S.D. ( n = 3 independent experiments). F , 293T cells were transfected with FLAG-ME1 and eGFP-6PGD, eGFP-6PGD mut1 , or eGFP-6PGD mut2 as indicated. Cell lysates were immunoprecipitated with anti-FLAG antibody. Input and immunoprecipitates were analyzed by Western blotting. G , 293T cells were transfected with FLAG-ME1 and eGFP-6PGD, eGFP-6PGD K76R , or eGFP-6PGD K294R as indicated. Cell lysates were immunoprecipitated with anti-FLAG antibody and analyzed by Western blotting. H , purified FLAG-6PGD, FLAG-6PGD K76R , and FLAG-6PGD K294R proteins were incubated with either FLAG-ME1 or FLAG peptide as indicated. 6PGD activity was measured ( top ), and purified proteins were analyzed by Coomassie Blue staining ( bottom ). All results are representative of three independent experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Evidence for a direct cross-talk between malic enzyme and the pentose phosphate pathway via structural interactions

    doi: 10.1074/jbc.M117.810309

    Figure Lengend Snippet: ME1 and 6PGD formed hetero-oligomers to promote 6PGD enzymatic activity. A , lysates from U2OS cells transfected with ME1 siRNA or control siRNA were treated with DMSO or the cross-linker DSS. Cell lysates were then prepared and analyzed by Western blotting. B , lysates from U2OS cells stably expressing ME1 or control vector were treated with DMSO or DSS. The mixtures were subjected to Western blotting analysis. C , 293T cells were transfected with GST-6PGD and FLAG-ME1 as indicated. Cell lysates were treated with DMSO or DSS, and analyzed by Western blotting. D , malic enzyme activity of purified FLAG-ME1 after being incubated with His peptide or His-6PGD proteins at different mole ratio as indicated ( top ). The protein expression was visualized by Coomassie Blue staining ( bottom ). Data are the means ± S.D. ( n = 3 independent experiments). E , activity of purified wild-type FLAG-6PGD, FLAG-6PGD mut1 (G10I, L11N, A12K, V13K, M14K, G15I), or FLAG-6PGD mut2 (H187N and D188L) protein in presence or absence of ME1 protein ( top ). Protein expression was analyzed by Coomassie Blue staining ( bottom ). Data are the means ± S.D. ( n = 3 independent experiments). F , 293T cells were transfected with FLAG-ME1 and eGFP-6PGD, eGFP-6PGD mut1 , or eGFP-6PGD mut2 as indicated. Cell lysates were immunoprecipitated with anti-FLAG antibody. Input and immunoprecipitates were analyzed by Western blotting. G , 293T cells were transfected with FLAG-ME1 and eGFP-6PGD, eGFP-6PGD K76R , or eGFP-6PGD K294R as indicated. Cell lysates were immunoprecipitated with anti-FLAG antibody and analyzed by Western blotting. H , purified FLAG-6PGD, FLAG-6PGD K76R , and FLAG-6PGD K294R proteins were incubated with either FLAG-ME1 or FLAG peptide as indicated. 6PGD activity was measured ( top ), and purified proteins were analyzed by Coomassie Blue staining ( bottom ). All results are representative of three independent experiments.

    Article Snippet: The following reagents were all purchased from Sigma: G6P, 6PG, β-nicotinamide adenine dinucleotide 2′-phosphate (NADP+ ), 6PGD from yeast, trichostatin A, FLAG peptide, and anti-FLAG M2 affinity gel except disuccinimidyl suberate (DSS) from Thermo Scientific and dimethyl sulfoxide (DMSO) from Amresco.

    Techniques: Activity Assay, Transfection, Western Blot, Stable Transfection, Expressing, Plasmid Preparation, Purification, Incubation, Staining, Immunoprecipitation

    Controlling TC-83 induced ROS response in microglial cells decreases inflammatory burden. (a) Experimental workflow indicating HMC3 cells were pre-treated for 2h with 0.1% DMSO, 1μM BAY 11–7082 (BAY-82), or 100pM mitoquinone mesylate (MitoQ) prior to inoculation with TC-83 (MOI:2). Levels of the pro-inflammatory cytokines (b) IL-1α, (c) IL-1β, (d), IL-6 and (e) IL-8 produced by HMC3 cells as the direct result of TC-83 infection were measured at 1, 2, and 6hpi. The quantitative data are depicted as the means of three biologically independent experiments ± SD. * p

    Journal: Virulence

    Article Title: Direct and indirect pro-inflammatory cytokine response resulting from TC-83 infection of glial cells

    doi: 10.1080/21505594.2018.1509668

    Figure Lengend Snippet: Controlling TC-83 induced ROS response in microglial cells decreases inflammatory burden. (a) Experimental workflow indicating HMC3 cells were pre-treated for 2h with 0.1% DMSO, 1μM BAY 11–7082 (BAY-82), or 100pM mitoquinone mesylate (MitoQ) prior to inoculation with TC-83 (MOI:2). Levels of the pro-inflammatory cytokines (b) IL-1α, (c) IL-1β, (d), IL-6 and (e) IL-8 produced by HMC3 cells as the direct result of TC-83 infection were measured at 1, 2, and 6hpi. The quantitative data are depicted as the means of three biologically independent experiments ± SD. * p

    Article Snippet: Antibodies, inhibitors, and reagents The reagents and antibodies (Abs) used were as follows: dimethyl sulfoxide (DMSO) (VWR 97,063–136); the mitochondrially targeted antioxidant mitoquinone mesylate (MedKoo Biosciences 317,102); the NF-κB inhibitor BAY 11–7082 (Selleckchem S2913); the IL-1β inhibitor Pirfenidone (SelleckChem S2907); IL-1α, IL-1β, IL-6, and IL-8 recombinant protein (Aushon 101-3FF-1-AB); mouse monoclonal Ab to TOMM20 (Abcam ab56783), Alexa Fluor 488-conjugated goat anti-mouse (Invitrogen A21202), Alexa Fluor 568-conjugated donkey anti-goat (Invitrogen A11057); Anti-Venezuelan equine encephalitis antibody clone 1A3B-7 (EMD Millipore MAB8755); and polyclonal goat serum to TC-83 capsid protein (BEI Resources NR-9403).

    Techniques: Produced, Infection

    Indirect inflammatory response dependent on mitochondrially derived ROS. (a) Experimental workflow indicating that U-87 MG cells were pre-treated for 2h with 0.1% DMSO, 1µM BAY 11–7082 (BAY-82), or 100pM mitoquinone mesylate (MitoQ) prior to inoculation with TC-83 (MOI:2). Supernatants were removed from infected U-87 MG cells at 2hpi and overlaid onto naïve HMC3 microglia, with (b) IL-1α, (c) IL-1β, (d) IL-6, and (e) IL-8 cytokine levels measured at 1, 2, and 6 hours post overlay. The quantitative data are depicted as the means of three biologically independent experiments ± SD. * p

    Journal: Virulence

    Article Title: Direct and indirect pro-inflammatory cytokine response resulting from TC-83 infection of glial cells

    doi: 10.1080/21505594.2018.1509668

    Figure Lengend Snippet: Indirect inflammatory response dependent on mitochondrially derived ROS. (a) Experimental workflow indicating that U-87 MG cells were pre-treated for 2h with 0.1% DMSO, 1µM BAY 11–7082 (BAY-82), or 100pM mitoquinone mesylate (MitoQ) prior to inoculation with TC-83 (MOI:2). Supernatants were removed from infected U-87 MG cells at 2hpi and overlaid onto naïve HMC3 microglia, with (b) IL-1α, (c) IL-1β, (d) IL-6, and (e) IL-8 cytokine levels measured at 1, 2, and 6 hours post overlay. The quantitative data are depicted as the means of three biologically independent experiments ± SD. * p

    Article Snippet: Antibodies, inhibitors, and reagents The reagents and antibodies (Abs) used were as follows: dimethyl sulfoxide (DMSO) (VWR 97,063–136); the mitochondrially targeted antioxidant mitoquinone mesylate (MedKoo Biosciences 317,102); the NF-κB inhibitor BAY 11–7082 (Selleckchem S2913); the IL-1β inhibitor Pirfenidone (SelleckChem S2907); IL-1α, IL-1β, IL-6, and IL-8 recombinant protein (Aushon 101-3FF-1-AB); mouse monoclonal Ab to TOMM20 (Abcam ab56783), Alexa Fluor 488-conjugated goat anti-mouse (Invitrogen A21202), Alexa Fluor 568-conjugated donkey anti-goat (Invitrogen A11057); Anti-Venezuelan equine encephalitis antibody clone 1A3B-7 (EMD Millipore MAB8755); and polyclonal goat serum to TC-83 capsid protein (BEI Resources NR-9403).

    Techniques: Derivative Assay, Infection

    Comparison of CFZ and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and DMSO (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.

    Journal: The Journal of investigative dermatology

    Article Title: The Physicochemical Basis of Clofazimine-Induced Skin Pigmentation

    doi: 10.1016/j.jid.2017.09.031

    Figure Lengend Snippet: Comparison of CFZ and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and DMSO (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.

    Article Snippet: To synthesize the hydrochloride salt crystals for CFZ and 568, 7mM drug solution in dimethyl sulfoxide (DMSO) (67-68-5, Fisher Scientific, Fair Lawn, NJ) was added to 1M NH4 Cl in 1:1 (v/v) ratio and left for 24-48 hours at room temperature in the dark.

    Techniques: Fluorescence, Microscopy

    The combination of LCRF‐0006 and bortezomib synergistically increases MM tumor response in vivo. A, Schematic representation of treatment regimen. C57BL/KaLwRij mice with established MM (day 14 post‐5TGM1 cell injection) were treated with LCRF‐0006 (100 mg/kg) and bortezomib (0.5 mg/kg) (LCRF‐0006 + bortezomib), LCRF‐0006 and DMSO vehicle (LCRF‐0006), 2‐HP‐b‐CD vehicle and bortezomib (bortezomib) or 2‐HP‐b‐CD and DMSO vehicles (vehicles) i.p., as per treatment regimen. B, Tumor burden was assessed at day 14, 21 and 28 by BLI. Graph depicts mean ± SEM. n = 5‐6 mice/treatment group. *** P

    Journal: FASEB BioAdvances

    Article Title: LCRF‐0006, a small molecule mimetic of the N‐cadherin antagonist peptide ADH‐1, synergistically increases multiple myeloma response to bortezomib, et al. LCRF‐0006, a small molecule mimetic of the N‐cadherin antagonist peptide ADH‐1, synergistically increases multiple myeloma response to bortezomib

    doi: 10.1096/fba.2019-00073

    Figure Lengend Snippet: The combination of LCRF‐0006 and bortezomib synergistically increases MM tumor response in vivo. A, Schematic representation of treatment regimen. C57BL/KaLwRij mice with established MM (day 14 post‐5TGM1 cell injection) were treated with LCRF‐0006 (100 mg/kg) and bortezomib (0.5 mg/kg) (LCRF‐0006 + bortezomib), LCRF‐0006 and DMSO vehicle (LCRF‐0006), 2‐HP‐b‐CD vehicle and bortezomib (bortezomib) or 2‐HP‐b‐CD and DMSO vehicles (vehicles) i.p., as per treatment regimen. B, Tumor burden was assessed at day 14, 21 and 28 by BLI. Graph depicts mean ± SEM. n = 5‐6 mice/treatment group. *** P

    Article Snippet: 2.2 Drugs For in vitro experiments, LCRF‐0006 (kindly provided by Crocus Laboratories) was solubilized in dimethyl sulfoxide (DMSO) (Merck).

    Techniques: In Vivo, Mouse Assay, Injection

    SEM image of PVA nanofiber (a) before and after solvent vapor treatment with (b) DMF, (c) methanol, and (d) DMSO at a temperature of 40 °C for 8 h, and (e) Young's modulus and tensile strength of PVA nanofiber mats with various solvent types at a temperature of 40 °C for 4 h.

    Journal: Heliyon

    Article Title: Solvent vapor treatment improves mechanical strength of electrospun polyvinyl alcohol nanofibers

    doi: 10.1016/j.heliyon.2018.e00592

    Figure Lengend Snippet: SEM image of PVA nanofiber (a) before and after solvent vapor treatment with (b) DMF, (c) methanol, and (d) DMSO at a temperature of 40 °C for 8 h, and (e) Young's modulus and tensile strength of PVA nanofiber mats with various solvent types at a temperature of 40 °C for 4 h.

    Article Snippet: Solvents used for vapor treatment include dimethyl sulfoxide (DMSO), N, N-dimethyl formamide (DMF), and methanol, which were purchased from Merck, Germany.

    Techniques:

    DSC curve of (a) PVA-NF-untreated, (b) PVA-NF-DMF-treated, (c) PVA-NF-methanol treated, and (d) PVA-NF-DMSO treated PVA nanofiber mats at a heating rate of 10 °C/minutes.

    Journal: Heliyon

    Article Title: Solvent vapor treatment improves mechanical strength of electrospun polyvinyl alcohol nanofibers

    doi: 10.1016/j.heliyon.2018.e00592

    Figure Lengend Snippet: DSC curve of (a) PVA-NF-untreated, (b) PVA-NF-DMF-treated, (c) PVA-NF-methanol treated, and (d) PVA-NF-DMSO treated PVA nanofiber mats at a heating rate of 10 °C/minutes.

    Article Snippet: Solvents used for vapor treatment include dimethyl sulfoxide (DMSO), N, N-dimethyl formamide (DMF), and methanol, which were purchased from Merck, Germany.

    Techniques:

    Effects of S42 or DHT on atrogin1, MuRF1 , Igf1 expression on C2C12 myotubes. C2C12 myotubes were incubated with 1–10 µM of S42 or 100 nM of DHT or appropriate vehicle (DMSO) for 24 h. (A), (B), (C) Comparison of mRNA expression levels of atrogin1 , MuRF1 and Igf1 relative to those of Gapdh , respectively are shown. Data are expressed as mean ± SE of triplicate samples. In statistical comparisons, the data of treated groups with DHT or S42 were compared with that of untreated group. *P

    Journal: Biochemistry and Biophysics Reports

    Article Title: Selective androgen receptor modulator, S42 has anabolic and anti-catabolic effects on cultured myotubes

    doi: 10.1016/j.bbrep.2019.01.006

    Figure Lengend Snippet: Effects of S42 or DHT on atrogin1, MuRF1 , Igf1 expression on C2C12 myotubes. C2C12 myotubes were incubated with 1–10 µM of S42 or 100 nM of DHT or appropriate vehicle (DMSO) for 24 h. (A), (B), (C) Comparison of mRNA expression levels of atrogin1 , MuRF1 and Igf1 relative to those of Gapdh , respectively are shown. Data are expressed as mean ± SE of triplicate samples. In statistical comparisons, the data of treated groups with DHT or S42 were compared with that of untreated group. *P

    Article Snippet: S42, DHT and rapamycin were dissolved in dimethyl sulfoxide (DMSO) (Nacalai Tesque, Kyoto, Japan) and insulin was dissolved in a zinc solution.

    Techniques: Expressing, Incubation

    Effects of S42 or DHT on Ar expression on C2C12 myotubes. C2C12 myotubes were incubated with 1–10 µM of S42 or 100 nM of DHT or appropriate vehicle (DMSO) for 24 h. (A) Comparison of mRNA expression levels of Ar relative to those of Gapdh by qPCR. Data are expressed as mean ± SE of triplicate samples. (B)Western blot analysis showing Ar and Gapdh. (C) Statistical comparison of the expression levels of Ar relative to Gapdh by Western blot analysis. Data are expressed as mean ± SE of triplicate samples. In statistical comparisons in (A) and (C), the data of treated groups with DHT or S42 were compared with that of untreated group. **P

    Journal: Biochemistry and Biophysics Reports

    Article Title: Selective androgen receptor modulator, S42 has anabolic and anti-catabolic effects on cultured myotubes

    doi: 10.1016/j.bbrep.2019.01.006

    Figure Lengend Snippet: Effects of S42 or DHT on Ar expression on C2C12 myotubes. C2C12 myotubes were incubated with 1–10 µM of S42 or 100 nM of DHT or appropriate vehicle (DMSO) for 24 h. (A) Comparison of mRNA expression levels of Ar relative to those of Gapdh by qPCR. Data are expressed as mean ± SE of triplicate samples. (B)Western blot analysis showing Ar and Gapdh. (C) Statistical comparison of the expression levels of Ar relative to Gapdh by Western blot analysis. Data are expressed as mean ± SE of triplicate samples. In statistical comparisons in (A) and (C), the data of treated groups with DHT or S42 were compared with that of untreated group. **P

    Article Snippet: S42, DHT and rapamycin were dissolved in dimethyl sulfoxide (DMSO) (Nacalai Tesque, Kyoto, Japan) and insulin was dissolved in a zinc solution.

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

    Inhibition of TMZ-induced G2 arrest by Rsv leads to mitotic catastrophe. U87 cells were treated with Rsv 30 μM, TMZ 100 μM or RT for 24, 38 and 48 h, followed by fixation and DAPI staining. (A) representative images of nuclei from cells treated with DMSO (control), Rsv for 38 h or RT for 48 h. Double arrows point to fragmented/irregular nuclei; single arrow points to micronuclei; double arrowheads point to enlarged nuclei; Scale bar: 6 μm; (B) representative visible and fluorescent images of nuclei from untreated cells showing a normal mitosis (i and ii) ; an abnormal chromosome condensation and mitosis, with cellular enlargement, in a cell treated with RT for 48 h (iii and iv) ; and a triple mitosis in a cell treated with Rsv for 48 h (v and vi) and. Scale bar: 10 μm; (C) direct counting of the percentage of nuclei presenting normal (top), irregular (mid) or large phenotype (bottom); *p

    Journal: BMC Cancer

    Article Title: Resveratrol abrogates the Temozolomide-induced G2 arrest leading to mitotic catastrophe and reinforces the Temozolomide-induced senescence in glioma cells

    doi: 10.1186/1471-2407-13-147

    Figure Lengend Snippet: Inhibition of TMZ-induced G2 arrest by Rsv leads to mitotic catastrophe. U87 cells were treated with Rsv 30 μM, TMZ 100 μM or RT for 24, 38 and 48 h, followed by fixation and DAPI staining. (A) representative images of nuclei from cells treated with DMSO (control), Rsv for 38 h or RT for 48 h. Double arrows point to fragmented/irregular nuclei; single arrow points to micronuclei; double arrowheads point to enlarged nuclei; Scale bar: 6 μm; (B) representative visible and fluorescent images of nuclei from untreated cells showing a normal mitosis (i and ii) ; an abnormal chromosome condensation and mitosis, with cellular enlargement, in a cell treated with RT for 48 h (iii and iv) ; and a triple mitosis in a cell treated with Rsv for 48 h (v and vi) and. Scale bar: 10 μm; (C) direct counting of the percentage of nuclei presenting normal (top), irregular (mid) or large phenotype (bottom); *p

    Article Snippet: TMZ and Rsv were dissolved in dimethyl sulfoxide (DMSO) (Acros Organics, NJ, USA).

    Techniques: Inhibition, Staining

    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Journal: Drug metabolism and pharmacokinetics

    Article Title: An Efficient Method for Differentiation of Human Induced Pluripotent Stem Cells into Hepatocyte-like Cells Retaining Drug Metabolizing Activity

    doi:

    Figure Lengend Snippet: Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Article Snippet: Oncostatin M (OSM), dexa-methasone (DEX), omeprazole (OME), rifampicin (RIF), dimethyl sulfoxide (DMSO), and human normal adult liver total RNA, derived from a 64-year-old male donor, were obtained from Wako Pure Chemicals (Osaka, Japan).

    Techniques: Activity Assay, Cell Culture, Liquid Chromatography, Mass Spectrometry

    Effects of drugs on expression of CYP3A enzymes and UGT1A1 mRNAs in the hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h. The total mRNA was extracted from the cells. The expression of CYP3A and UGT1A1 mRNAs were analyzed by microarray analysis as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. Values were normalized to the levels of GAPDH mRNA. The graphs represent the relative gene expression level when the levels in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Journal: Drug metabolism and pharmacokinetics

    Article Title: An Efficient Method for Differentiation of Human Induced Pluripotent Stem Cells into Hepatocyte-like Cells Retaining Drug Metabolizing Activity

    doi:

    Figure Lengend Snippet: Effects of drugs on expression of CYP3A enzymes and UGT1A1 mRNAs in the hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h. The total mRNA was extracted from the cells. The expression of CYP3A and UGT1A1 mRNAs were analyzed by microarray analysis as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. Values were normalized to the levels of GAPDH mRNA. The graphs represent the relative gene expression level when the levels in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Article Snippet: Oncostatin M (OSM), dexa-methasone (DEX), omeprazole (OME), rifampicin (RIF), dimethyl sulfoxide (DMSO), and human normal adult liver total RNA, derived from a 64-year-old male donor, were obtained from Wako Pure Chemicals (Osaka, Japan).

    Techniques: Expressing, Microarray

    PLK1 phosphorylates BEX4 and regulates its subcellular localization during mitosis. a HeLa cells were transfected with shLuc, shBEX4, shCDK1, or shPLK1 and cultured in the presence of nocodazole (200 ng/ml) for 16 h. The cells were collected by shake-off, then lysed and immunoblotted with anti-PLK1, anti-CDK1, anti-BEX4, and anti-β-actin. Expression levels relative to respective controls are shown below the blots. b HeLa cells were transfected with control shLuc or PLK1-targeting shRNA, cultured on coverslips for 24 h and stained with anti-aurora A (Aur A), anti-BEX4, and DAPI. The metaphase cells were then analyzed. Scale bars represent 5 μm. c HeLa cells were cultured on coverslips for 24 h, then treated with BI2536 (300 nmol/l; a selective PLK1 inhibitor) or DMSO as the control. At 2 h post-treatment, the cells were fixed with 4% paraformaldehyde and stained with anti-BEX4 and anti-aurora A (Aur A) antibodies. DNA was visualized by DAPI staining. The insets show magnified images of centrosomes. Scale bars represent 5 μm. d HeLa cells were transfected with shLuc or shPLK1. At 36 h after transfection, the cells were treated with cycloheximide (CHX) for the indicated times and then subjected to immunoblotting with anti-BEX4, anti-PLK1, and anti-actin antibodies. e , f All serine (S) and threonine (T) residues in human BEX4 protein. HeLa cells were transfected with GFP-fused BEX4 mutant constructs with serine and/or threonine substituted with alanine (S3A, T29A, S35A, T94A, or T107A), or a BEX4 wild-type construct. The expression of each BEX4 expression construct was analyzed by immunoblotting using anti-GFP, anti-BEX4, and anti-actin antibodies ( e ). Cells were fixed with 4% paraformaldehyde and stained with anti-GFP and anti-aurora A (Aur A) antibodies. DNA was visualized by DAPI staining ( f ). The insets show magnified images of the centrosomes. Scale bars represent 5 μm

    Journal: Experimental & Molecular Medicine

    Article Title: Oncogenic potential of BEX4 is conferred by Polo-like kinase 1-mediated phosphorylation

    doi: 10.1038/s12276-018-0168-0

    Figure Lengend Snippet: PLK1 phosphorylates BEX4 and regulates its subcellular localization during mitosis. a HeLa cells were transfected with shLuc, shBEX4, shCDK1, or shPLK1 and cultured in the presence of nocodazole (200 ng/ml) for 16 h. The cells were collected by shake-off, then lysed and immunoblotted with anti-PLK1, anti-CDK1, anti-BEX4, and anti-β-actin. Expression levels relative to respective controls are shown below the blots. b HeLa cells were transfected with control shLuc or PLK1-targeting shRNA, cultured on coverslips for 24 h and stained with anti-aurora A (Aur A), anti-BEX4, and DAPI. The metaphase cells were then analyzed. Scale bars represent 5 μm. c HeLa cells were cultured on coverslips for 24 h, then treated with BI2536 (300 nmol/l; a selective PLK1 inhibitor) or DMSO as the control. At 2 h post-treatment, the cells were fixed with 4% paraformaldehyde and stained with anti-BEX4 and anti-aurora A (Aur A) antibodies. DNA was visualized by DAPI staining. The insets show magnified images of centrosomes. Scale bars represent 5 μm. d HeLa cells were transfected with shLuc or shPLK1. At 36 h after transfection, the cells were treated with cycloheximide (CHX) for the indicated times and then subjected to immunoblotting with anti-BEX4, anti-PLK1, and anti-actin antibodies. e , f All serine (S) and threonine (T) residues in human BEX4 protein. HeLa cells were transfected with GFP-fused BEX4 mutant constructs with serine and/or threonine substituted with alanine (S3A, T29A, S35A, T94A, or T107A), or a BEX4 wild-type construct. The expression of each BEX4 expression construct was analyzed by immunoblotting using anti-GFP, anti-BEX4, and anti-actin antibodies ( e ). Cells were fixed with 4% paraformaldehyde and stained with anti-GFP and anti-aurora A (Aur A) antibodies. DNA was visualized by DAPI staining ( f ). The insets show magnified images of the centrosomes. Scale bars represent 5 μm

    Article Snippet: The following reagents were used: MG132, cycloheximide (CHX), dimethyl sulfoxide (DMSO) (AG Scientific, San Diego, CA, USA), nocodazole (Sigma-Aldrich), and PLK1 kinase inhibitor BI2536 (Axon Medchem, Groningen, Netherlands).

    Techniques: Transfection, Cell Culture, Expressing, shRNA, Staining, Mutagenesis, Construct

    The in-vitro cytotoxicity of different NPs measured by MTT assay. (a) The cytotoxic effect of AgFeO 2 (Bio) and FeO 2 NPs synthesised by green co-reduction using A. blitum leaves extract and AgFeO 2 (Che) and FeO 2 NPs synthesised by chemical co-reduction precipitation method using NaBH 4 on non-cancerous human embryonic kidney cell lines (HEK 293 T) after 24 h of treatment were evaluated by mitochondrial activity using the MTT assay. The bar graph represents the mean value of three replicates where cells were treated 20 μg of NPs and cells treated with 10% DMSO were considered as control. (b) HEK 293 T cells treated with different NPs after 24 h incubation. HEK 293 T cells untreated (left panel) and the cells treated with 20 μg of Ag-FeO 2 (middle panel) and with 20 μg of FeO 2 (right panel). Magnification: 20 × . One-way ANOVAs were performed to evaluate significance comparing the both NPs to the control. A value of p

    Journal: Biotechnology Reports

    Article Title: Plant extract mediated synthesis enhanced the functional properties of silver ferrite nanoparticles over chemical mediated synthesis

    doi: 10.1016/j.btre.2020.e00469

    Figure Lengend Snippet: The in-vitro cytotoxicity of different NPs measured by MTT assay. (a) The cytotoxic effect of AgFeO 2 (Bio) and FeO 2 NPs synthesised by green co-reduction using A. blitum leaves extract and AgFeO 2 (Che) and FeO 2 NPs synthesised by chemical co-reduction precipitation method using NaBH 4 on non-cancerous human embryonic kidney cell lines (HEK 293 T) after 24 h of treatment were evaluated by mitochondrial activity using the MTT assay. The bar graph represents the mean value of three replicates where cells were treated 20 μg of NPs and cells treated with 10% DMSO were considered as control. (b) HEK 293 T cells treated with different NPs after 24 h incubation. HEK 293 T cells untreated (left panel) and the cells treated with 20 μg of Ag-FeO 2 (middle panel) and with 20 μg of FeO 2 (right panel). Magnification: 20 × . One-way ANOVAs were performed to evaluate significance comparing the both NPs to the control. A value of p

    Article Snippet: Dulbecco’s modified eagle’s medium (DMEM), penicillin-streptomycin-neomycin solution, fetal bovine serum (FBS) were purchased from Thermofischer Scientific (New York, USA), 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay kit and dimethyl sulfoxide (DMSO) were procured from Himedia Laboratories (Mumbai, India).

    Techniques: In Vitro, MTT Assay, Activity Assay, Incubation

    HDACs regulate the DNA damage response MCF-7 cells were treated with vehicle (DMSO) or vorinostat (Vor.) for 48 hours before adding epirubicin (0.5 μM) for an additional 0-8 hours. Total cell lysate was processed for western blotting examining the activation and stabilization of p53 due to increasing lengths of exposure to epirubicin (A.), and the concentration effect of vorinostat (B.). (C.) Cells grown on glass coverslips were treated as in (A.) before fixation, and immunofluorescence imaging of FITC-p53 and DAPI (D.). (E.) Cells treated as in (A.) were analyzed for induction of p21 and acetylation of histone H4 by western blotting. (E.) Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) analysis for the induction of GADD45A and RRM2B normalized to β-glucuronidase ( h.Gus ) for total RNA in cells treated as in (A). (*p

    Journal: Molecular cancer therapeutics

    Article Title: Histone Deacetylase Regulation of ATM-Mediated DNA Damage Signaling

    doi: 10.1158/1535-7163.MCT-12-1242

    Figure Lengend Snippet: HDACs regulate the DNA damage response MCF-7 cells were treated with vehicle (DMSO) or vorinostat (Vor.) for 48 hours before adding epirubicin (0.5 μM) for an additional 0-8 hours. Total cell lysate was processed for western blotting examining the activation and stabilization of p53 due to increasing lengths of exposure to epirubicin (A.), and the concentration effect of vorinostat (B.). (C.) Cells grown on glass coverslips were treated as in (A.) before fixation, and immunofluorescence imaging of FITC-p53 and DAPI (D.). (E.) Cells treated as in (A.) were analyzed for induction of p21 and acetylation of histone H4 by western blotting. (E.) Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) analysis for the induction of GADD45A and RRM2B normalized to β-glucuronidase ( h.Gus ) for total RNA in cells treated as in (A). (*p

    Article Snippet: Entinostat (MS-275) was obtained from Selleck Chemicals LLC, epirubicin from Calbiochem (EMD Chemical), dimethyl sulfoxide (DMSO) from MP Biomedicals LLC.

    Techniques: Western Blot, Activation Assay, Concentration Assay, Immunofluorescence, Imaging, Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR

    Effect of testosterone on probasin, Oat1- and Oat3-promoter activity. OK cells were either transfected with pSG5 or pSG5-rAR, and rAR expression and cellular localization were analyzed using immunofluorescence staining (green color rAR, blue color DAPI staining; excitation wavelength 488 nm and 365 nm) (1A). Promoter constructs of rat probasin, Oat1 and Oat3, and the expression vector for rAR were transiently transfected into OK cells (1B and 1C). Cells were cultured 43 h with either 100 nM testosterone (black bars) or with 0.0003% DMSO as control (white bars) (1B and 1C). Luciferase activity was measured and firefly luciferase was normalized to Renilla luciferase. Data are reported as the fold increase presented as mean ± S.E.M.; n = 4; n.s.: not significant; ***: p

    Journal: PLoS ONE

    Article Title: Male-Dominant Activation of Rat Renal Organic Anion Transporter 1 (Oat1) and 3 (Oat3) Expression by Transcription Factor BCL6

    doi: 10.1371/journal.pone.0035556

    Figure Lengend Snippet: Effect of testosterone on probasin, Oat1- and Oat3-promoter activity. OK cells were either transfected with pSG5 or pSG5-rAR, and rAR expression and cellular localization were analyzed using immunofluorescence staining (green color rAR, blue color DAPI staining; excitation wavelength 488 nm and 365 nm) (1A). Promoter constructs of rat probasin, Oat1 and Oat3, and the expression vector for rAR were transiently transfected into OK cells (1B and 1C). Cells were cultured 43 h with either 100 nM testosterone (black bars) or with 0.0003% DMSO as control (white bars) (1B and 1C). Luciferase activity was measured and firefly luciferase was normalized to Renilla luciferase. Data are reported as the fold increase presented as mean ± S.E.M.; n = 4; n.s.: not significant; ***: p

    Article Snippet: For rAR-transfection medium was supplemented with 100 nM testosterone (Fluka, Germany) dissolved in dimethyl sulfoxide (DMSO) (AppliChem, Germany), or control 0.0003% DMSO, in the absence of antibiotics.

    Techniques: Activity Assay, Transfection, Expressing, Immunofluorescence, Staining, Construct, Plasmid Preparation, Cell Culture, Luciferase

    TCDD-induced binding of AHR to putative DRE sites in PTPN6 promoter Nuclear protein was isolated from HepG2 cells treated with vehicle (VH, 0.01% DMSO) or TCDD (T, 30nM), incubated with 32 P -labeled A) or unlabeled B) consensus DRE and four DRE oligomers in PTPN6 promoter (indicated by the position relative to transcription start site). A) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, dried and autoradiographed. B) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, transferred to nitrocellulose, and probed with anti-AHR antibody. Arrow indicates specific binding of AHR to DRE oligomers. Results are representative of more than two independent experiments.

    Journal: Toxicology and applied pharmacology

    Article Title: SHP-1 is Directly Activated by the Aryl Hydrocarbon Receptor and regulates BCL-6 in the presence of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)

    doi: 10.1016/j.taap.2016.08.014

    Figure Lengend Snippet: TCDD-induced binding of AHR to putative DRE sites in PTPN6 promoter Nuclear protein was isolated from HepG2 cells treated with vehicle (VH, 0.01% DMSO) or TCDD (T, 30nM), incubated with 32 P -labeled A) or unlabeled B) consensus DRE and four DRE oligomers in PTPN6 promoter (indicated by the position relative to transcription start site). A) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, dried and autoradiographed. B) Protein:DNA complexes were resolved on a 4% nondenaturing PAGE gel, transferred to nitrocellulose, and probed with anti-AHR antibody. Arrow indicates specific binding of AHR to DRE oligomers. Results are representative of more than two independent experiments.

    Article Snippet: 99.1% pure TCDD dissolved in dimethyl sulfoxide (DMSO) was purchased from AccuStandard Inc., (New Haven, CT).

    Techniques: Binding Assay, Isolation, Incubation, Labeling, Polyacrylamide Gel Electrophoresis

    ( A ) SEC elugram of AMCA-PLGA; the black line indicates the refractive index of the PLGA expressed as relative units (RIU), and the gray line indicates the ultraviolet absorption by AMCA at 350 nm expressed as relative milli-units (mAU). ( B ) Stability studies via fluorescence intensity measurements of AMCA-PLGA in DMSO for > 120 hours at 4°C (solid line, crosses), 20°C (dotted line, triangles) and 37°C (broken line, circles). Data are expressed as ratios of I/I 0 and shown as the mean ± SD of three independent experiments. Abbreviations: AMCA-PLGA, 7-amino-4-methyl-3-coumarinylacetic acid-poly( d,l -lactide-co-glycolide); DMSO, dimethyl sulfoxide; mAU, milli-absorption unit; PLGA, poly( d,l -lactide-co-glycolide); RIU, refractive index unit; SD, standard deviation; SEC, size exclusion chromatography.

    Journal: International Journal of Nanomedicine

    Article Title: A blue fluorescent labeling technique utilizing micro- and nanoparticles for tracking in LIVE/DEAD® stained pathogenic biofilms of Staphylococcus aureus and Burkholderia cepacia

    doi: 10.2147/IJN.S98401

    Figure Lengend Snippet: ( A ) SEC elugram of AMCA-PLGA; the black line indicates the refractive index of the PLGA expressed as relative units (RIU), and the gray line indicates the ultraviolet absorption by AMCA at 350 nm expressed as relative milli-units (mAU). ( B ) Stability studies via fluorescence intensity measurements of AMCA-PLGA in DMSO for > 120 hours at 4°C (solid line, crosses), 20°C (dotted line, triangles) and 37°C (broken line, circles). Data are expressed as ratios of I/I 0 and shown as the mean ± SD of three independent experiments. Abbreviations: AMCA-PLGA, 7-amino-4-methyl-3-coumarinylacetic acid-poly( d,l -lactide-co-glycolide); DMSO, dimethyl sulfoxide; mAU, milli-absorption unit; PLGA, poly( d,l -lactide-co-glycolide); RIU, refractive index unit; SD, standard deviation; SEC, size exclusion chromatography.

    Article Snippet: Stability of AMCA-PLGA A 4 mg/mL solution of AMCA-PLGA was prepared in dimethyl sulfoxide (DMSO) (ROTIPURAN® , ≥99.9%, p.a., Carl Roth GmbH), and 200 μL aliquots were transferred to 96-well plates (Greiner Bio-One, Frickenhausen, Germany).

    Techniques: Size-exclusion Chromatography, Fluorescence, Standard Deviation