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  • 99
    Millipore ϐ actin
    ϐ Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Enzo Biochem beta β mhc
    Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and <t>beta-MHC,</t> respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.
    Beta β Mhc, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore β cyclocitral
    <t>β-Cyclocitral</t> induces meristematic cell divisions in Arabidopsis . ( A ) Confocal images of primary root meristems. (Scale bar, 50 μm.) Meristematic cortex cells are highlighted in orange. ( B ) Relative number of cortex cells in the primary
    β Cyclocitral, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Tocris beta funaltrexamine beta funaltrexamine β fna
    <t>β-Cyclocitral</t> induces meristematic cell divisions in Arabidopsis . ( A ) Confocal images of primary root meristems. (Scale bar, 50 μm.) Meristematic cortex cells are highlighted in orange. ( B ) Relative number of cortex cells in the primary
    Beta Funaltrexamine Beta Funaltrexamine β Fna, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore β phenylcinnamaldehyde
    Catalytic activity of the different catalysts in the hydrogenation of <t>β‐phenylcinnamaldehyde</t> (BPCMA). First order rate constants were obtained by fitting the reaction profiles with first order kinetic over 20 h of reaction. The composite catalysts have a Pt weight loading of 0.3–0.5 wt.%, whilst Pt‐A−Cl and Pt−Y−NH 3 have weight loadings of 0.7–0.8 wt.%. Conditions: 135 mmol BPCMA/l, BPCMA/Pt (mol/mol)=950, i‐pro 6 ml, H 2 O 1 ml, H 2 20 bar, 70 °C, 500 rpm.
    β Phenylcinnamaldehyde, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore β butyrolactone
    Ring-opening polymerization of <t>β-butyrolactone</t> using pectin as initiator to yield pec-PHB.
    β Butyrolactone, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore β elemene
    Typical chromatogram of 28‐day‐old plantlets of Brassica napus L. var. Es Astrid using selected ion monitoring (SIM) mode. Peak identification: 1: myrcene, 2: limonene, 3: n ‐butyl benzene internal standard (IS) not used, 4: <t>β‐elemene,</t> 5: octylbenzene (IS), 6: (E,E)‐α‐farnesene [Colour figure can be viewed at http://wileyonlinelibrary.com ]
    β Elemene, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore β glucan β glucan
    Microbicidal activity of <t>β-glucan-treated</t> neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) at 37°C for different times (0, 30, 60, 90, and 120 min). The quantity of viable yeast was estimated by plating the samples in Sabouraund Dextrose Agar (SDA) at 37°C for 24 h. The data are expressed as the mean ± SD of three separate experiments. * p ≤0.05, significant difference compared with the control group (yeast alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.
    β Glucan β Glucan, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore β naphthoflavone β nf
    Enzyme-labeled fluorescence (ELF) in situ hybridization control experiments utilizing cultured rat hepatoma cells and formalin-fixed, paraffin-embedded human tissue sections. (A) 22-μM <t>beta-napthoflavone</t> <t>(β-NF)-induced</t> H4IIE rat cells hybridized with rat biotin-conjugated CYP1A1 oligomer. (B) 22-μM β-NF-treated H4IIe rat cells probed with the rat biotin-labeled CYP1A1 20-mer and pretreated with 150 μ/ml of RNase A. (C) 22-μM β-NF-exposed H4IIE rat cells hybridized with rat biotinylated CYP1A1 2Gmer plus 60-fold excess nonbiotinylated rat CYP1A1 probe. (D) Poorly differentiated squamous cell carcinoma of human oral epithelium probed with human CYP1A1 biotin-labeled 20-mer. (E) Poorly differentiated squamous cell carcinoma of human oral epithelium hybridized with the partially homologous rat CYP1A1 biotin-conjugated oligomer probe. (F) Poorly differentiated squamous cell carcinoma of human oral epithelium without the addition of a biotinylated oligomer to the hybridization buffer. Magnification 400×.
    β Naphthoflavone β Nf, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore β bromostyrene
    Enzyme-labeled fluorescence (ELF) in situ hybridization control experiments utilizing cultured rat hepatoma cells and formalin-fixed, paraffin-embedded human tissue sections. (A) 22-μM <t>beta-napthoflavone</t> <t>(β-NF)-induced</t> H4IIE rat cells hybridized with rat biotin-conjugated CYP1A1 oligomer. (B) 22-μM β-NF-treated H4IIe rat cells probed with the rat biotin-labeled CYP1A1 20-mer and pretreated with 150 μ/ml of RNase A. (C) 22-μM β-NF-exposed H4IIE rat cells hybridized with rat biotinylated CYP1A1 2Gmer plus 60-fold excess nonbiotinylated rat CYP1A1 probe. (D) Poorly differentiated squamous cell carcinoma of human oral epithelium probed with human CYP1A1 biotin-labeled 20-mer. (E) Poorly differentiated squamous cell carcinoma of human oral epithelium hybridized with the partially homologous rat CYP1A1 biotin-conjugated oligomer probe. (F) Poorly differentiated squamous cell carcinoma of human oral epithelium without the addition of a biotinylated oligomer to the hybridization buffer. Magnification 400×.
    β Bromostyrene, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore stat1 β β mice
    STAT1β shows prolonged tyrosine 701 phosphorylation. (A to D) BMMϕ derived from WT (+/+), <t>Stat1</t> <t>β/β</t> (β/β), and Stat1 α/α (α/α) mice were stimulated with IFN-β (A) or
    Stat1 β β Mice, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore β lactamase
    Mineral shells formed from [W/O/W] double emulsions support in vitro protein expression. ( A ) Schematic overview of the second, double emulsion–producing, flow-focusing junction of a two-junction flow-focusing microfluidic device used to generate mineralized double emulsions (see fig. S10 and movie S4). ( B ) Schematic of [W/O/W] droplet mineralization to form an interfacial mineral layer around bacterial extracts in the innermost water phase. Here, “S” is a fluorogenic substrate (CCF2) that changes emission properties when enzymatically converted to product (“P”) by <t>β-lactamase</t> (β-lac) enzyme. ( C ) Polarized light optical micrograph shows interfacial birefringence. ( D ) Flow cytometry scatter plots of 50,000 droplets, proving that mineralized droplets support compartmentalized in vitro protein expression.
    β Lactamase, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 285 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore β lapachone
    ROS reagents inhibit the activity of the SMN complex in vitro and in cells (A) Effect of H 2 O 2 on the activity of the SMN complex in vitro . Magnetic beads snRNP assembly assay was carried out in the presence of increasing amounts of H 2 O 2 . IC 50 was calculated from the dose-response curve. Error bars represent SDs from triplicate measurements. (B) Effect of menadione on SMN complex activity in vitro . The same experimental procedure was carried out as in (A), except that menadione was used instead. (C) Dose-dependent effect of menadione on SMN complex activity in cells. HeLa cells were treated with menadione at the indicated concentrations or with DMSO control for 1 hour. SMN complex activity in extracts from various treated cells was measured in comparison to DMSO control cell extract (100% activity) by magnetic beads snRNP assembly assay. Error bars represent SDs from 3 independent measurements. (D) Extracts from (C) mixed with sample buffer without or with DTT were resolved by SDS-PAGE and analyzed by Western blot of the entire membrane with anti-SMN antibody 62E7. The molecular mass markers in kDa are indicated on the left. “redSMN” indicates monomer SMN migrating at normal molecular mass and “oxSMN” indicates disulfide-crosslinked SMN upon oxidation. (E) <t>β-lapachone</t> and menadione generate ROS in live cells. HeLa cells were incubated 30 minutes with ROS indicator dye H 2 DCFDA (10 μM) or without dye as a control, then treated with compounds at indicated concentrations or DMSO as control. Fluorescence images were acquired 30 minutes after treatment.
    β Lapachone, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore β eudesmol
    ROS reagents inhibit the activity of the SMN complex in vitro and in cells (A) Effect of H 2 O 2 on the activity of the SMN complex in vitro . Magnetic beads snRNP assembly assay was carried out in the presence of increasing amounts of H 2 O 2 . IC 50 was calculated from the dose-response curve. Error bars represent SDs from triplicate measurements. (B) Effect of menadione on SMN complex activity in vitro . The same experimental procedure was carried out as in (A), except that menadione was used instead. (C) Dose-dependent effect of menadione on SMN complex activity in cells. HeLa cells were treated with menadione at the indicated concentrations or with DMSO control for 1 hour. SMN complex activity in extracts from various treated cells was measured in comparison to DMSO control cell extract (100% activity) by magnetic beads snRNP assembly assay. Error bars represent SDs from 3 independent measurements. (D) Extracts from (C) mixed with sample buffer without or with DTT were resolved by SDS-PAGE and analyzed by Western blot of the entire membrane with anti-SMN antibody 62E7. The molecular mass markers in kDa are indicated on the left. “redSMN” indicates monomer SMN migrating at normal molecular mass and “oxSMN” indicates disulfide-crosslinked SMN upon oxidation. (E) <t>β-lapachone</t> and menadione generate ROS in live cells. HeLa cells were incubated 30 minutes with ROS indicator dye H 2 DCFDA (10 μM) or without dye as a control, then treated with compounds at indicated concentrations or DMSO as control. Fluorescence images were acquired 30 minutes after treatment.
    β Eudesmol, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore β hbcd
    Excretion of <t>β-HBCD-derived</t> radioactivity over time following single doses of 3, 30, or 100mg/kg by gavage. Values are the mean ± SD of four mice. *The value is significantly higher than that for the 100mg/kg group ( p
    β Hbcd, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore β napthoflavone
    Histochemical detection of β-glucosidase activity in mouse tissues . (a, b) Cryostat sections of snap frozen small intestine from non-transgenic mice stained with BCI-glu. (a) Endogenous activity in the villus brush-border. (b) No activity following incubation at 65°C for 20 min. (c-i) BCI-glu staining of tissues from R26 SYNbglA R (left of panel) and PGKcre m /R26 SYNbglA R (right of panel) mice: (c) heart and thymus, (d) spleen and pancreas, (e) kidney, (f) skeletal muscle, (g) liver, (h) glandular stomach and (i) brain. (j, k) Small intestinal wholemounts heat treated at 65°C and stained with BCI-glu from: (j) untreated Ahcre/R26 SYNbglA R; (k) <t>β-napthoflavone</t> treated Ahcre/R26 SYNbglA R mice (4 weeks post induction), showing detectable enzyme activity only in (k). (l-o) Wholemount of colon from an Ahcre/R26 SYNbglA R mouse prepared 16 weeks after β-napthoflavone treatment and stained with Mag-glu (p, proximal; d, distal). (l) Extensive recombination occurs throughout as indicated by magenta staining but becomes increasingly variegated towards the distal end. (m-o) Shows enlargements of areas indicated by arrows. Punctate magenta staining corresponds to individual colonic crypts. Bars: A, B 200 μm, C-O 1 cm.
    β Napthoflavone, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore beta hexaclorocyclohexane β hch
    Evaluation of the signaling pathways triggered by <t>β-hexaclorocyclohexane</t> <t>(β-HCH).</t> Immunoblot analysis of the time-course assay performed on human prostate cancer (LNCaP), human breast cancer (MCF-7 and MDA-MB 468), and human hepatoma (HepG2) cells treated with 10 μM β-HCH. Samples were analyzed for signal transducer and activator of transcription 3 (STAT3) and each cell line for a specific membrane or membrane associated tyrosine kinase receptor: EGFR in MDA-MB 468 cells, JAK2 in HepG2 cells, SRC in LNCaP cells and HER2 in MCF-7 cells. Both unmodified and the corresponding phosphorylated form were detected for each protein using specific antibodies.
    Beta Hexaclorocyclohexane β Hch, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore β funaltrexamine hydrochloride β fna
    Evaluation of the signaling pathways triggered by <t>β-hexaclorocyclohexane</t> <t>(β-HCH).</t> Immunoblot analysis of the time-course assay performed on human prostate cancer (LNCaP), human breast cancer (MCF-7 and MDA-MB 468), and human hepatoma (HepG2) cells treated with 10 μM β-HCH. Samples were analyzed for signal transducer and activator of transcription 3 (STAT3) and each cell line for a specific membrane or membrane associated tyrosine kinase receptor: EGFR in MDA-MB 468 cells, JAK2 in HepG2 cells, SRC in LNCaP cells and HER2 in MCF-7 cells. Both unmodified and the corresponding phosphorylated form were detected for each protein using specific antibodies.
    β Funaltrexamine Hydrochloride β Fna, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore β methylphenethylamine
    Evaluation of the signaling pathways triggered by <t>β-hexaclorocyclohexane</t> <t>(β-HCH).</t> Immunoblot analysis of the time-course assay performed on human prostate cancer (LNCaP), human breast cancer (MCF-7 and MDA-MB 468), and human hepatoma (HepG2) cells treated with 10 μM β-HCH. Samples were analyzed for signal transducer and activator of transcription 3 (STAT3) and each cell line for a specific membrane or membrane associated tyrosine kinase receptor: EGFR in MDA-MB 468 cells, JAK2 in HepG2 cells, SRC in LNCaP cells and HER2 in MCF-7 cells. Both unmodified and the corresponding phosphorylated form were detected for each protein using specific antibodies.
    β Methylphenethylamine, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore β tetralone
    Transformation of <t>β-tetralone</t> ( 3 ) in the culture of Chaetomium sp . KCh 6651
    β Tetralone, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore iκb kinase β ikk β
    Transformation of <t>β-tetralone</t> ( 3 ) in the culture of Chaetomium sp . KCh 6651
    Iκb Kinase β Ikk β, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore β galactosidase determination β gal assays
    Transformation of <t>β-tetralone</t> ( 3 ) in the culture of Chaetomium sp . KCh 6651
    β Galactosidase Determination β Gal Assays, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore β gal
    Level of <t>β-Gal</t> expression in five parental clones established for RMCE. The parental construct containing a hyg-tk fusion gene under the control of a tk promoter (pTK) is exchanged for a lacZ-neo fusion gene cassette that resides on the exchange
    β Gal, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 571 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and beta-MHC, respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.

    Journal: PLoS ONE

    Article Title: Identification and Characterization of Calcium Sparks in Cardiomyocytes Derived from Human Induced Pluripotent Stem Cells

    doi: 10.1371/journal.pone.0055266

    Figure Lengend Snippet: Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and beta-MHC, respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.

    Article Snippet: After blocking with 5% goat serum in PBS for 1 h at room temperature, cells stained with mouse anti-human cardiac sarcomeric alpha-actinin (α-actinin) (clone EA-35, Sigma) and mouse anti-human cardiac myosin heave chain, beta (β-MHC) (Alexis Biochemicals, FL, USA).

    Techniques: Derivative Assay, Staining, Patch Clamp

    β-Cyclocitral induces meristematic cell divisions in Arabidopsis . ( A ) Confocal images of primary root meristems. (Scale bar, 50 μm.) Meristematic cortex cells are highlighted in orange. ( B ) Relative number of cortex cells in the primary

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

    Article Title: β-Cyclocitral is a conserved root growth regulator

    doi: 10.1073/pnas.1821445116

    Figure Lengend Snippet: β-Cyclocitral induces meristematic cell divisions in Arabidopsis . ( A ) Confocal images of primary root meristems. (Scale bar, 50 μm.) Meristematic cortex cells are highlighted in orange. ( B ) Relative number of cortex cells in the primary

    Article Snippet: Optimized working concentrations of β-cyclocitral (#16976; Sigma Aldrich) in media were 750 nM, 100 μM, and 10 μM for Arabidopsis , tomato, and rice, respectively.

    Techniques:

    Identification of β-cyclocitral, a root growth promoter in Arabidopsis . ( A ) The LR capacity of D15-treated plants, normalized to control plants. The IC 50 is highlighted in red. ( B ) Seedlings after treatment with 30 μM D15 and 25 μM

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

    Article Title: β-Cyclocitral is a conserved root growth regulator

    doi: 10.1073/pnas.1821445116

    Figure Lengend Snippet: Identification of β-cyclocitral, a root growth promoter in Arabidopsis . ( A ) The LR capacity of D15-treated plants, normalized to control plants. The IC 50 is highlighted in red. ( B ) Seedlings after treatment with 30 μM D15 and 25 μM

    Article Snippet: Optimized working concentrations of β-cyclocitral (#16976; Sigma Aldrich) in media were 750 nM, 100 μM, and 10 μM for Arabidopsis , tomato, and rice, respectively.

    Techniques:

    β-Cyclocitral has conserved effects on root architecture in tomato and rice. ( A ) Tomato seedlings treated with β-cyclocitral. (Scale bar, 10 mm.) ( Inset ) The growth angle (θ) between the tip of the LR and the primary root measured

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

    Article Title: β-Cyclocitral is a conserved root growth regulator

    doi: 10.1073/pnas.1821445116

    Figure Lengend Snippet: β-Cyclocitral has conserved effects on root architecture in tomato and rice. ( A ) Tomato seedlings treated with β-cyclocitral. (Scale bar, 10 mm.) ( Inset ) The growth angle (θ) between the tip of the LR and the primary root measured

    Article Snippet: Optimized working concentrations of β-cyclocitral (#16976; Sigma Aldrich) in media were 750 nM, 100 μM, and 10 μM for Arabidopsis , tomato, and rice, respectively.

    Techniques:

    β-Cyclocitral promotes rice root growth under salt stress. ( A ) Rice roots treated with β-cyclocitral and grown in gel with 50 mM NaCl. (Scale bar, 10 mm.) ( B ) Root system depth in seedlings treated β-cyclocitral and grown in gel

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

    Article Title: β-Cyclocitral is a conserved root growth regulator

    doi: 10.1073/pnas.1821445116

    Figure Lengend Snippet: β-Cyclocitral promotes rice root growth under salt stress. ( A ) Rice roots treated with β-cyclocitral and grown in gel with 50 mM NaCl. (Scale bar, 10 mm.) ( B ) Root system depth in seedlings treated β-cyclocitral and grown in gel

    Article Snippet: Optimized working concentrations of β-cyclocitral (#16976; Sigma Aldrich) in media were 750 nM, 100 μM, and 10 μM for Arabidopsis , tomato, and rice, respectively.

    Techniques:

    Catalytic activity of the different catalysts in the hydrogenation of β‐phenylcinnamaldehyde (BPCMA). First order rate constants were obtained by fitting the reaction profiles with first order kinetic over 20 h of reaction. The composite catalysts have a Pt weight loading of 0.3–0.5 wt.%, whilst Pt‐A−Cl and Pt−Y−NH 3 have weight loadings of 0.7–0.8 wt.%. Conditions: 135 mmol BPCMA/l, BPCMA/Pt (mol/mol)=950, i‐pro 6 ml, H 2 O 1 ml, H 2 20 bar, 70 °C, 500 rpm.

    Journal: Chemcatchem

    Article Title: Assessment of the Location of Pt Nanoparticles in Pt/zeolite Y/γ‐Al2O3 Composite Catalysts

    doi: 10.1002/cctc.201901617

    Figure Lengend Snippet: Catalytic activity of the different catalysts in the hydrogenation of β‐phenylcinnamaldehyde (BPCMA). First order rate constants were obtained by fitting the reaction profiles with first order kinetic over 20 h of reaction. The composite catalysts have a Pt weight loading of 0.3–0.5 wt.%, whilst Pt‐A−Cl and Pt−Y−NH 3 have weight loadings of 0.7–0.8 wt.%. Conditions: 135 mmol BPCMA/l, BPCMA/Pt (mol/mol)=950, i‐pro 6 ml, H 2 O 1 ml, H 2 20 bar, 70 °C, 500 rpm.

    Article Snippet: Hydrogenation of β‐phenylcinnamaldehyde (BPCMA, Sigma‐Aldrich) was performed in stainless steel autoclaves with a total volume of 15 ml.

    Techniques: Activity Assay

    Ring-opening polymerization of β-butyrolactone using pectin as initiator to yield pec-PHB.

    Journal: ACS Omega

    Article Title: Electrospun Pectin-Polyhydroxybutyrate Nanofibers for Retinal Tissue Engineering

    doi: 10.1021/acsomega.7b01604

    Figure Lengend Snippet: Ring-opening polymerization of β-butyrolactone using pectin as initiator to yield pec-PHB.

    Article Snippet: 4 Materials and Methods Pectin (from apple), β-butyrolactone, tin(II) 2-ethylhexanoate, and 1,1,1,3,3,3-hexafluoro-2-propanol were purchased from Sigma-Aldrich.

    Techniques:

    Typical chromatogram of 28‐day‐old plantlets of Brassica napus L. var. Es Astrid using selected ion monitoring (SIM) mode. Peak identification: 1: myrcene, 2: limonene, 3: n ‐butyl benzene internal standard (IS) not used, 4: β‐elemene, 5: octylbenzene (IS), 6: (E,E)‐α‐farnesene [Colour figure can be viewed at http://wileyonlinelibrary.com ]

    Journal: Phytochemical Analysis

    Article Title: A laboratory high‐throughput glass chamber using dynamic headspace TD‐GC/MS method for the analysis of whole Brassica napus L. plantlet volatiles under cadmium‐related abiotic stress. A laboratory high‐throughput glass chamber using dynamic headspace TD‐GC/MS method for the analysis of whole Brassica napus L. plantlet volatiles under cadmium‐related abiotic stress

    doi: 10.1002/pca.2750

    Figure Lengend Snippet: Typical chromatogram of 28‐day‐old plantlets of Brassica napus L. var. Es Astrid using selected ion monitoring (SIM) mode. Peak identification: 1: myrcene, 2: limonene, 3: n ‐butyl benzene internal standard (IS) not used, 4: β‐elemene, 5: octylbenzene (IS), 6: (E,E)‐α‐farnesene [Colour figure can be viewed at http://wileyonlinelibrary.com ]

    Article Snippet: In this way representative single‐ion peaks with respective relative abundance of myrcene (23.03%), β‐elemene (7.29%) and (E,E)‐α‐farnesene (9.45%) were integrated and compared with the equivalent single‐ion response of 1 μL of hexane solution containing an internal standard of octylbenzene (0.5 mg/mL) (2.69%) (Sigma‐Aldrich).

    Techniques:

    Microbicidal activity of β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) at 37°C for different times (0, 30, 60, 90, and 120 min). The quantity of viable yeast was estimated by plating the samples in Sabouraund Dextrose Agar (SDA) at 37°C for 24 h. The data are expressed as the mean ± SD of three separate experiments. * p ≤0.05, significant difference compared with the control group (yeast alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: Microbicidal activity of β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) at 37°C for different times (0, 30, 60, 90, and 120 min). The quantity of viable yeast was estimated by plating the samples in Sabouraund Dextrose Agar (SDA) at 37°C for 24 h. The data are expressed as the mean ± SD of three separate experiments. * p ≤0.05, significant difference compared with the control group (yeast alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Activity Assay, Incubation

    Phagocytosis activity of β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated for 1 h at 37°C with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) labeled with FITC. Phagocytosis was determined by flow cytometry, and the results are expressed as the mean fluorescence (in arbitrary units [au]) ± SD of three independent experiments. # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: Phagocytosis activity of β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated for 1 h at 37°C with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) labeled with FITC. Phagocytosis was determined by flow cytometry, and the results are expressed as the mean fluorescence (in arbitrary units [au]) ± SD of three independent experiments. # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Activity Assay, Incubation, Labeling, Flow Cytometry, Cytometry, Fluorescence

    Cytokine release by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and activated or not by the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) and 1 µg/ml LPS and cultured for 18 h. (a, a’) IL-8. (b, b’) IL-1β. (c, c’) IL-1Ra. (d, d’) TNF-α. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: Cytokine release by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and activated or not by the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) and 1 µg/ml LPS and cultured for 18 h. (a, a’) IL-8. (b, b’) IL-1β. (c, c’) IL-1Ra. (d, d’) TNF-α. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Cell Culture

    Oxygen consumption by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and activated or not by the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml). Oxygen consumption was monitored for 5–10 min and calculated from the polarographic recordings using an initial concentration of dissolved oxygen of 190 µM at 37°C. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: Oxygen consumption by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata . Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and activated or not by the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml). Oxygen consumption was monitored for 5–10 min and calculated from the polarographic recordings using an initial concentration of dissolved oxygen of 190 µM at 37°C. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Concentration Assay

    HOCl production by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata determined by spectrophotometry. Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and activated or not by the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) and read at 655 nm. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: HOCl production by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata determined by spectrophotometry. Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and activated or not by the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml) and read at 655 nm. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Spectrophotometry

    Myeloperoxidase activity of β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata (integrated light emission). The inset represents kinetic study of MPO activity of β-glucan-treated neutrophils after 20 minutes of incubation. Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (2×10 7 CFU/ml) for 30 min. (a,a’) ATCC. (b,b’) ASS. (c,c’) VVC. (d,d’) RVVC. After incubation, chemiluminescence was monitored for 20 min at 37°C in a microplate luminometer using luminol as a chemical light amplifier. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: Myeloperoxidase activity of β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata (integrated light emission). The inset represents kinetic study of MPO activity of β-glucan-treated neutrophils after 20 minutes of incubation. Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (2×10 7 CFU/ml) for 30 min. (a,a’) ATCC. (b,b’) ASS. (c,c’) VVC. (d,d’) RVVC. After incubation, chemiluminescence was monitored for 20 min at 37°C in a microplate luminometer using luminol as a chemical light amplifier. The data are expressed as the mean ± SD of three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Activity Assay, Incubation

    Intracellular oxidant species production by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata determined by flow cytometry. Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated for 1 h with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml), followed by 30 min incubation with DHR. The data are expressed as the mean ± SD of at least three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils. (C and D) Representative dot plot display of FL1 (green fluorescence) vs . FL2 on a logarithmic scale. (C – (a) ATCC, (c) ASS, (e) VVC,(g) RVVC) C. albicans with untreated neutrophils. (C – (b) ATCC,(d) ASS,(f) VVC,(h) RVVC) C. albicans with neutrophils previously treated with 3 mg/ml β-glucan. (D – (a’) ATCC,(c’) ASS,(e’) VVC,(g’) RVVC) C. glabrata with untreated neutrophils. (D – (b’) ATCC,(d’) ASS,(f’) VVC,(h’) RVVC) C. glabrata with neutrophils previously treated with 3 mg/ml β-glucan.

    Journal: PLoS ONE

    Article Title: β-Glucan Induces Reactive Oxygen Species Production in Human Neutrophils to Improve the Killing of Candida albicans and Candida glabrata Isolates from Vulvovaginal Candidiasis

    doi: 10.1371/journal.pone.0107805

    Figure Lengend Snippet: Intracellular oxidant species production by β-glucan-treated neutrophils activated by different isolates of C. albicans and C. glabrata determined by flow cytometry. Neutrophils (2.0×10 6 cells/ml) were previously treated or not with 3 mg/ml β-glucan and incubated for 1 h with the reference strain and different isolates of (A) C. albicans and (B) C. glabrata (RVVC, VVC, and ASS; 2.0×10 7 CFU/ml), followed by 30 min incubation with DHR. The data are expressed as the mean ± SD of at least three independent experiments. * p ≤0.05, significant difference compared with the control group (neutrophils alone); # p ≤0.05, significant difference compared with untreated and activated neutrophils. (C and D) Representative dot plot display of FL1 (green fluorescence) vs . FL2 on a logarithmic scale. (C – (a) ATCC, (c) ASS, (e) VVC,(g) RVVC) C. albicans with untreated neutrophils. (C – (b) ATCC,(d) ASS,(f) VVC,(h) RVVC) C. albicans with neutrophils previously treated with 3 mg/ml β-glucan. (D – (a’) ATCC,(c’) ASS,(e’) VVC,(g’) RVVC) C. glabrata with untreated neutrophils. (D – (b’) ATCC,(d’) ASS,(f’) VVC,(h’) RVVC) C. glabrata with neutrophils previously treated with 3 mg/ml β-glucan.

    Article Snippet: β-glucan β-glucan derived from Laminaria digitata was purchased from Sigma Chemical Co. (St. Louis, MO, USA; L-9634).

    Techniques: Flow Cytometry, Cytometry, Incubation, Fluorescence

    Enzyme-labeled fluorescence (ELF) in situ hybridization control experiments utilizing cultured rat hepatoma cells and formalin-fixed, paraffin-embedded human tissue sections. (A) 22-μM beta-napthoflavone (β-NF)-induced H4IIE rat cells hybridized with rat biotin-conjugated CYP1A1 oligomer. (B) 22-μM β-NF-treated H4IIe rat cells probed with the rat biotin-labeled CYP1A1 20-mer and pretreated with 150 μ/ml of RNase A. (C) 22-μM β-NF-exposed H4IIE rat cells hybridized with rat biotinylated CYP1A1 2Gmer plus 60-fold excess nonbiotinylated rat CYP1A1 probe. (D) Poorly differentiated squamous cell carcinoma of human oral epithelium probed with human CYP1A1 biotin-labeled 20-mer. (E) Poorly differentiated squamous cell carcinoma of human oral epithelium hybridized with the partially homologous rat CYP1A1 biotin-conjugated oligomer probe. (F) Poorly differentiated squamous cell carcinoma of human oral epithelium without the addition of a biotinylated oligomer to the hybridization buffer. Magnification 400×.

    Journal: In vitro toxicology

    Article Title: Detection of Cytochrome P450 mRNA in Tissue Sections and Cell Lines Using Enzyme-Labeled Fluorescence In Situ Hybridization

    doi:

    Figure Lengend Snippet: Enzyme-labeled fluorescence (ELF) in situ hybridization control experiments utilizing cultured rat hepatoma cells and formalin-fixed, paraffin-embedded human tissue sections. (A) 22-μM beta-napthoflavone (β-NF)-induced H4IIE rat cells hybridized with rat biotin-conjugated CYP1A1 oligomer. (B) 22-μM β-NF-treated H4IIe rat cells probed with the rat biotin-labeled CYP1A1 20-mer and pretreated with 150 μ/ml of RNase A. (C) 22-μM β-NF-exposed H4IIE rat cells hybridized with rat biotinylated CYP1A1 2Gmer plus 60-fold excess nonbiotinylated rat CYP1A1 probe. (D) Poorly differentiated squamous cell carcinoma of human oral epithelium probed with human CYP1A1 biotin-labeled 20-mer. (E) Poorly differentiated squamous cell carcinoma of human oral epithelium hybridized with the partially homologous rat CYP1A1 biotin-conjugated oligomer probe. (F) Poorly differentiated squamous cell carcinoma of human oral epithelium without the addition of a biotinylated oligomer to the hybridization buffer. Magnification 400×.

    Article Snippet: Beta-naphthoflavone (β-NF) was purchased from Aldrich Chemical Co. (Milwaukee, WI), and levamisole was acquired from Sigma Chemical Co. (St. Louis, MO).

    Techniques: Labeling, Fluorescence, In Situ Hybridization, Cell Culture, Formalin-fixed Paraffin-Embedded, Hybridization

    Enzyme-labeled fluorescence (ELF) in situ hybridization using a rat biotin-conjugated CYP1A1 oligomer probe with cultured rat hepatoma cells. (A9 untreated H4IIE cells probed with biotinylated CYP1A1 oligomer. (B) 22-μM beta-naphoflavone (β-NF)-treated H4IIE cells hybridized with biotin-labeled CYP1A1 oligomer (C) 22-μM β-NF exposed H4IIE cells lacking the biotinylated CYP1A1 probe from the hybridization solution. (D) Unexposed Fao cells probed with biotinylated CYP1A1 oligomer. (E) 22-μM β-NF-treated Fao cells hybridized with biotin-labeled CYP1A1 oligomer (F) 22-μM β-NF-exposed Fao cells without the biotinylated CYP1A1 probe. Magnification 400×.

    Journal: In vitro toxicology

    Article Title: Detection of Cytochrome P450 mRNA in Tissue Sections and Cell Lines Using Enzyme-Labeled Fluorescence In Situ Hybridization

    doi:

    Figure Lengend Snippet: Enzyme-labeled fluorescence (ELF) in situ hybridization using a rat biotin-conjugated CYP1A1 oligomer probe with cultured rat hepatoma cells. (A9 untreated H4IIE cells probed with biotinylated CYP1A1 oligomer. (B) 22-μM beta-naphoflavone (β-NF)-treated H4IIE cells hybridized with biotin-labeled CYP1A1 oligomer (C) 22-μM β-NF exposed H4IIE cells lacking the biotinylated CYP1A1 probe from the hybridization solution. (D) Unexposed Fao cells probed with biotinylated CYP1A1 oligomer. (E) 22-μM β-NF-treated Fao cells hybridized with biotin-labeled CYP1A1 oligomer (F) 22-μM β-NF-exposed Fao cells without the biotinylated CYP1A1 probe. Magnification 400×.

    Article Snippet: Beta-naphthoflavone (β-NF) was purchased from Aldrich Chemical Co. (Milwaukee, WI), and levamisole was acquired from Sigma Chemical Co. (St. Louis, MO).

    Techniques: Labeling, Fluorescence, In Situ Hybridization, Cell Culture, Hybridization

    STAT1β shows prolonged tyrosine 701 phosphorylation. (A to D) BMMϕ derived from WT (+/+), Stat1 β/β (β/β), and Stat1 α/α (α/α) mice were stimulated with IFN-β (A) or

    Journal: Molecular and Cellular Biology

    Article Title: STAT1β Is Not Dominant Negative and Is Capable of Contributing to Gamma Interferon-Dependent Innate Immunity

    doi: 10.1128/MCB.00295-14

    Figure Lengend Snippet: STAT1β shows prolonged tyrosine 701 phosphorylation. (A to D) BMMϕ derived from WT (+/+), Stat1 β/β (β/β), and Stat1 α/α (α/α) mice were stimulated with IFN-β (A) or

    Article Snippet: Genetic screening of WT, Stat1 α/α , and Stat1 β/β mice was performed by a duplex PCR with primers (purchased from Sigma-Aldrich) using DNA from mouse tail biopsy specimens.

    Techniques: Derivative Assay, Mouse Assay

    STAT1β shows prolonged nuclear localization and prolonged promoter binding after IFN-γ treatment compared to STAT1α. (A) BMMϕ derived from WT (+/+), Stat1 β/β (β/β), and Stat1 α/α

    Journal: Molecular and Cellular Biology

    Article Title: STAT1β Is Not Dominant Negative and Is Capable of Contributing to Gamma Interferon-Dependent Innate Immunity

    doi: 10.1128/MCB.00295-14

    Figure Lengend Snippet: STAT1β shows prolonged nuclear localization and prolonged promoter binding after IFN-γ treatment compared to STAT1α. (A) BMMϕ derived from WT (+/+), Stat1 β/β (β/β), and Stat1 α/α

    Article Snippet: Genetic screening of WT, Stat1 α/α , and Stat1 β/β mice was performed by a duplex PCR with primers (purchased from Sigma-Aldrich) using DNA from mouse tail biopsy specimens.

    Techniques: Binding Assay, Derivative Assay

    STAT1α and STAT1β can mediate type I and type III IFN-dependent antiviral immunity in vivo . (A) EMCV (50 PFU/mouse) was administered i.p. to WT ( Stat1 +/+ ), Stat1 β/β , Stat1 α/α , and Stat1 −/−

    Journal: Molecular and Cellular Biology

    Article Title: STAT1β Is Not Dominant Negative and Is Capable of Contributing to Gamma Interferon-Dependent Innate Immunity

    doi: 10.1128/MCB.00295-14

    Figure Lengend Snippet: STAT1α and STAT1β can mediate type I and type III IFN-dependent antiviral immunity in vivo . (A) EMCV (50 PFU/mouse) was administered i.p. to WT ( Stat1 +/+ ), Stat1 β/β , Stat1 α/α , and Stat1 −/−

    Article Snippet: Genetic screening of WT, Stat1 α/α , and Stat1 β/β mice was performed by a duplex PCR with primers (purchased from Sigma-Aldrich) using DNA from mouse tail biopsy specimens.

    Techniques: In Vivo

    STAT1β is transcriptionally active in response to IFN-β and IFN-γ. BMMϕ isolated from WT (+/+), Stat1 β/β (β/β), Stat1 α/α (α/α), and Stat1 −/−

    Journal: Molecular and Cellular Biology

    Article Title: STAT1β Is Not Dominant Negative and Is Capable of Contributing to Gamma Interferon-Dependent Innate Immunity

    doi: 10.1128/MCB.00295-14

    Figure Lengend Snippet: STAT1β is transcriptionally active in response to IFN-β and IFN-γ. BMMϕ isolated from WT (+/+), Stat1 β/β (β/β), Stat1 α/α (α/α), and Stat1 −/−

    Article Snippet: Genetic screening of WT, Stat1 α/α , and Stat1 β/β mice was performed by a duplex PCR with primers (purchased from Sigma-Aldrich) using DNA from mouse tail biopsy specimens.

    Techniques: Isolation

    STAT1α and STAT1β show differential efficiencies in immune defense against MCMV and L. monocytogenes infections. (A) WT ( Stat1 +/+ ), Stat1 β/β , Stat1 α/α , and Stat1 −/− mice were infected i.p.

    Journal: Molecular and Cellular Biology

    Article Title: STAT1β Is Not Dominant Negative and Is Capable of Contributing to Gamma Interferon-Dependent Innate Immunity

    doi: 10.1128/MCB.00295-14

    Figure Lengend Snippet: STAT1α and STAT1β show differential efficiencies in immune defense against MCMV and L. monocytogenes infections. (A) WT ( Stat1 +/+ ), Stat1 β/β , Stat1 α/α , and Stat1 −/− mice were infected i.p.

    Article Snippet: Genetic screening of WT, Stat1 α/α , and Stat1 β/β mice was performed by a duplex PCR with primers (purchased from Sigma-Aldrich) using DNA from mouse tail biopsy specimens.

    Techniques: Mouse Assay, Infection

    Transcriptional activities of STAT1α and STAT1β overlap but are nonredundant. BMMϕ isolated from WT (+/+), Stat1 β/β (β/β), Stat1 α/α (α/α), and Stat1 −/−

    Journal: Molecular and Cellular Biology

    Article Title: STAT1β Is Not Dominant Negative and Is Capable of Contributing to Gamma Interferon-Dependent Innate Immunity

    doi: 10.1128/MCB.00295-14

    Figure Lengend Snippet: Transcriptional activities of STAT1α and STAT1β overlap but are nonredundant. BMMϕ isolated from WT (+/+), Stat1 β/β (β/β), Stat1 α/α (α/α), and Stat1 −/−

    Article Snippet: Genetic screening of WT, Stat1 α/α , and Stat1 β/β mice was performed by a duplex PCR with primers (purchased from Sigma-Aldrich) using DNA from mouse tail biopsy specimens.

    Techniques: Isolation

    Mineral shells formed from [W/O/W] double emulsions support in vitro protein expression. ( A ) Schematic overview of the second, double emulsion–producing, flow-focusing junction of a two-junction flow-focusing microfluidic device used to generate mineralized double emulsions (see fig. S10 and movie S4). ( B ) Schematic of [W/O/W] droplet mineralization to form an interfacial mineral layer around bacterial extracts in the innermost water phase. Here, “S” is a fluorogenic substrate (CCF2) that changes emission properties when enzymatically converted to product (“P”) by β-lactamase (β-lac) enzyme. ( C ) Polarized light optical micrograph shows interfacial birefringence. ( D ) Flow cytometry scatter plots of 50,000 droplets, proving that mineralized droplets support compartmentalized in vitro protein expression.

    Journal: Science Advances

    Article Title: Combinatorial microfluidic droplet engineering for biomimetic material synthesis

    doi: 10.1126/sciadv.1600567

    Figure Lengend Snippet: Mineral shells formed from [W/O/W] double emulsions support in vitro protein expression. ( A ) Schematic overview of the second, double emulsion–producing, flow-focusing junction of a two-junction flow-focusing microfluidic device used to generate mineralized double emulsions (see fig. S10 and movie S4). ( B ) Schematic of [W/O/W] droplet mineralization to form an interfacial mineral layer around bacterial extracts in the innermost water phase. Here, “S” is a fluorogenic substrate (CCF2) that changes emission properties when enzymatically converted to product (“P”) by β-lactamase (β-lac) enzyme. ( C ) Polarized light optical micrograph shows interfacial birefringence. ( D ) Flow cytometry scatter plots of 50,000 droplets, proving that mineralized droplets support compartmentalized in vitro protein expression.

    Article Snippet: Soluble bacterial extracts, including a gene coding for β-lactamase, were used as the internal water phase ( , fig. S10, and movie S5). β-Lactamase was selected as an enzyme reporter rather than inherently fluorescent proteins to take advantage of the potential for fluorescence signal amplification: β-lactamase cleavage of a fluorogenic substrate (“CCF2,” Sigma; emission, 518 nm) generates a large excess of fluorescent small-molecule product (emission, 447 nm) relative to the number of β-lactamase proteins produced within the droplets, thus helping ensure that β-lactamase production within droplets can be measured using a commercial flow cytometer.

    Techniques: In Vitro, Expressing, Flow Cytometry, Cytometry

    ROS reagents inhibit the activity of the SMN complex in vitro and in cells (A) Effect of H 2 O 2 on the activity of the SMN complex in vitro . Magnetic beads snRNP assembly assay was carried out in the presence of increasing amounts of H 2 O 2 . IC 50 was calculated from the dose-response curve. Error bars represent SDs from triplicate measurements. (B) Effect of menadione on SMN complex activity in vitro . The same experimental procedure was carried out as in (A), except that menadione was used instead. (C) Dose-dependent effect of menadione on SMN complex activity in cells. HeLa cells were treated with menadione at the indicated concentrations or with DMSO control for 1 hour. SMN complex activity in extracts from various treated cells was measured in comparison to DMSO control cell extract (100% activity) by magnetic beads snRNP assembly assay. Error bars represent SDs from 3 independent measurements. (D) Extracts from (C) mixed with sample buffer without or with DTT were resolved by SDS-PAGE and analyzed by Western blot of the entire membrane with anti-SMN antibody 62E7. The molecular mass markers in kDa are indicated on the left. “redSMN” indicates monomer SMN migrating at normal molecular mass and “oxSMN” indicates disulfide-crosslinked SMN upon oxidation. (E) β-lapachone and menadione generate ROS in live cells. HeLa cells were incubated 30 minutes with ROS indicator dye H 2 DCFDA (10 μM) or without dye as a control, then treated with compounds at indicated concentrations or DMSO as control. Fluorescence images were acquired 30 minutes after treatment.

    Journal: Molecular cell

    Article Title: Inactivation of the SMN complex by Oxidative Stress

    doi: 10.1016/j.molcel.2008.06.004

    Figure Lengend Snippet: ROS reagents inhibit the activity of the SMN complex in vitro and in cells (A) Effect of H 2 O 2 on the activity of the SMN complex in vitro . Magnetic beads snRNP assembly assay was carried out in the presence of increasing amounts of H 2 O 2 . IC 50 was calculated from the dose-response curve. Error bars represent SDs from triplicate measurements. (B) Effect of menadione on SMN complex activity in vitro . The same experimental procedure was carried out as in (A), except that menadione was used instead. (C) Dose-dependent effect of menadione on SMN complex activity in cells. HeLa cells were treated with menadione at the indicated concentrations or with DMSO control for 1 hour. SMN complex activity in extracts from various treated cells was measured in comparison to DMSO control cell extract (100% activity) by magnetic beads snRNP assembly assay. Error bars represent SDs from 3 independent measurements. (D) Extracts from (C) mixed with sample buffer without or with DTT were resolved by SDS-PAGE and analyzed by Western blot of the entire membrane with anti-SMN antibody 62E7. The molecular mass markers in kDa are indicated on the left. “redSMN” indicates monomer SMN migrating at normal molecular mass and “oxSMN” indicates disulfide-crosslinked SMN upon oxidation. (E) β-lapachone and menadione generate ROS in live cells. HeLa cells were incubated 30 minutes with ROS indicator dye H 2 DCFDA (10 μM) or without dye as a control, then treated with compounds at indicated concentrations or DMSO as control. Fluorescence images were acquired 30 minutes after treatment.

    Article Snippet: For confirmation studies and treatment on cells, β-lapachone, H2 O2 , cumene hydroperoxide, and menadione were purchased from Sigma-Aldrich Chemical Co.

    Techniques: Activity Assay, In Vitro, Magnetic Beads, SDS Page, Western Blot, Incubation, Fluorescence

    ROS mapping of disulfide-crosslinked cysteines in SMN (A) Sequence alignment of human ( Homo sapien s), mouse ( Mus musculus ), and frog ( Xenopus laevies ) SMN protein sequences. Conserved residues are shaded in gray. Cysteine residues are highlighted. Exons and their boundaries are indicated with opposite-directed arrows. The schematic diagram shows SMN protein domain organization and positions of cysteines. Two cysteines (C60 and C250) that form disulfide bridges are marked (-S-S-). (B) Human SMN protein (WT, wild type; ΔEx7, exon7 deletion mutant; no Cys, mutation of all 8 cysteines to alanines; C60, C98, C123, and C250, mutation of 7 cysteines to alanines except for cysteine at positions 60, 98, 123, and 250, respectively) were produced by in vitro transcription and translation in the presence of 35 S-Met and then treated with 40 μM β-lapachone or DMSO for 1 hour. Samples were mixed with sample buffer without DTT, and then analyzed by SDS-PAGE and autoradiography. Molecular mass markers in kDa are indicated on the left. Protein bands corresponding to monomer SMN (redSMN), disulfide-crosslinked SMN (oxSMN) and SMN dimer (oxSMN dimer) are indicated on the right. (C) SMN amino terminus deletion (Ex3-7) and carboxyl terminus deletion (Ex1-4) mutants were tested for crosslinking, as described in panel (B). Note that these mutants were constructed in pcDNA3-myc-pyruvate kinase (PK, ~60kD) vector to facilitate detection of otherwise small fragments.

    Journal: Molecular cell

    Article Title: Inactivation of the SMN complex by Oxidative Stress

    doi: 10.1016/j.molcel.2008.06.004

    Figure Lengend Snippet: ROS mapping of disulfide-crosslinked cysteines in SMN (A) Sequence alignment of human ( Homo sapien s), mouse ( Mus musculus ), and frog ( Xenopus laevies ) SMN protein sequences. Conserved residues are shaded in gray. Cysteine residues are highlighted. Exons and their boundaries are indicated with opposite-directed arrows. The schematic diagram shows SMN protein domain organization and positions of cysteines. Two cysteines (C60 and C250) that form disulfide bridges are marked (-S-S-). (B) Human SMN protein (WT, wild type; ΔEx7, exon7 deletion mutant; no Cys, mutation of all 8 cysteines to alanines; C60, C98, C123, and C250, mutation of 7 cysteines to alanines except for cysteine at positions 60, 98, 123, and 250, respectively) were produced by in vitro transcription and translation in the presence of 35 S-Met and then treated with 40 μM β-lapachone or DMSO for 1 hour. Samples were mixed with sample buffer without DTT, and then analyzed by SDS-PAGE and autoradiography. Molecular mass markers in kDa are indicated on the left. Protein bands corresponding to monomer SMN (redSMN), disulfide-crosslinked SMN (oxSMN) and SMN dimer (oxSMN dimer) are indicated on the right. (C) SMN amino terminus deletion (Ex3-7) and carboxyl terminus deletion (Ex1-4) mutants were tested for crosslinking, as described in panel (B). Note that these mutants were constructed in pcDNA3-myc-pyruvate kinase (PK, ~60kD) vector to facilitate detection of otherwise small fragments.

    Article Snippet: For confirmation studies and treatment on cells, β-lapachone, H2 O2 , cumene hydroperoxide, and menadione were purchased from Sigma-Aldrich Chemical Co.

    Techniques: Sequencing, Mutagenesis, Produced, In Vitro, SDS Page, Autoradiography, Construct, Plasmid Preparation

    β-lapachone potently and selectively inhibits the SMN complex-mediated snRNP assembly in vitro and in cells (A) Chemical structure of β-lapachone. (B) Concentration-dependent inhibition of SMN complex activity by β-lapachone in cells. HeLa cells were treated with various concentrations of β-lapachone or with DMSO (control) for 1 hour. SMN complex activity in extracts from treated cells was measured using magnetic beads snRNP assembly assay and compared to DMSO-treated control cells (100% activity). IC 50 was calculated from the dose-reponse graph. Error bars represent SDs from 3 independent measurements. (C) β-lapachone selectively inhibits SMN complex-mediated Sm core assembly. Assembly reactions were performed using either cell extracts or purified native snRNP proteins lacking the SMN complex (Sm proteins). Both samples were adjusted to contain a similar amount of Sm proteins. Magnetic beads snRNP assembly assay was carried out with U4 or control U4ΔSm snRNA in the presence of either 20 or 100 μM β-lapachone or DMSO control. Sm core assembly on U4 snRNA in the presence of DMSO was considered 100% activity. The error bars represent SDs from 3 independent measurements.

    Journal: Molecular cell

    Article Title: Inactivation of the SMN complex by Oxidative Stress

    doi: 10.1016/j.molcel.2008.06.004

    Figure Lengend Snippet: β-lapachone potently and selectively inhibits the SMN complex-mediated snRNP assembly in vitro and in cells (A) Chemical structure of β-lapachone. (B) Concentration-dependent inhibition of SMN complex activity by β-lapachone in cells. HeLa cells were treated with various concentrations of β-lapachone or with DMSO (control) for 1 hour. SMN complex activity in extracts from treated cells was measured using magnetic beads snRNP assembly assay and compared to DMSO-treated control cells (100% activity). IC 50 was calculated from the dose-reponse graph. Error bars represent SDs from 3 independent measurements. (C) β-lapachone selectively inhibits SMN complex-mediated Sm core assembly. Assembly reactions were performed using either cell extracts or purified native snRNP proteins lacking the SMN complex (Sm proteins). Both samples were adjusted to contain a similar amount of Sm proteins. Magnetic beads snRNP assembly assay was carried out with U4 or control U4ΔSm snRNA in the presence of either 20 or 100 μM β-lapachone or DMSO control. Sm core assembly on U4 snRNA in the presence of DMSO was considered 100% activity. The error bars represent SDs from 3 independent measurements.

    Article Snippet: For confirmation studies and treatment on cells, β-lapachone, H2 O2 , cumene hydroperoxide, and menadione were purchased from Sigma-Aldrich Chemical Co.

    Techniques: In Vitro, Concentration Assay, Inhibition, Activity Assay, Magnetic Beads, Purification

    SMN protein is oxidized to form intermolecular disulfide bonds upon β-lapachone treatment (A) Indirect immunofluorescence staining of SMN (2B1; green) and snRNPs (Y12; red) in HeLa PV cells treated 3 hours with 5 μM β-lapachone or DMSO control. (B) HeLa total cell extracts prepared from cells treated 3 hours with 5 μM β-lapachone or DMSO control were resolved by SDS-PAGE and analyzed by quantitative Western blotting, using JBP1 and Magoh as loading controls. Extracts were prepared and mixed with sample buffer without DTT. The membrane was cut into strips for probing of each protein at the corresponding molecular mass. ) were used for in vitro assembly reactions in the presence of either 100 μM β-lapachone or DMSO control. The SMN complex was isolated by anti-Flag immunoprecipitation, mixed with sample buffer without or with DTT and resolved by SDS-PAGE. Western blot analysis was performed on the entire membrane with anti-SMN antibody 62E7. Molecular mass markers in kDa are indicated on the left. “redSMN” indicates monomer SMN migrating at normal molecular mass and “oxSMN” indicates disulfide-crosslinked SMN upon oxidation.

    Journal: Molecular cell

    Article Title: Inactivation of the SMN complex by Oxidative Stress

    doi: 10.1016/j.molcel.2008.06.004

    Figure Lengend Snippet: SMN protein is oxidized to form intermolecular disulfide bonds upon β-lapachone treatment (A) Indirect immunofluorescence staining of SMN (2B1; green) and snRNPs (Y12; red) in HeLa PV cells treated 3 hours with 5 μM β-lapachone or DMSO control. (B) HeLa total cell extracts prepared from cells treated 3 hours with 5 μM β-lapachone or DMSO control were resolved by SDS-PAGE and analyzed by quantitative Western blotting, using JBP1 and Magoh as loading controls. Extracts were prepared and mixed with sample buffer without DTT. The membrane was cut into strips for probing of each protein at the corresponding molecular mass. ) were used for in vitro assembly reactions in the presence of either 100 μM β-lapachone or DMSO control. The SMN complex was isolated by anti-Flag immunoprecipitation, mixed with sample buffer without or with DTT and resolved by SDS-PAGE. Western blot analysis was performed on the entire membrane with anti-SMN antibody 62E7. Molecular mass markers in kDa are indicated on the left. “redSMN” indicates monomer SMN migrating at normal molecular mass and “oxSMN” indicates disulfide-crosslinked SMN upon oxidation.

    Article Snippet: For confirmation studies and treatment on cells, β-lapachone, H2 O2 , cumene hydroperoxide, and menadione were purchased from Sigma-Aldrich Chemical Co.

    Techniques: Immunofluorescence, Staining, SDS Page, Western Blot, In Vitro, Isolation, Immunoprecipitation

    DTT prevents the inhibition of the activity of the SMN complex by β-lapachone Cell extracts treated with 20 μM β-lapachone, or 20 μM β-lapachone together with 20 mM DTT, or DMSO control were analyzed by non-reducing Western blot. The relative levels of monomer SMN (“redSMN”) were calculated as the percentage of that in DMSO control and shown by the blue bar. Assembly activities of the SMN complex were measured by magnetic beads snRNP assembly assay using the same set of treated extracts and shown by the red bar. Error bars represent SDs from 3 independent experiments.

    Journal: Molecular cell

    Article Title: Inactivation of the SMN complex by Oxidative Stress

    doi: 10.1016/j.molcel.2008.06.004

    Figure Lengend Snippet: DTT prevents the inhibition of the activity of the SMN complex by β-lapachone Cell extracts treated with 20 μM β-lapachone, or 20 μM β-lapachone together with 20 mM DTT, or DMSO control were analyzed by non-reducing Western blot. The relative levels of monomer SMN (“redSMN”) were calculated as the percentage of that in DMSO control and shown by the blue bar. Assembly activities of the SMN complex were measured by magnetic beads snRNP assembly assay using the same set of treated extracts and shown by the red bar. Error bars represent SDs from 3 independent experiments.

    Article Snippet: For confirmation studies and treatment on cells, β-lapachone, H2 O2 , cumene hydroperoxide, and menadione were purchased from Sigma-Aldrich Chemical Co.

    Techniques: Inhibition, Activity Assay, Western Blot, Magnetic Beads

    Excretion of β-HBCD-derived radioactivity over time following single doses of 3, 30, or 100mg/kg by gavage. Values are the mean ± SD of four mice. *The value is significantly higher than that for the 100mg/kg group ( p

    Journal: Toxicological Sciences

    Article Title: The Fate of β-Hexabromocyclododecane in Female C57BL/6 Mice

    doi: 10.1093/toxsci/kft121

    Figure Lengend Snippet: Excretion of β-HBCD-derived radioactivity over time following single doses of 3, 30, or 100mg/kg by gavage. Values are the mean ± SD of four mice. *The value is significantly higher than that for the 100mg/kg group ( p

    Article Snippet: For iv administration, β-HBCD in toluene was added to one part Cremophor EL (Sigma-Aldrich, St Louis, MO).

    Techniques: Derivative Assay, Radioactivity, Mouse Assay

    β-HBCD-derived radioactivity remaining in tissues 4 days following single doses of 3, 30, or 100mg/kg by gavage. Values are the mean ± SD for three to four mice. *The value is significantly higher than that for the 3mg/kg group ( p

    Journal: Toxicological Sciences

    Article Title: The Fate of β-Hexabromocyclododecane in Female C57BL/6 Mice

    doi: 10.1093/toxsci/kft121

    Figure Lengend Snippet: β-HBCD-derived radioactivity remaining in tissues 4 days following single doses of 3, 30, or 100mg/kg by gavage. Values are the mean ± SD for three to four mice. *The value is significantly higher than that for the 3mg/kg group ( p

    Article Snippet: For iv administration, β-HBCD in toluene was added to one part Cremophor EL (Sigma-Aldrich, St Louis, MO).

    Techniques: Derivative Assay, Radioactivity, Mouse Assay

    β-HBCD-derived radioactivity remaining in tissues and cumulatively excreted 24h following oral and iv administration of 3mg/kg. Values are for the mean ± SD of four mice. *The value is significantly different from the corresponding value

    Journal: Toxicological Sciences

    Article Title: The Fate of β-Hexabromocyclododecane in Female C57BL/6 Mice

    doi: 10.1093/toxsci/kft121

    Figure Lengend Snippet: β-HBCD-derived radioactivity remaining in tissues and cumulatively excreted 24h following oral and iv administration of 3mg/kg. Values are for the mean ± SD of four mice. *The value is significantly different from the corresponding value

    Article Snippet: For iv administration, β-HBCD in toluene was added to one part Cremophor EL (Sigma-Aldrich, St Louis, MO).

    Techniques: Derivative Assay, Radioactivity, Mouse Assay

    Histochemical detection of β-glucosidase activity in mouse tissues . (a, b) Cryostat sections of snap frozen small intestine from non-transgenic mice stained with BCI-glu. (a) Endogenous activity in the villus brush-border. (b) No activity following incubation at 65°C for 20 min. (c-i) BCI-glu staining of tissues from R26 SYNbglA R (left of panel) and PGKcre m /R26 SYNbglA R (right of panel) mice: (c) heart and thymus, (d) spleen and pancreas, (e) kidney, (f) skeletal muscle, (g) liver, (h) glandular stomach and (i) brain. (j, k) Small intestinal wholemounts heat treated at 65°C and stained with BCI-glu from: (j) untreated Ahcre/R26 SYNbglA R; (k) β-napthoflavone treated Ahcre/R26 SYNbglA R mice (4 weeks post induction), showing detectable enzyme activity only in (k). (l-o) Wholemount of colon from an Ahcre/R26 SYNbglA R mouse prepared 16 weeks after β-napthoflavone treatment and stained with Mag-glu (p, proximal; d, distal). (l) Extensive recombination occurs throughout as indicated by magenta staining but becomes increasingly variegated towards the distal end. (m-o) Shows enlargements of areas indicated by arrows. Punctate magenta staining corresponds to individual colonic crypts. Bars: A, B 200 μm, C-O 1 cm.

    Journal: BMC Biology

    Article Title: Characterization of a heat resistant ss-glucosidase as a new reporter in cells and mice

    doi: 10.1186/1741-7007-8-89

    Figure Lengend Snippet: Histochemical detection of β-glucosidase activity in mouse tissues . (a, b) Cryostat sections of snap frozen small intestine from non-transgenic mice stained with BCI-glu. (a) Endogenous activity in the villus brush-border. (b) No activity following incubation at 65°C for 20 min. (c-i) BCI-glu staining of tissues from R26 SYNbglA R (left of panel) and PGKcre m /R26 SYNbglA R (right of panel) mice: (c) heart and thymus, (d) spleen and pancreas, (e) kidney, (f) skeletal muscle, (g) liver, (h) glandular stomach and (i) brain. (j, k) Small intestinal wholemounts heat treated at 65°C and stained with BCI-glu from: (j) untreated Ahcre/R26 SYNbglA R; (k) β-napthoflavone treated Ahcre/R26 SYNbglA R mice (4 weeks post induction), showing detectable enzyme activity only in (k). (l-o) Wholemount of colon from an Ahcre/R26 SYNbglA R mouse prepared 16 weeks after β-napthoflavone treatment and stained with Mag-glu (p, proximal; d, distal). (l) Extensive recombination occurs throughout as indicated by magenta staining but becomes increasingly variegated towards the distal end. (m-o) Shows enlargements of areas indicated by arrows. Punctate magenta staining corresponds to individual colonic crypts. Bars: A, B 200 μm, C-O 1 cm.

    Article Snippet: For induction of the Ah promoter, mice received interperitoneal injections of 80 mg/kg β-napthoflavone (βNF; Sigma) dissolved in corn oil (8 mg/mL) at the frequencies stated and controls received either no treatment or corn oil only.

    Techniques: Activity Assay, Transgenic Assay, Mouse Assay, Staining, Incubation

    Evaluation of the signaling pathways triggered by β-hexaclorocyclohexane (β-HCH). Immunoblot analysis of the time-course assay performed on human prostate cancer (LNCaP), human breast cancer (MCF-7 and MDA-MB 468), and human hepatoma (HepG2) cells treated with 10 μM β-HCH. Samples were analyzed for signal transducer and activator of transcription 3 (STAT3) and each cell line for a specific membrane or membrane associated tyrosine kinase receptor: EGFR in MDA-MB 468 cells, JAK2 in HepG2 cells, SRC in LNCaP cells and HER2 in MCF-7 cells. Both unmodified and the corresponding phosphorylated form were detected for each protein using specific antibodies.

    Journal: International Journal of Molecular Sciences

    Article Title: STAT3, a Hub Protein of Cellular Signaling Pathways, Is Triggered by β-Hexaclorocyclohexane

    doi: 10.3390/ijms19072108

    Figure Lengend Snippet: Evaluation of the signaling pathways triggered by β-hexaclorocyclohexane (β-HCH). Immunoblot analysis of the time-course assay performed on human prostate cancer (LNCaP), human breast cancer (MCF-7 and MDA-MB 468), and human hepatoma (HepG2) cells treated with 10 μM β-HCH. Samples were analyzed for signal transducer and activator of transcription 3 (STAT3) and each cell line for a specific membrane or membrane associated tyrosine kinase receptor: EGFR in MDA-MB 468 cells, JAK2 in HepG2 cells, SRC in LNCaP cells and HER2 in MCF-7 cells. Both unmodified and the corresponding phosphorylated form were detected for each protein using specific antibodies.

    Article Snippet: Beta-hexaclorocyclohexane (β-HCH) (Sigma-Aldrich, 33376), at a final concentration of 10 μM, was tested on each cell line pre-treated or not with specific inhibitors: 6 μM AZD1480 (Sigma-Aldrich, SML1505), 100 μM S3I-201 (Sigma-Aldrich, SML0330), 70 nM Dasatinib (Selleckchem, Roma, Italy, Cat. No. S1021), 0.8 μM Lapatinib (Sigma-Aldrich, CDS022971), and 15 μM Gefitinib (Sigma-Aldrich, SLM1657).

    Techniques: Multiple Displacement Amplification

    Transformation of β-tetralone ( 3 ) in the culture of Chaetomium sp . KCh 6651

    Journal: Current Microbiology

    Article Title: Enantioselective Dynamic Process Reduction of ?- and ?-Tetralone and Stereoinversion of Resulting Alcohols in a Selected Strain Culture

    doi: 10.1007/s00284-012-0143-2

    Figure Lengend Snippet: Transformation of β-tetralone ( 3 ) in the culture of Chaetomium sp . KCh 6651

    Article Snippet: Materials The substrates: α-tetralone ( 1 ) and β-tetralone ( 3 ) were purchased from Sigma-Aldrich.

    Techniques: Transformation Assay

    Time dependence of the transformation of β-tetralone ( 3 ) in Chaetomium sp . KCh 6651 culture

    Journal: Current Microbiology

    Article Title: Enantioselective Dynamic Process Reduction of ?- and ?-Tetralone and Stereoinversion of Resulting Alcohols in a Selected Strain Culture

    doi: 10.1007/s00284-012-0143-2

    Figure Lengend Snippet: Time dependence of the transformation of β-tetralone ( 3 ) in Chaetomium sp . KCh 6651 culture

    Article Snippet: Materials The substrates: α-tetralone ( 1 ) and β-tetralone ( 3 ) were purchased from Sigma-Aldrich.

    Techniques: Transformation Assay

    Level of β-Gal expression in five parental clones established for RMCE. The parental construct containing a hyg-tk fusion gene under the control of a tk promoter (pTK) is exchanged for a lacZ-neo fusion gene cassette that resides on the exchange

    Journal: Molecular and Cellular Biology

    Article Title: Performance of Genomic Bordering Elements at Predefined Genomic Loci

    doi: 10.1128/MCB.25.6.2260-2272.2005

    Figure Lengend Snippet: Level of β-Gal expression in five parental clones established for RMCE. The parental construct containing a hyg-tk fusion gene under the control of a tk promoter (pTK) is exchanged for a lacZ-neo fusion gene cassette that resides on the exchange

    Article Snippet: Readings for each sample were determined in triplicate, corrected for the cell number, and referred to a known concentration of purified β-Gal (Sigma).

    Techniques: Expressing, Clone Assay, Construct