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Bio-Rad • thin walled
• Thin Walled, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Polymerase Chain Reaction:

Article Title: Patch-Seq Protocol to Analyze the Electrophysiology, Morphology and Transcriptome of Whole Single Neurons Derived From Human Pluripotent Stem Cells
Article Snippet: .. Consumables • Nonstick, RNase-free 1.5-ml microfuge tubes (Thermo Fisher Scientific, AM12450) • Sterile filter pipette tips 10, 30, 100, 200, and 1000 μl (Gilson, DIAMOND) • Sterile serological pipettes 2, 5, 10, and 25 ml (Corning, 4486-4489) • Sterile aspirating pipettes 2 ml (Corning, 9186) • Thin-walled 0.2-ml PCR tubes (Bio-Rad, TFI-0201) • Borosilicate capillary glass with filament, o.d. .. 0.86 mm, length 100 mm (Sutter Instrument, BF150-86-10) • Parafilm (Sigma-Aldrich, P7793) • 96-well PCR reaction plates (Thermo Fisher Scientific, MicroAmp) • 48-well tissue culture plates, sterile, tissue culture-treated (Corning, 3548) • 24-well tissue culture plates, sterile, tissue culture-treated (Corning, 3524) • Conical tubes 15 ml (Corning, 430828) • Conical tubes 50 ml (Corning, 430828) • Coverslips for 24-well plates, 12 mm diameter, No. 1 thickness (ProScitech, G401-12) • Coverslips for 48-well plates, 8 mm diameter, No. 1 thickness (ProScitech, G401-08) • Sterile disposable reagent reservoirs (Corning, 4870) • Delicate task kimwipes (KimTech Science by Kimberly Clark, 34133) • Saran wrap

Transferring:

Article Title: Patch-Seq Protocol to Analyze the Electrophysiology, Morphology and Transcriptome of Whole Single Neurons Derived From Human Pluripotent Stem Cells
Article Snippet: .. Consumables • Nonstick, RNase-free 1.5-ml microfuge tubes (Thermo Fisher Scientific, AM12450) • Sterile filter pipette tips 10, 30, 100, 200, and 1000 μl (Gilson, DIAMOND) • Sterile serological pipettes 2, 5, 10, and 25 ml (Corning, 4486-4489) • Sterile aspirating pipettes 2 ml (Corning, 9186) • Thin-walled 0.2-ml PCR tubes (Bio-Rad, TFI-0201) • Borosilicate capillary glass with filament, o.d. .. 0.86 mm, length 100 mm (Sutter Instrument, BF150-86-10) • Parafilm (Sigma-Aldrich, P7793) • 96-well PCR reaction plates (Thermo Fisher Scientific, MicroAmp) • 48-well tissue culture plates, sterile, tissue culture-treated (Corning, 3548) • 24-well tissue culture plates, sterile, tissue culture-treated (Corning, 3524) • Conical tubes 15 ml (Corning, 430828) • Conical tubes 50 ml (Corning, 430828) • Coverslips for 24-well plates, 12 mm diameter, No. 1 thickness (ProScitech, G401-12) • Coverslips for 48-well plates, 8 mm diameter, No. 1 thickness (ProScitech, G401-08) • Sterile disposable reagent reservoirs (Corning, 4870) • Delicate task kimwipes (KimTech Science by Kimberly Clark, 34133) • Saran wrap

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    Bio-Rad iref 2 fraction
    Products of influenza virus replication factor <t>(IREF-2)-dependent</t> unprimed RNA synthesis. ( A ) RNase T2 protection assay. Radioactively labeled vRNA products were synthesized in the cell-free viral RNA synthesis system with micrococcal nuclease-treated vRNP (mnRNP) and the v53 model template in the presence of ApG (lanes 1–3), the c53 model template in the presence of ApG (lanes 4–6), and c53 in the presence of the IREF-2 fraction and in the absence of ApG (lanes 7–9). Viral RNA products were hybridized with excess amounts of nonlabeled v53 (lanes 2, 5, and 8) or c53 (lanes 3, 6, and 9), which was followed by digestion with RNase T2. Hybridized and digested RNA samples were extracted, collected, and subjected to 10% Urea-PAGE followed by autoradiography visualization. The closed arrowhead indicates 53-nt-long RNAs. ( B ) Analysis of the 5'-terminal structure of IREF-2-dependent unprimed vRNA products. [α- 32 P] GTP-labeled IREF-2-dependent unprimed vRNA products were prepared in the cell-free viral RNA synthesis system. The radioactively labeled 53-nt-long vRNA products were isolated from 10% Urea-PAGE, which was followed by excision and elution from the gel. A portion of the isolated 53-nt-long products was treated with alkaline phosphatase (lanes 2 and 4). Both nontreated and alkaline phosphatase-treated [α- 32 P] GTP-labeled unprimed vRNA products were digested with RNase T2 (lanes 1–4) or snake venom phosphodiesterase (lane 5). The digested materials were spotted onto a polyethylenimine (PEI)-cellulose thin layer and developed with 1 N acetic acid-4 M LiCl (4:1, v/v) (left panel; lanes 1 and 2) or 1.6 M LiCl (right panel; lanes 3–6) and visualized by autoradiography. For mobility standards, nonradiolabeled AMP, ADP, and ATP were also subjected to thin-layer chromatography and are indicated on the left side of each panel. For a marker of pppAp, [γ- 32 P] ATP-labeled v53 synthesized using T7 RNA polymerase was also subjected to RNase T2 digestion and then to thin-layer chromatography (lane 6). The expected nucleotide positions are indicated on the right side of each panel by closed arrowheads. DOI: http://dx.doi.org/10.7554/eLife.08939.004
    Iref 2 Fraction, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/iref 2 fraction/product/Bio-Rad
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    90
    Bio-Rad mutant strain h1246
    Functional identification of MiPDAT in Saccharomyces cerevisiae <t>H1246.</t> ( A ) Lipid analysis of Saccharomyces cerevisiae by TLC. Lane 1: H1246 mutant; Lane 2: H1246 mutant transformed with pY-MiPDAT; Lane 3: triolein standard purchased from Nu Chek Prep, Inc. (UK); Lane 4: SCY62 (wild-type); Lane 5: H1246 transformed with empty pYES2. ( B ) Fluorescent staining of yeast cells with BODIPY. Lipid bodies where neutral lipids accumulated were visualized in the yeast cells with BODIPY fluorescence. The wild-type strain Scy62 was used as a positive control. The mutant H1246 and the mutant harbouring the empty vector (pYES2) were used as negative controls. The mutant expressing MiPDAT was analysed. All bars in the image B represent a length of 5 μm.
    Mutant Strain H1246, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Products of influenza virus replication factor (IREF-2)-dependent unprimed RNA synthesis. ( A ) RNase T2 protection assay. Radioactively labeled vRNA products were synthesized in the cell-free viral RNA synthesis system with micrococcal nuclease-treated vRNP (mnRNP) and the v53 model template in the presence of ApG (lanes 1–3), the c53 model template in the presence of ApG (lanes 4–6), and c53 in the presence of the IREF-2 fraction and in the absence of ApG (lanes 7–9). Viral RNA products were hybridized with excess amounts of nonlabeled v53 (lanes 2, 5, and 8) or c53 (lanes 3, 6, and 9), which was followed by digestion with RNase T2. Hybridized and digested RNA samples were extracted, collected, and subjected to 10% Urea-PAGE followed by autoradiography visualization. The closed arrowhead indicates 53-nt-long RNAs. ( B ) Analysis of the 5'-terminal structure of IREF-2-dependent unprimed vRNA products. [α- 32 P] GTP-labeled IREF-2-dependent unprimed vRNA products were prepared in the cell-free viral RNA synthesis system. The radioactively labeled 53-nt-long vRNA products were isolated from 10% Urea-PAGE, which was followed by excision and elution from the gel. A portion of the isolated 53-nt-long products was treated with alkaline phosphatase (lanes 2 and 4). Both nontreated and alkaline phosphatase-treated [α- 32 P] GTP-labeled unprimed vRNA products were digested with RNase T2 (lanes 1–4) or snake venom phosphodiesterase (lane 5). The digested materials were spotted onto a polyethylenimine (PEI)-cellulose thin layer and developed with 1 N acetic acid-4 M LiCl (4:1, v/v) (left panel; lanes 1 and 2) or 1.6 M LiCl (right panel; lanes 3–6) and visualized by autoradiography. For mobility standards, nonradiolabeled AMP, ADP, and ATP were also subjected to thin-layer chromatography and are indicated on the left side of each panel. For a marker of pppAp, [γ- 32 P] ATP-labeled v53 synthesized using T7 RNA polymerase was also subjected to RNase T2 digestion and then to thin-layer chromatography (lane 6). The expected nucleotide positions are indicated on the right side of each panel by closed arrowheads. DOI: http://dx.doi.org/10.7554/eLife.08939.004

    Journal: eLife

    Article Title: pp32 and APRIL are host cell-derived regulators of influenza virus RNA synthesis from cRNA

    doi: 10.7554/eLife.08939

    Figure Lengend Snippet: Products of influenza virus replication factor (IREF-2)-dependent unprimed RNA synthesis. ( A ) RNase T2 protection assay. Radioactively labeled vRNA products were synthesized in the cell-free viral RNA synthesis system with micrococcal nuclease-treated vRNP (mnRNP) and the v53 model template in the presence of ApG (lanes 1–3), the c53 model template in the presence of ApG (lanes 4–6), and c53 in the presence of the IREF-2 fraction and in the absence of ApG (lanes 7–9). Viral RNA products were hybridized with excess amounts of nonlabeled v53 (lanes 2, 5, and 8) or c53 (lanes 3, 6, and 9), which was followed by digestion with RNase T2. Hybridized and digested RNA samples were extracted, collected, and subjected to 10% Urea-PAGE followed by autoradiography visualization. The closed arrowhead indicates 53-nt-long RNAs. ( B ) Analysis of the 5'-terminal structure of IREF-2-dependent unprimed vRNA products. [α- 32 P] GTP-labeled IREF-2-dependent unprimed vRNA products were prepared in the cell-free viral RNA synthesis system. The radioactively labeled 53-nt-long vRNA products were isolated from 10% Urea-PAGE, which was followed by excision and elution from the gel. A portion of the isolated 53-nt-long products was treated with alkaline phosphatase (lanes 2 and 4). Both nontreated and alkaline phosphatase-treated [α- 32 P] GTP-labeled unprimed vRNA products were digested with RNase T2 (lanes 1–4) or snake venom phosphodiesterase (lane 5). The digested materials were spotted onto a polyethylenimine (PEI)-cellulose thin layer and developed with 1 N acetic acid-4 M LiCl (4:1, v/v) (left panel; lanes 1 and 2) or 1.6 M LiCl (right panel; lanes 3–6) and visualized by autoradiography. For mobility standards, nonradiolabeled AMP, ADP, and ATP were also subjected to thin-layer chromatography and are indicated on the left side of each panel. For a marker of pppAp, [γ- 32 P] ATP-labeled v53 synthesized using T7 RNA polymerase was also subjected to RNase T2 digestion and then to thin-layer chromatography (lane 6). The expected nucleotide positions are indicated on the right side of each panel by closed arrowheads. DOI: http://dx.doi.org/10.7554/eLife.08939.004

    Article Snippet: The dialyzed IREF-2 fraction was loaded onto a cation exchanger (Uno-S, Bio-Rad), and the IREF-2 activity was recovered in the fraction unbound to the column.

    Techniques: Labeling, Synthesized, Polyacrylamide Gel Electrophoresis, Autoradiography, Isolation, Thin Layer Chromatography, Marker

    Effect of influenza virus replication factor-2 (IREF-2) on viral reporter RNA syntheses from a reconstituted model replicon. HEK293T of control and IREF-2 knockdown (KD) cells (approximately, 3 × 10 5 cells in a 22-mm-diameter dish) were transfected with expression plasmids pCAGGS-PB1, -PB2, -PA, and -NP (15 ng each). In addition, 1.5 ng of either phPolI-vNS-Luc (for expression of vNS-Luc; left panel ) or phPolI-cNS-Luc (for expression of cNS-Luc; right panel ) was co-transfected as a viral genomic source. At 24 hr post co-transfection, viral reporter levels in both the control KD and the IREF-2 KD cells were quantitatively determined by RT-qPCR as described previously ( Kawaguchi et al., 2011 ) and in 'Materials and methods'. Quantification and standard deviations of the viral reporter RNA levels from IREF-2 KD cells expressed as a percentage of the value from the control KD cells. Each experiment was repeated three times. DOI: http://dx.doi.org/10.7554/eLife.08939.011

    Journal: eLife

    Article Title: pp32 and APRIL are host cell-derived regulators of influenza virus RNA synthesis from cRNA

    doi: 10.7554/eLife.08939

    Figure Lengend Snippet: Effect of influenza virus replication factor-2 (IREF-2) on viral reporter RNA syntheses from a reconstituted model replicon. HEK293T of control and IREF-2 knockdown (KD) cells (approximately, 3 × 10 5 cells in a 22-mm-diameter dish) were transfected with expression plasmids pCAGGS-PB1, -PB2, -PA, and -NP (15 ng each). In addition, 1.5 ng of either phPolI-vNS-Luc (for expression of vNS-Luc; left panel ) or phPolI-cNS-Luc (for expression of cNS-Luc; right panel ) was co-transfected as a viral genomic source. At 24 hr post co-transfection, viral reporter levels in both the control KD and the IREF-2 KD cells were quantitatively determined by RT-qPCR as described previously ( Kawaguchi et al., 2011 ) and in 'Materials and methods'. Quantification and standard deviations of the viral reporter RNA levels from IREF-2 KD cells expressed as a percentage of the value from the control KD cells. Each experiment was repeated three times. DOI: http://dx.doi.org/10.7554/eLife.08939.011

    Article Snippet: The dialyzed IREF-2 fraction was loaded onto a cation exchanger (Uno-S, Bio-Rad), and the IREF-2 activity was recovered in the fraction unbound to the column.

    Techniques: Transfection, Expressing, Cotransfection, Quantitative RT-PCR

    Protein profiles of native and recombinant influenza virus replication factor-2 (IREF-2s). Native or recombinant IREF-2 proteins (50 ng) were subjected to 11.5% SDS-PAGE followed by silver staining (lanes 1–4) and western blot analysis with anti-pp32 antibody (lanes 5–8) or anti-APRIL antibody (lanes 9–12). The Mono-Q fraction 6 (shown in Figure 1C ) was used as native pp32 (lanes 1, 5, and 9). Mono-Q fractions 9 and 10 (also shown in Figure 1C ) were further purified with Mono-Q and used as native APRIL (lanes 2, 6, and 10). Recombinant pp32 (lanes 3, 7, and 11) and APRIL (lanes 4, 8, and 12) were prepared using the Escherichia. coli expression system, as described in 'Materials and methods'. DOI: http://dx.doi.org/10.7554/eLife.08939.006

    Journal: eLife

    Article Title: pp32 and APRIL are host cell-derived regulators of influenza virus RNA synthesis from cRNA

    doi: 10.7554/eLife.08939

    Figure Lengend Snippet: Protein profiles of native and recombinant influenza virus replication factor-2 (IREF-2s). Native or recombinant IREF-2 proteins (50 ng) were subjected to 11.5% SDS-PAGE followed by silver staining (lanes 1–4) and western blot analysis with anti-pp32 antibody (lanes 5–8) or anti-APRIL antibody (lanes 9–12). The Mono-Q fraction 6 (shown in Figure 1C ) was used as native pp32 (lanes 1, 5, and 9). Mono-Q fractions 9 and 10 (also shown in Figure 1C ) were further purified with Mono-Q and used as native APRIL (lanes 2, 6, and 10). Recombinant pp32 (lanes 3, 7, and 11) and APRIL (lanes 4, 8, and 12) were prepared using the Escherichia. coli expression system, as described in 'Materials and methods'. DOI: http://dx.doi.org/10.7554/eLife.08939.006

    Article Snippet: The dialyzed IREF-2 fraction was loaded onto a cation exchanger (Uno-S, Bio-Rad), and the IREF-2 activity was recovered in the fraction unbound to the column.

    Techniques: Recombinant, SDS Page, Silver Staining, Western Blot, Purification, Expressing

    Purification of influenza virus replication factor-2 (IREF-2). ( A ) IREF-2 activity in uninfected nuclear extracts (NEs). Biochemical complementation assays using a cell-free vRNA replication system for fractions separated by phosphocellulose column chromatography were performed. The fractions, P0.05 (lane 3), P0.2 (lane 4), P0.5 (lane 5), and P1.0 (lane 6), were individually assayed in the cell-free viral RNA synthesis reaction employing 5 ng PB1-equivalent micrococcal nuclease-treated vRNP (mnRNP) as an enzyme source and 10 ng of the complementary RNA (cRNA) model template (c53), as described in the 'Materials and methods'. Dinucleotide ApG, serving as primer for viral RNA synthesis, was added to a final concentration of 0.2 mM (lane 1). To confirm the components required for the reactions, cell-free viral RNA synthesis with mnRNP and c53 in the presence of the P0.05 fraction was carried out (lane 7; identical to the conditions of lane 3). Simultaneously, reactions omitting the cRNA model template (lane 8), mnRNP (lane 9), or P0.05 fraction (lane 10; identical to the conditions of lane 2) were also carried out. After incubation at 30°C for 2 hr, each reaction product was collected and subjected to 10% Urea-PAGE followed by autoradiography. ( B ) Purification scheme of IREF-2 from uninfected HeLa cell NEnuclear extracts. For details regarding the column chromatography, see 'Materials and methods'. ( C ) Profile of the fractions from Mono-Q column chromatography at the final purification step. Each Mono-Q fraction (fraction numbers 1–11) or input material for the Mono-Q column chromatography (i.e., unbound fraction of the Uno-S column chromatography) was individually added to this cell-free viral RNA synthesis reaction in the absence of any added primers ( upper panel ). Each Mono-Q fraction was subjected to 11.5% SDS-PAGE, and polypeptides were visualized by silver staining ( lower panel ). The closed arrowhead indicates 53 mer RNA products. The open arrowhead (50 mer) indicates the product possibly generated by internal priming of ApG. The arrows indicate two candidate peptides responsible for IREF-2 activity. The molecular weight (kDa) positions are denoted on the left side of the panel. DOI: http://dx.doi.org/10.7554/eLife.08939.003

    Journal: eLife

    Article Title: pp32 and APRIL are host cell-derived regulators of influenza virus RNA synthesis from cRNA

    doi: 10.7554/eLife.08939

    Figure Lengend Snippet: Purification of influenza virus replication factor-2 (IREF-2). ( A ) IREF-2 activity in uninfected nuclear extracts (NEs). Biochemical complementation assays using a cell-free vRNA replication system for fractions separated by phosphocellulose column chromatography were performed. The fractions, P0.05 (lane 3), P0.2 (lane 4), P0.5 (lane 5), and P1.0 (lane 6), were individually assayed in the cell-free viral RNA synthesis reaction employing 5 ng PB1-equivalent micrococcal nuclease-treated vRNP (mnRNP) as an enzyme source and 10 ng of the complementary RNA (cRNA) model template (c53), as described in the 'Materials and methods'. Dinucleotide ApG, serving as primer for viral RNA synthesis, was added to a final concentration of 0.2 mM (lane 1). To confirm the components required for the reactions, cell-free viral RNA synthesis with mnRNP and c53 in the presence of the P0.05 fraction was carried out (lane 7; identical to the conditions of lane 3). Simultaneously, reactions omitting the cRNA model template (lane 8), mnRNP (lane 9), or P0.05 fraction (lane 10; identical to the conditions of lane 2) were also carried out. After incubation at 30°C for 2 hr, each reaction product was collected and subjected to 10% Urea-PAGE followed by autoradiography. ( B ) Purification scheme of IREF-2 from uninfected HeLa cell NEnuclear extracts. For details regarding the column chromatography, see 'Materials and methods'. ( C ) Profile of the fractions from Mono-Q column chromatography at the final purification step. Each Mono-Q fraction (fraction numbers 1–11) or input material for the Mono-Q column chromatography (i.e., unbound fraction of the Uno-S column chromatography) was individually added to this cell-free viral RNA synthesis reaction in the absence of any added primers ( upper panel ). Each Mono-Q fraction was subjected to 11.5% SDS-PAGE, and polypeptides were visualized by silver staining ( lower panel ). The closed arrowhead indicates 53 mer RNA products. The open arrowhead (50 mer) indicates the product possibly generated by internal priming of ApG. The arrows indicate two candidate peptides responsible for IREF-2 activity. The molecular weight (kDa) positions are denoted on the left side of the panel. DOI: http://dx.doi.org/10.7554/eLife.08939.003

    Article Snippet: The dialyzed IREF-2 fraction was loaded onto a cation exchanger (Uno-S, Bio-Rad), and the IREF-2 activity was recovered in the fraction unbound to the column.

    Techniques: Purification, Activity Assay, Column Chromatography, Concentration Assay, Incubation, Polyacrylamide Gel Electrophoresis, Autoradiography, SDS Page, Silver Staining, Generated, Molecular Weight

    Functional identification of MiPDAT in Saccharomyces cerevisiae H1246. ( A ) Lipid analysis of Saccharomyces cerevisiae by TLC. Lane 1: H1246 mutant; Lane 2: H1246 mutant transformed with pY-MiPDAT; Lane 3: triolein standard purchased from Nu Chek Prep, Inc. (UK); Lane 4: SCY62 (wild-type); Lane 5: H1246 transformed with empty pYES2. ( B ) Fluorescent staining of yeast cells with BODIPY. Lipid bodies where neutral lipids accumulated were visualized in the yeast cells with BODIPY fluorescence. The wild-type strain Scy62 was used as a positive control. The mutant H1246 and the mutant harbouring the empty vector (pYES2) were used as negative controls. The mutant expressing MiPDAT was analysed. All bars in the image B represent a length of 5 μm.

    Journal: Scientific Reports

    Article Title: Phospholipid: diacylglycerol acyltransferase contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress

    doi: 10.1038/srep26610

    Figure Lengend Snippet: Functional identification of MiPDAT in Saccharomyces cerevisiae H1246. ( A ) Lipid analysis of Saccharomyces cerevisiae by TLC. Lane 1: H1246 mutant; Lane 2: H1246 mutant transformed with pY-MiPDAT; Lane 3: triolein standard purchased from Nu Chek Prep, Inc. (UK); Lane 4: SCY62 (wild-type); Lane 5: H1246 transformed with empty pYES2. ( B ) Fluorescent staining of yeast cells with BODIPY. Lipid bodies where neutral lipids accumulated were visualized in the yeast cells with BODIPY fluorescence. The wild-type strain Scy62 was used as a positive control. The mutant H1246 and the mutant harbouring the empty vector (pYES2) were used as negative controls. The mutant expressing MiPDAT was analysed. All bars in the image B represent a length of 5 μm.

    Article Snippet: This recombinant vector and the empty plasmid pYES2, the negative control, were separately introduced into the mutant strain H1246 by electroporation (Bio-Rad, USA).

    Techniques: Functional Assay, Thin Layer Chromatography, Mutagenesis, Transformation Assay, Staining, Fluorescence, Positive Control, Plasmid Preparation, Expressing