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Toyobo ribonuclease inhibitor
Ribonuclease Inhibitor, supplied by Toyobo, used in various techniques. Bioz Stars score: 92/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ribonuclease inhibitor/product/Toyobo
Average 92 stars, based on 30 article reviews
Price from $9.99 to $1999.99
ribonuclease inhibitor - by Bioz Stars, 2020-08
92/100 stars

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Labeling:

Article Title: Glutamic acid decarboxylase 1 alternative splicing isoforms: characterization, expression and quantification in the mouse brain
Article Snippet: .. The reaction was carried out for 2 hours at 37°C in 20 μl of transcription buffer, containing 150 ng template DNA, 1 mM GTP, 1 mM ATP, 1 mM CTP, 0.65 mM UTP, 0.35 mM DIG-11-UTP (DIG RNA Labeling Mix, Roche Diagnostics, Mannheim, Germany), 20 units of ribonuclease inhibitor (Toyobo), and 40 units of T7 (Stratagene, La Jolla, CA) RNA polymerase. ..

Article Title: Postnatal alteration of collapsin response mediator protein 4 mRNA expression in the mouse brain
Article Snippet: .. To generate an antisense or sense probe labeled with digoxigenin, the template DNA was incubated for 2 h at 37 °C with T7 (for antisense probe) or T3 (for sense probe) RNA polymerase (Roche Diagnostics) in 20 μL transcription mixture containing 1 μg template DNA, 2 μL transcription buffer (10× ), 2 μL DIG RNA labeling mix (Roche Diagnostics), 0.5 μL ribonuclease inhibitor (Toyobo, Tokyo, Japan), and 2 μL appropriate RNA polymerase. .. Then, 2.5 μL LiCl (4 m ), 2 μL EDTA (0.2 m , pH 8.0), and 75 μL absolute EtOH were added to the solution and incubated overnight at −20 °C.

Polymerase Chain Reaction:

Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys
Article Snippet: .. Briefly, the transcription reaction was performed at 37 °C for 4 h, in a reaction mixture (5 ml) containing 80 mM Hepes–NaOH buffer (pH 8.1), 20 mM MgCl2 , 40 mM KCl, 20 mM dithiothreitol (DTT), 2 mM spermine, 14 μg/ml bovine serum albumin (BSA), 20 mM GMP, 5 mM each of ATP, GTP, CTP and UTP, 0.28 mg/ml T7 RNA polymerase, 5 unit pyrophosphatase (Sigma), 0.5 μl ribonuclease inhibitor (TOYOBO), and 10 μg/ml PCR-amplified DNA as a template. .. The products were purified by Resource Q column chromatography.

Incubation:

Article Title: A Putative Transcription Factor with Seven Zinc-Finger Motifs Identified in the Developing Suprachiasmatic Nucleus by the Differential Display PCR Method
Article Snippet: .. Heat-denatured total RNA (0.5 μg) was incubated with 300 U of Moloney murine leukemia virus reverse transcriptase (Toyobo) in a 20 μl reaction volume for 60 min at 35°C in the presence of 20 μ m dNTP and 40 U of ribonuclease inhibitor (Toyobo), using the oligo (dT) primer T12MA, T12MC, T12MG, or T12MT (M, a mixture of A, C, and G) as anchor primer. .. An aliquot (0.5 μl) of the samples was then added to 4.5 μl of PCR solution containing 2 μ m dNTPs, 5 μCi [α-33 P]dATP (3000 Ci/mmol, New England Nuclear), 0.5 U of AmpliTaq polymerase (Perkin-Elmer, Norwalk, CT), 1 μ m anchor primer (T12MN), and 0.5 μ m arbitrary primers.

Article Title: Postnatal alteration of collapsin response mediator protein 4 mRNA expression in the mouse brain
Article Snippet: .. To generate an antisense or sense probe labeled with digoxigenin, the template DNA was incubated for 2 h at 37 °C with T7 (for antisense probe) or T3 (for sense probe) RNA polymerase (Roche Diagnostics) in 20 μL transcription mixture containing 1 μg template DNA, 2 μL transcription buffer (10× ), 2 μL DIG RNA labeling mix (Roche Diagnostics), 0.5 μL ribonuclease inhibitor (Toyobo, Tokyo, Japan), and 2 μL appropriate RNA polymerase. .. Then, 2.5 μL LiCl (4 m ), 2 μL EDTA (0.2 m , pH 8.0), and 75 μL absolute EtOH were added to the solution and incubated overnight at −20 °C.

other:

Article Title: Gene Expressions for Signal Transduction under Acidic Conditions
Article Snippet: Other Reagents Taq DNA polymerase (Bio Academia) and Ribonuclease inhibitor (TOYOBO) were used.

Reverse Transcription Polymerase Chain Reaction:

Article Title: Late stage definitive endodermal differentiation can be defined by Daf1 expression
Article Snippet: .. RT-PCR analysis RNA was extracted from the cells using the RNeasy Micro-Kit (QIAGEN) and then 1 μg of RNA was reverse transcribed using ReverTra Ace (TOYOBO), ribonuclease inhibitor, recombinant (TOYOBO), and Oligo dT primers (TOYOBO). ..

Recombinant:

Article Title: Late stage definitive endodermal differentiation can be defined by Daf1 expression
Article Snippet: .. RT-PCR analysis RNA was extracted from the cells using the RNeasy Micro-Kit (QIAGEN) and then 1 μg of RNA was reverse transcribed using ReverTra Ace (TOYOBO), ribonuclease inhibitor, recombinant (TOYOBO), and Oligo dT primers (TOYOBO). ..

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  • 92
    Toyobo rnase inhibitor
    Products of influenza virus replication factor (IREF-2)-dependent unprimed RNA synthesis. ( A ) <t>RNase</t> 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] <t>GTP-labeled</t> 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
    Rnase Inhibitor, supplied by Toyobo, used in various techniques. Bioz Stars score: 92/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase inhibitor/product/Toyobo
    Average 92 stars, based on 21 article reviews
    Price from $9.99 to $1999.99
    rnase inhibitor - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    86
    Toyobo halo rnase h1 mutants
    Products of influenza virus replication factor (IREF-2)-dependent unprimed RNA synthesis. ( A ) <t>RNase</t> 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] <t>GTP-labeled</t> 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
    Halo Rnase H1 Mutants, supplied by Toyobo, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/halo rnase h1 mutants/product/Toyobo
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    halo rnase h1 mutants - by Bioz Stars, 2020-08
    86/100 stars
      Buy from Supplier

    Image Search Results


    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: Cell-free viral RNA synthesis was carried out at 30°C in a final volume of 20 μl or 25 μl in the presence of 50 mM HEPES-NaOH (pH 7.9), 3 mM MgCl2 , 50 mM KCl, 1 mM DTT, 500 μM each of ATP, UTP, and CTP and 25 μM GTP, 5 μCi of [α-32 P] GTP (3000 Ci/mmol), 8 U of RNase inhibitor from human placenta (Toyobo, Japan), 10 ng of a 53-nt-long model viral RNA template of negative or positive polarity (v53 and c53, respectively) and approximately 40 μg NP-equivalent, alternatively 5 ng PB1-equivalent of mnRNP as an enzyme source.

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

    Electrophoresis mobility shift assay for influenza virus replication factor-2 (IREF-2) and viral RNA. Radioactively labeled 53-nt-long model vRNA and complementary RNA(cRNA) probes (v53 and c53; 246.9 cpm/fmol) were synthesized by T7 RNA polymerase using [α- 32 P] GTP and isolated by gel excision. Each 500 pM (final concentration) of the labeled viral RNA probes, v53 (lanes 1–7) and c53 (lanes 8–14) was incubated with 10 nM or 50 nM of recombinant NP prepared using the Escherichia. coli expression system (lanes 2, 3, 9, and 10), recombinant pp32 (lanes 4, 5, 11, and 12), and recombinant APRIL (lanes 6, 7, 13, and 14) in 50 mM HEPES-NaOH (pH 7.9), 50 mM KCl, 0.5 U/μl of RNase inhibitor, and 15% (v/v) glycerol at 30°C for 30 min. After incubation, each binding mixture was loaded onto 0.6% agarose gel (buffered with TBE) and separated by electrophoresis (50 V for 3 hr). The gel was dried and visualized by autoradiography. DOI: http://dx.doi.org/10.7554/eLife.08939.008

    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: Electrophoresis mobility shift assay for influenza virus replication factor-2 (IREF-2) and viral RNA. Radioactively labeled 53-nt-long model vRNA and complementary RNA(cRNA) probes (v53 and c53; 246.9 cpm/fmol) were synthesized by T7 RNA polymerase using [α- 32 P] GTP and isolated by gel excision. Each 500 pM (final concentration) of the labeled viral RNA probes, v53 (lanes 1–7) and c53 (lanes 8–14) was incubated with 10 nM or 50 nM of recombinant NP prepared using the Escherichia. coli expression system (lanes 2, 3, 9, and 10), recombinant pp32 (lanes 4, 5, 11, and 12), and recombinant APRIL (lanes 6, 7, 13, and 14) in 50 mM HEPES-NaOH (pH 7.9), 50 mM KCl, 0.5 U/μl of RNase inhibitor, and 15% (v/v) glycerol at 30°C for 30 min. After incubation, each binding mixture was loaded onto 0.6% agarose gel (buffered with TBE) and separated by electrophoresis (50 V for 3 hr). The gel was dried and visualized by autoradiography. DOI: http://dx.doi.org/10.7554/eLife.08939.008

    Article Snippet: Cell-free viral RNA synthesis was carried out at 30°C in a final volume of 20 μl or 25 μl in the presence of 50 mM HEPES-NaOH (pH 7.9), 3 mM MgCl2 , 50 mM KCl, 1 mM DTT, 500 μM each of ATP, UTP, and CTP and 25 μM GTP, 5 μCi of [α-32 P] GTP (3000 Ci/mmol), 8 U of RNase inhibitor from human placenta (Toyobo, Japan), 10 ng of a 53-nt-long model viral RNA template of negative or positive polarity (v53 and c53, respectively) and approximately 40 μg NP-equivalent, alternatively 5 ng PB1-equivalent of mnRNP as an enzyme source.

    Techniques: Electrophoresis, Mobility Shift, Labeling, Synthesized, Isolation, Concentration Assay, Incubation, Recombinant, Expressing, Binding Assay, Agarose Gel Electrophoresis, Autoradiography

    Coimmunoprecipitation of progeny vRNP segments with active/GTP-bound Rab11A. ( A ) Coimmunoprecipitation of viral proteins with FLAG-Rab11A and its mutants. MDCK-Neo (lanes 1 and 5), MDCK-F11A-WT (lanes 2 and 6), -DN (lanes 3 and 7), and -CA (lanes 4 and 8) cells were infected with PR8 strain and harvested at 7 hpi. PNS were subjected to immunoprecipitation assays using anti-FLAG mAb, and 10% input (lanes 1–4) and precipitates (lanes 5–6) were analyzed by Western blotting with mouse anti-HA antiserum and anti-FLAG mAb, rabbit anti-PB2, PB1, PA, NP, and M1 antisera. ( B ) Coimmunoprecipitation of FLAG-Rab11 CA mutant with viral RNP complexes. Immunoprecipitation assay was carried out using anti-NP mAb61A5. Precipitates were treated with RNase A and eluates were subjected to Western blotting analysis. ( C ) Coimmunoprecipitation efficiencies of viral RNAs. The amounts of viral RNAs in the immunoprecipitates with anti-FLAG mAb were quantified by polarity-specific reverse transcription followed by segment-specific semiquantitative real-time PCR. Coimmunoprecipitation efficiencies were calculated as percentage of RNA amounts in precipitates relative to those in the input ( Figure S3 ). Segment numbers were indicated at the bottom. Columns indicated the coimmunoprecipitation efficiencies of vRNAs (gray and black columns) and c/mRNAs (hatched and white columns) from MDCK-F11A-DN and -CA. ( D ) Coimmunoprecipitation of vRNP components in the presence of RNase A. Immunoprecipitation assays using infected MDCK-F11A-CA cells were carried out in the absence (lane 1) or the presence of 1, 10, and 100 ng/µl RNase A (lanes 2–4, respectively). Coprecipitated vRNP components (PB2, PB1, PA, and NP) and direct precipitates (FLAG-Rab11A CA) were detected by Western blotting.

    Journal: PLoS ONE

    Article Title: Apical Transport of Influenza A Virus Ribonucleoprotein Requires Rab11-positive Recycling Endosome

    doi: 10.1371/journal.pone.0021123

    Figure Lengend Snippet: Coimmunoprecipitation of progeny vRNP segments with active/GTP-bound Rab11A. ( A ) Coimmunoprecipitation of viral proteins with FLAG-Rab11A and its mutants. MDCK-Neo (lanes 1 and 5), MDCK-F11A-WT (lanes 2 and 6), -DN (lanes 3 and 7), and -CA (lanes 4 and 8) cells were infected with PR8 strain and harvested at 7 hpi. PNS were subjected to immunoprecipitation assays using anti-FLAG mAb, and 10% input (lanes 1–4) and precipitates (lanes 5–6) were analyzed by Western blotting with mouse anti-HA antiserum and anti-FLAG mAb, rabbit anti-PB2, PB1, PA, NP, and M1 antisera. ( B ) Coimmunoprecipitation of FLAG-Rab11 CA mutant with viral RNP complexes. Immunoprecipitation assay was carried out using anti-NP mAb61A5. Precipitates were treated with RNase A and eluates were subjected to Western blotting analysis. ( C ) Coimmunoprecipitation efficiencies of viral RNAs. The amounts of viral RNAs in the immunoprecipitates with anti-FLAG mAb were quantified by polarity-specific reverse transcription followed by segment-specific semiquantitative real-time PCR. Coimmunoprecipitation efficiencies were calculated as percentage of RNA amounts in precipitates relative to those in the input ( Figure S3 ). Segment numbers were indicated at the bottom. Columns indicated the coimmunoprecipitation efficiencies of vRNAs (gray and black columns) and c/mRNAs (hatched and white columns) from MDCK-F11A-DN and -CA. ( D ) Coimmunoprecipitation of vRNP components in the presence of RNase A. Immunoprecipitation assays using infected MDCK-F11A-CA cells were carried out in the absence (lane 1) or the presence of 1, 10, and 100 ng/µl RNase A (lanes 2–4, respectively). Coprecipitated vRNP components (PB2, PB1, PA, and NP) and direct precipitates (FLAG-Rab11A CA) were detected by Western blotting.

    Article Snippet: For RNase sensitivity assay, PNS of infected MDCK-F11A-CA cells were similarly prepared except for RNase inhibitor.

    Techniques: Infection, Immunoprecipitation, Western Blot, Mutagenesis, Real-time Polymerase Chain Reaction