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Promega rnaase inhibitor rnasin
Rnaase Inhibitor Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 80 stars, based on 1 article reviews
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rnaase inhibitor rnasin - by Bioz Stars, 2020-03
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Related Articles

Real-time Polymerase Chain Reaction:

Article Title: Salicylic Acid-Independent ENHANCED DISEASE SUSCEPTIBILITY1 Signaling in Arabidopsis Immunity and Cell Death Is Regulated by the Monooxygenase FMO1 and the Nudix Hydrolase NUDT7 [W]
Article Snippet: RT reactions were performed with 1 μg of total RNA and 0.5 μg of oligo(dT)18 primer at 42°C using reverse transcriptase and RNAase inhibitor RNasin (both from Promega) in a 20-μL reaction volume. .. RT-PCR conditions were as follows: 95°C for 10 min and 50 cycles of 95°C for 30 s, 55°C for 30 s, and 72°C for 1 min and 30 s. Relative transcript levels were determined by quantitative real-time PCR using SYBR green dye on an ABI PRISM 7700 sequence detection system (Applied Biosystems).

Reverse Transcription Polymerase Chain Reaction:

Article Title: Salicylic Acid-Independent ENHANCED DISEASE SUSCEPTIBILITY1 Signaling in Arabidopsis Immunity and Cell Death Is Regulated by the Monooxygenase FMO1 and the Nudix Hydrolase NUDT7 [W]
Article Snippet: Paragraph title: RT-PCR Analysis ... RT reactions were performed with 1 μg of total RNA and 0.5 μg of oligo(dT)18 primer at 42°C using reverse transcriptase and RNAase inhibitor RNasin (both from Promega) in a 20-μL reaction volume.

Mutagenesis:

Article Title: Salicylic Acid-Independent ENHANCED DISEASE SUSCEPTIBILITY1 Signaling in Arabidopsis Immunity and Cell Death Is Regulated by the Monooxygenase FMO1 and the Nudix Hydrolase NUDT7 [W]
Article Snippet: RT reactions were performed with 1 μg of total RNA and 0.5 μg of oligo(dT)18 primer at 42°C using reverse transcriptase and RNAase inhibitor RNasin (both from Promega) in a 20-μL reaction volume. .. Primers for ACTIN , FMO1 , and NUDT7 were as described for the mutant characterization.

SYBR Green Assay:

Article Title: Salicylic Acid-Independent ENHANCED DISEASE SUSCEPTIBILITY1 Signaling in Arabidopsis Immunity and Cell Death Is Regulated by the Monooxygenase FMO1 and the Nudix Hydrolase NUDT7 [W]
Article Snippet: RT reactions were performed with 1 μg of total RNA and 0.5 μg of oligo(dT)18 primer at 42°C using reverse transcriptase and RNAase inhibitor RNasin (both from Promega) in a 20-μL reaction volume. .. RT-PCR conditions were as follows: 95°C for 10 min and 50 cycles of 95°C for 30 s, 55°C for 30 s, and 72°C for 1 min and 30 s. Relative transcript levels were determined by quantitative real-time PCR using SYBR green dye on an ABI PRISM 7700 sequence detection system (Applied Biosystems).

Microarray:

Article Title: Salicylic Acid-Independent ENHANCED DISEASE SUSCEPTIBILITY1 Signaling in Arabidopsis Immunity and Cell Death Is Regulated by the Monooxygenase FMO1 and the Nudix Hydrolase NUDT7 [W]
Article Snippet: Total RNA was extracted as described for the preparation of the microarray samples. .. RT reactions were performed with 1 μg of total RNA and 0.5 μg of oligo(dT)18 primer at 42°C using reverse transcriptase and RNAase inhibitor RNasin (both from Promega) in a 20-μL reaction volume.

Sequencing:

Article Title: Salicylic Acid-Independent ENHANCED DISEASE SUSCEPTIBILITY1 Signaling in Arabidopsis Immunity and Cell Death Is Regulated by the Monooxygenase FMO1 and the Nudix Hydrolase NUDT7 [W]
Article Snippet: RT reactions were performed with 1 μg of total RNA and 0.5 μg of oligo(dT)18 primer at 42°C using reverse transcriptase and RNAase inhibitor RNasin (both from Promega) in a 20-μL reaction volume. .. RT-PCR conditions were as follows: 95°C for 10 min and 50 cycles of 95°C for 30 s, 55°C for 30 s, and 72°C for 1 min and 30 s. Relative transcript levels were determined by quantitative real-time PCR using SYBR green dye on an ABI PRISM 7700 sequence detection system (Applied Biosystems).

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    Promega rnase h buffer
    <t>RNase</t> H activation by LNA/DNA and 2′- O -methyl gapmers. (Top) Results of RNase H assay. Full-length VR1 mRNA was incubated with a 5-fold excess of oligonucleotides in the presence of RNase H for 7.5 min at 37°C. Substrate (S) and cleavage products (P1 + P2) were separated on a 1.5% agarose gel and stained with ethidium bromide. Lane 1, control; lane 2, DNA 1; lane 3, LNA 9; lane 4, LNA 12; lane 5, LNA 13; lane 6, LNA 14; lane 7, LNA 15; lane 8, OMe 1; Lane 9, OMe 2; lane 10, OMe 3. (Bottom) Quantitative evaluation of the gel. All values are averages and standard deviations of at least three independent experiments and were normalized.
    Rnase H Buffer, supplied by Promega, used in various techniques. Bioz Stars score: 83/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase h buffer/product/Promega
    Average 83 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    rnase h buffer - by Bioz Stars, 2020-03
    83/100 stars
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    86
    Promega rnase h protection assay
    U1C depletion results in specific alternative splicing alterations in HeLa cells: Specificity and validation. ( A ) U1C knockdown (kd) in HeLa cells. Whole cell lysates were analyzed by SDS-PAGE and Western blot detecting U1C and γ-tubulin. U1 snRNA steady-state levels were analyzed by Northern blotting with probes specific for U1 snRNA and, as a loading control, U3 snoRNA. HeLa cells after U1C knockdown (ΔC) and luciferase-siRNA treated control cells (ctr) were compared. ( B ) Graphical overview of U1C-dependent alternative splicing targets identified by RNA-Seq analysis. ( C ) U1 snRNA blocking in HeLa cells. The efficiency of U1 snRNA blocking was determined by <t>RNase</t> H protection and silver staining. The positions of the full-length U1 snRNA (U1 uncut), the RNase H-cleaved U1 snRNA (U1 cut), and the U2 snRNA (as a control) are marked on the right. ( D ) Alternative splicing patterns of selected U1C target genes (names above the lanes) were analyzed by RT-PCR, using total RNA from HeLa cells after U1C-knockdown (ctr vs. ΔC) or U1 snRNA blocking (ctr vs. U1). Target-specific primers (arrows in the schematics on the right of the panels) were designed to amplify both alternative splicing isoforms. M , DNA size markers (in bp). Upper panel: Top and lower bands represent exon inclusion and skipping products, respectively; an unspecific product for SNHG5 is marked by open circles between the lanes. Lower panel: For MARCH7 top and lower bands reflect usage of the proximal and distal 5′ splice site, respectively. For UFM1 three alternative 5′ splice sites are activated upon U1C knockdown labeled with 1, 2, and 3 on the right.
    Rnase H Protection Assay, supplied by Promega, 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/rnase h protection assay/product/Promega
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase h protection assay - by Bioz Stars, 2020-03
    86/100 stars
      Buy from Supplier

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    RNase H activation by LNA/DNA and 2′- O -methyl gapmers. (Top) Results of RNase H assay. Full-length VR1 mRNA was incubated with a 5-fold excess of oligonucleotides in the presence of RNase H for 7.5 min at 37°C. Substrate (S) and cleavage products (P1 + P2) were separated on a 1.5% agarose gel and stained with ethidium bromide. Lane 1, control; lane 2, DNA 1; lane 3, LNA 9; lane 4, LNA 12; lane 5, LNA 13; lane 6, LNA 14; lane 7, LNA 15; lane 8, OMe 1; Lane 9, OMe 2; lane 10, OMe 3. (Bottom) Quantitative evaluation of the gel. All values are averages and standard deviations of at least three independent experiments and were normalized.

    Journal: Nucleic Acids Research

    Article Title: Design of antisense oligonucleotides stabilized by locked nucleic acids

    doi:

    Figure Lengend Snippet: RNase H activation by LNA/DNA and 2′- O -methyl gapmers. (Top) Results of RNase H assay. Full-length VR1 mRNA was incubated with a 5-fold excess of oligonucleotides in the presence of RNase H for 7.5 min at 37°C. Substrate (S) and cleavage products (P1 + P2) were separated on a 1.5% agarose gel and stained with ethidium bromide. Lane 1, control; lane 2, DNA 1; lane 3, LNA 9; lane 4, LNA 12; lane 5, LNA 13; lane 6, LNA 14; lane 7, LNA 15; lane 8, OMe 1; Lane 9, OMe 2; lane 10, OMe 3. (Bottom) Quantitative evaluation of the gel. All values are averages and standard deviations of at least three independent experiments and were normalized.

    Article Snippet: The standard RNase H assay was performed as described previously ( ): 100 nM VR1 mRNA were incubated with a 5-fold excess of an antisense oligonucleotide in a total volume of 10 µl in RNase H buffer (40 mM Tris–HCl pH 7.2, 4 mM MgCl2 , 1 mM DTT, 150 mM NaCl and 1.25 U/µl RNasin; Promega, Madison, WI) for 7.5 min at 37°C in the presence of 0.4 U E.coli RNase H (Promega).

    Techniques: Activation Assay, Rnase H Assay, Incubation, Agarose Gel Electrophoresis, Staining

    RNase H assays with a short RNA target. Lane 1, one base ladder produced by alkaline hydrolysis; lane 2, cleavage products after incubation with RNase T1; lane 3, 18mer RNA; lanes 4 and 5, products after incubation of target RNA with all DNA antisense oligonucleotide (DNA 1) in the presence of RNase H after 10 and 30 min, respectively; lanes 6 and 7, products after incubation of target RNA with end-block LNA/DNA/LNA oligonucleotide (LNA 17) in the presence of RNase H after 10 and 30 min; lanes 8 and 9, products after incubation of target RNA with LNA/DNA mixmer (LNA 9) in the presence of RNase H after 10 and 30 min; lanes 10 and 11, products after incubation of target RNA with phosphorothioate in the presence of RNase H after 10 and 30 min. For further details see text.

    Journal: Nucleic Acids Research

    Article Title: Design of antisense oligonucleotides stabilized by locked nucleic acids

    doi:

    Figure Lengend Snippet: RNase H assays with a short RNA target. Lane 1, one base ladder produced by alkaline hydrolysis; lane 2, cleavage products after incubation with RNase T1; lane 3, 18mer RNA; lanes 4 and 5, products after incubation of target RNA with all DNA antisense oligonucleotide (DNA 1) in the presence of RNase H after 10 and 30 min, respectively; lanes 6 and 7, products after incubation of target RNA with end-block LNA/DNA/LNA oligonucleotide (LNA 17) in the presence of RNase H after 10 and 30 min; lanes 8 and 9, products after incubation of target RNA with LNA/DNA mixmer (LNA 9) in the presence of RNase H after 10 and 30 min; lanes 10 and 11, products after incubation of target RNA with phosphorothioate in the presence of RNase H after 10 and 30 min. For further details see text.

    Article Snippet: The standard RNase H assay was performed as described previously ( ): 100 nM VR1 mRNA were incubated with a 5-fold excess of an antisense oligonucleotide in a total volume of 10 µl in RNase H buffer (40 mM Tris–HCl pH 7.2, 4 mM MgCl2 , 1 mM DTT, 150 mM NaCl and 1.25 U/µl RNasin; Promega, Madison, WI) for 7.5 min at 37°C in the presence of 0.4 U E.coli RNase H (Promega).

    Techniques: Produced, Incubation, Blocking Assay

    RNase H mapping of newly synthesized RNA

    Journal: Methods (San Diego, Calif.)

    Article Title: Flavivirus RNA Synthesis in vitro

    doi: 10.1016/j.ymeth.2015.08.002

    Figure Lengend Snippet: RNase H mapping of newly synthesized RNA

    Article Snippet: RNA samples are then precipitated with ethanol and resuspended with 20 μl of RNase H buffer (50 mM Tris-HCl, pH 8.0, 100 mM NaCl, 10 mM MgCl2 , 1 mM dithiothreitol, 10 units of RNasin (Promega), 4 units of RNase H (Thermostable; Epicenter Technologies), 200 μM oligodeoxynucleotide of either (+)- or (−)-strand polarity.

    Techniques: Synthesized

    Affinity purification of 7SL RNA. ( A ) Sequence of the four antisense oligonucleotides used to probe 7SL RNA in RBCs. ( B ) 7SL RNA from an RBC lysate was cleaved by RNase H only when it was hybridized to oligo 2 (red). 7SL RNA from mouse 3T3 cells was not cleaved. Experiment was done twice. ( C ) Affinity purification of 7SL. Total RNA in the supernatant (Sup.) and the pull-down (P.D.) after hybridization with a 7SL RNA antisense probe (7SL oligo) or a control probe ( X.t. oligo). RNA was detected by SYBR gold. Analysis of the pulled-down RNA showed readily detectable 7SL RNA by Northern blotting. Experiment was done twice. ( D , left lane) Total proteins (minus hemoglobins) before pull-down. ( Right lanes) Proteins in the pull-down fractions shown in C . Proteins detected by silver staining. In the 7SL pull-down fraction, the major bands are assumed to be spectrin (α and β chains), protein 4.1 and band3, based on their molecular weights and on the abundance of these proteins in the mass spectroscopic analysis. Experiment was done twice. ( E ) Proteins and RNA pulled down by antibodies against spectrin α and protein 4.1. ( Top panels) Pulled-down proteins were analyzed by Western blots against spectrin α, protein 4.1 and SART3. SART3 was detected in both pull-downs. Only spectrin alpha was sufficiently abundant to be detected in the input lane. Western blots were performed once. ( Bottom panels) Pulled-down RNAs were analyzed by RT-PCR using oligos targeting 7SL RNA and two hemoglobin mRNAs, Hba and Hbb. 7SL RNA was detected in both pull-downs. Northern blots were done twice.

    Journal: RNA

    Article Title: 7SL RNA in vertebrate red blood cells

    doi: 10.1261/rna.065474.117

    Figure Lengend Snippet: Affinity purification of 7SL RNA. ( A ) Sequence of the four antisense oligonucleotides used to probe 7SL RNA in RBCs. ( B ) 7SL RNA from an RBC lysate was cleaved by RNase H only when it was hybridized to oligo 2 (red). 7SL RNA from mouse 3T3 cells was not cleaved. Experiment was done twice. ( C ) Affinity purification of 7SL. Total RNA in the supernatant (Sup.) and the pull-down (P.D.) after hybridization with a 7SL RNA antisense probe (7SL oligo) or a control probe ( X.t. oligo). RNA was detected by SYBR gold. Analysis of the pulled-down RNA showed readily detectable 7SL RNA by Northern blotting. Experiment was done twice. ( D , left lane) Total proteins (minus hemoglobins) before pull-down. ( Right lanes) Proteins in the pull-down fractions shown in C . Proteins detected by silver staining. In the 7SL pull-down fraction, the major bands are assumed to be spectrin (α and β chains), protein 4.1 and band3, based on their molecular weights and on the abundance of these proteins in the mass spectroscopic analysis. Experiment was done twice. ( E ) Proteins and RNA pulled down by antibodies against spectrin α and protein 4.1. ( Top panels) Pulled-down proteins were analyzed by Western blots against spectrin α, protein 4.1 and SART3. SART3 was detected in both pull-downs. Only spectrin alpha was sufficiently abundant to be detected in the input lane. Western blots were performed once. ( Bottom panels) Pulled-down RNAs were analyzed by RT-PCR using oligos targeting 7SL RNA and two hemoglobin mRNAs, Hba and Hbb. 7SL RNA was detected in both pull-downs. Northern blots were done twice.

    Article Snippet: Cells were homogenized in 500 µL RNase H buffer: 50 mM HEPES pH 7.5, 150 mM NaCl, 5 mM MgCl2 , 1 mM DTT, 0.2 U RNasin (Promega), one protease inhibitor cocktail tablet (cOmplete Tablets–Mini EASYpack, Roche) and 1% Tween-20.

    Techniques: Affinity Purification, Sequencing, Hybridization, Northern Blot, Silver Staining, Western Blot, Reverse Transcription Polymerase Chain Reaction

    U1C depletion results in specific alternative splicing alterations in HeLa cells: Specificity and validation. ( A ) U1C knockdown (kd) in HeLa cells. Whole cell lysates were analyzed by SDS-PAGE and Western blot detecting U1C and γ-tubulin. U1 snRNA steady-state levels were analyzed by Northern blotting with probes specific for U1 snRNA and, as a loading control, U3 snoRNA. HeLa cells after U1C knockdown (ΔC) and luciferase-siRNA treated control cells (ctr) were compared. ( B ) Graphical overview of U1C-dependent alternative splicing targets identified by RNA-Seq analysis. ( C ) U1 snRNA blocking in HeLa cells. The efficiency of U1 snRNA blocking was determined by RNase H protection and silver staining. The positions of the full-length U1 snRNA (U1 uncut), the RNase H-cleaved U1 snRNA (U1 cut), and the U2 snRNA (as a control) are marked on the right. ( D ) Alternative splicing patterns of selected U1C target genes (names above the lanes) were analyzed by RT-PCR, using total RNA from HeLa cells after U1C-knockdown (ctr vs. ΔC) or U1 snRNA blocking (ctr vs. U1). Target-specific primers (arrows in the schematics on the right of the panels) were designed to amplify both alternative splicing isoforms. M , DNA size markers (in bp). Upper panel: Top and lower bands represent exon inclusion and skipping products, respectively; an unspecific product for SNHG5 is marked by open circles between the lanes. Lower panel: For MARCH7 top and lower bands reflect usage of the proximal and distal 5′ splice site, respectively. For UFM1 three alternative 5′ splice sites are activated upon U1C knockdown labeled with 1, 2, and 3 on the right.

    Journal: PLoS Genetics

    Article Title: A Novel Intra-U1 snRNP Cross-Regulation Mechanism: Alternative Splicing Switch Links U1C and U1-70K Expression

    doi: 10.1371/journal.pgen.1003856

    Figure Lengend Snippet: U1C depletion results in specific alternative splicing alterations in HeLa cells: Specificity and validation. ( A ) U1C knockdown (kd) in HeLa cells. Whole cell lysates were analyzed by SDS-PAGE and Western blot detecting U1C and γ-tubulin. U1 snRNA steady-state levels were analyzed by Northern blotting with probes specific for U1 snRNA and, as a loading control, U3 snoRNA. HeLa cells after U1C knockdown (ΔC) and luciferase-siRNA treated control cells (ctr) were compared. ( B ) Graphical overview of U1C-dependent alternative splicing targets identified by RNA-Seq analysis. ( C ) U1 snRNA blocking in HeLa cells. The efficiency of U1 snRNA blocking was determined by RNase H protection and silver staining. The positions of the full-length U1 snRNA (U1 uncut), the RNase H-cleaved U1 snRNA (U1 cut), and the U2 snRNA (as a control) are marked on the right. ( D ) Alternative splicing patterns of selected U1C target genes (names above the lanes) were analyzed by RT-PCR, using total RNA from HeLa cells after U1C-knockdown (ctr vs. ΔC) or U1 snRNA blocking (ctr vs. U1). Target-specific primers (arrows in the schematics on the right of the panels) were designed to amplify both alternative splicing isoforms. M , DNA size markers (in bp). Upper panel: Top and lower bands represent exon inclusion and skipping products, respectively; an unspecific product for SNHG5 is marked by open circles between the lanes. Lower panel: For MARCH7 top and lower bands reflect usage of the proximal and distal 5′ splice site, respectively. For UFM1 three alternative 5′ splice sites are activated upon U1C knockdown labeled with 1, 2, and 3 on the right.

    Article Snippet: The efficiency of U1 snRNA inhibition was analyzed by an RNase H protection assay: Whole cell extracts were incubated with 5 µM antisense DNA oligonucleotide ( 5′-CAGGTAAGTAT-3′ ) and 1.5 U RNase H (Promega) for 30 min at 37°C.

    Techniques: SDS Page, Western Blot, Northern Blot, Luciferase, RNA Sequencing Assay, Blocking Assay, Silver Staining, Reverse Transcription Polymerase Chain Reaction, Labeling