m 7 gpppa  (New England Biolabs)


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    New England Biolabs m 7 gpppa
    M 7 Gpppa, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    m 7 gpppa  (New England Biolabs)


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    New England Biolabs m 7 gpppa
    M 7 Gpppa, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    m 7 gpppa rna cap structure analog  (New England Biolabs)


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    New England Biolabs m 7 gpppa rna cap structure analog
    M 7 Gpppa Rna Cap Structure Analog, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    m7 g 5 ppp 5  (New England Biolabs)


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    g 5 ppp 5  (New England Biolabs)


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    New England Biolabs g 5 ppp 5
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    ppp  (New England Biolabs)


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    New England Biolabs ppp
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    a 5ʹ ppp 5ʹ g rna cap structure analog  (New England Biolabs)


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    New England Biolabs a 5ʹ ppp 5ʹ g rna cap structure analog
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    g 5 ppp 5  (New England Biolabs)


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    New England Biolabs g 5 ppp 5
    G 5 Ppp 5, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    m7 g 5 ppp 5  (New England Biolabs)


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    New England Biolabs m7 g 5 ppp 5
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    m 7 gpppa rna cap structure analog  (New England Biolabs)


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    New England Biolabs m 7 gpppa rna cap structure analog
    Identification of FAD cap binding proteins in budding yeast. ( A ) Schematic illustration of the FAD cap <t>-RNA</t> Affinity Purification (FcRAP). ( B ) Eluates from FcRAP were loaded on to a 4%-12% Bis-Tris gel and stained with SYPRO Ruby. The <t>m</t> <t>7</t> G cap affinity purification was used as a control. All protein bands labeled on the gel were excised from the gel and identified using mass spectrometry. ( C ) Electrophoretic mobility shift assay (EMSA) using increasing concentration of Xrn1 (2.5, 5 and 7.5 pmol) and a fixed concentration (5 pmol) of uniformly labeled in vitro transcribed FAD-capped or NAD-capped or triphosphate RNA (pppA–). ( D ) EMSA using equimolar concentration (5 pmol) of Xrn1 and uniformly labeled in vitro transcribed FAD-capped or NAD-capped or pppA–RNAs in the absence and presence of 7 pmol and 14 pmol total yeast RNA as a nonspecific competitor.
    M 7 Gpppa Rna Cap Structure Analog, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Identification of a novel deFADding activity in human, yeast and bacterial 5′ to 3′ exoribonucleases"

    Article Title: Identification of a novel deFADding activity in human, yeast and bacterial 5′ to 3′ exoribonucleases

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkac617

    Identification of FAD cap binding proteins in budding yeast. ( A ) Schematic illustration of the FAD cap -RNA Affinity Purification (FcRAP). ( B ) Eluates from FcRAP were loaded on to a 4%-12% Bis-Tris gel and stained with SYPRO Ruby. The m 7 G cap affinity purification was used as a control. All protein bands labeled on the gel were excised from the gel and identified using mass spectrometry. ( C ) Electrophoretic mobility shift assay (EMSA) using increasing concentration of Xrn1 (2.5, 5 and 7.5 pmol) and a fixed concentration (5 pmol) of uniformly labeled in vitro transcribed FAD-capped or NAD-capped or triphosphate RNA (pppA–). ( D ) EMSA using equimolar concentration (5 pmol) of Xrn1 and uniformly labeled in vitro transcribed FAD-capped or NAD-capped or pppA–RNAs in the absence and presence of 7 pmol and 14 pmol total yeast RNA as a nonspecific competitor.
    Figure Legend Snippet: Identification of FAD cap binding proteins in budding yeast. ( A ) Schematic illustration of the FAD cap -RNA Affinity Purification (FcRAP). ( B ) Eluates from FcRAP were loaded on to a 4%-12% Bis-Tris gel and stained with SYPRO Ruby. The m 7 G cap affinity purification was used as a control. All protein bands labeled on the gel were excised from the gel and identified using mass spectrometry. ( C ) Electrophoretic mobility shift assay (EMSA) using increasing concentration of Xrn1 (2.5, 5 and 7.5 pmol) and a fixed concentration (5 pmol) of uniformly labeled in vitro transcribed FAD-capped or NAD-capped or triphosphate RNA (pppA–). ( D ) EMSA using equimolar concentration (5 pmol) of Xrn1 and uniformly labeled in vitro transcribed FAD-capped or NAD-capped or pppA–RNAs in the absence and presence of 7 pmol and 14 pmol total yeast RNA as a nonspecific competitor.

    Techniques Used: Binding Assay, Affinity Purification, Staining, Labeling, Mass Spectrometry, Electrophoretic Mobility Shift Assay, Concentration Assay, In Vitro

    RNase AM is a novel deFADding enzyme in E. coli . ( A ) Reaction products of in vitro deFADding assays with 100 nM recombinant RNase AM. Uniformly 32 P-labeled monophosphate (pA–) or FAD-capped RNA (FAD–), NAD-capped (NAD–) and m 7 G-capped (m 7 G–). Reaction products were resolved on 15% 7 M urea PAGE gels. ( B ) Time-course decay analysis of ∼300 nM uniformly 32 P-labeled monophosphate or FAD-capped RNA with the indicated amount of RNase AM protein are shown. Quantitation of RNA remaining is plotted from three independent experiments with ± SD denoted by error bars along with the one phase decay curve. ( C ) To demonstrate that RNase AM releases intact FAD upon deFADding like Xrn1 (in Figure ), FAD-capQ assay using different amount of in vitro transcribed FAD-capped RNA was used. Catalytic-dead mutant of RNase AM, D20A was used as control for the reaction. ( D ) Total RNA from WT and rnase AMΔ were subjected to the FAD-capQ assay to detect total levels of cellular FAD-capped RNA. Data represents an average from three independent biological experiments. Error bars represent ± SD with unpaired t -test; * P < 0.05, ** P < 0.001, *** P < 0.0001.
    Figure Legend Snippet: RNase AM is a novel deFADding enzyme in E. coli . ( A ) Reaction products of in vitro deFADding assays with 100 nM recombinant RNase AM. Uniformly 32 P-labeled monophosphate (pA–) or FAD-capped RNA (FAD–), NAD-capped (NAD–) and m 7 G-capped (m 7 G–). Reaction products were resolved on 15% 7 M urea PAGE gels. ( B ) Time-course decay analysis of ∼300 nM uniformly 32 P-labeled monophosphate or FAD-capped RNA with the indicated amount of RNase AM protein are shown. Quantitation of RNA remaining is plotted from three independent experiments with ± SD denoted by error bars along with the one phase decay curve. ( C ) To demonstrate that RNase AM releases intact FAD upon deFADding like Xrn1 (in Figure ), FAD-capQ assay using different amount of in vitro transcribed FAD-capped RNA was used. Catalytic-dead mutant of RNase AM, D20A was used as control for the reaction. ( D ) Total RNA from WT and rnase AMΔ were subjected to the FAD-capQ assay to detect total levels of cellular FAD-capped RNA. Data represents an average from three independent biological experiments. Error bars represent ± SD with unpaired t -test; * P < 0.05, ** P < 0.001, *** P < 0.0001.

    Techniques Used: In Vitro, Recombinant, Labeling, Quantitation Assay, Mutagenesis

    rna cap structure analog  (New England Biolabs)


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