rnase a Millipore Search Results


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  • 99
    Millipore rnase a
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 21605 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ribonuclease a
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Ribonuclease A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4821 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Merck KGaA rnase a
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Rnase A, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 97/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Millipore ribonuclease a detection kit
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Ribonuclease A Detection Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Millipore deoxyribonuclease free ribonuclease a
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Deoxyribonuclease Free Ribonuclease A, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore ribonuclease a solution
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Ribonuclease A Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore type iia ribonuclease a
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Type Iia Ribonuclease A, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore ribonuclease a rnase
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Ribonuclease A Rnase, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ribonuclease a pbs
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Ribonuclease A Pbs, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore native rnase a
    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to <t>RNase</t> A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.
    Native Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Millipore pm rnase a
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Pm Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rnase a treatement
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Rnase A Treatement, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore rnase a buffer
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Rnase A Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Millipore partial rnase a
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Partial Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Millipore rnase a pi
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Rnase A Pi, supplied by Millipore, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore rnase a t1
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Rnase A T1, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Millipore pancreatic rnase a
    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and <t>RNAse</t> A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.
    Pancreatic Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 87/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore bovine pancreas ribonuclease a
    Effect of osmolytes on K m of <t>RNase-A.</t> Plot of Δ K m versus [osmolyte]. Δ K m of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.
    Bovine Pancreas Ribonuclease A, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore dnase free ribonuclease a
    Effect of osmolytes on K m of <t>RNase-A.</t> Plot of Δ K m versus [osmolyte]. Δ K m of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.
    Dnase Free Ribonuclease A, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 137 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore i a rnase a
    Effect of osmolytes on K m of <t>RNase-A.</t> Plot of Δ K m versus [osmolyte]. Δ K m of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.
    I A Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore bovine pancreatic ribonuclease a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Bovine Pancreatic Ribonuclease A, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Millipore dnase rnase a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Dnase Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore protease free rnase a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Protease Free Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ribonuclease a from bovine pancreas
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Ribonuclease A From Bovine Pancreas, supplied by Millipore, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rnase a native enzyme
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Rnase A Native Enzyme, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rnase a type xii a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Rnase A Type Xii A, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bovine pancreatic rnase a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Bovine Pancreatic Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore native bovine rnase a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
    Native Bovine Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore recombinant proteins rnase a
    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine <t>RNase</t> A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).
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    DDX17 interacts with essential splicing factors. (a) Schematic representation of HIV-1 genome organization and mapping of the splice sites described in this manuscript. Other known sites have been omitted for simplicity. (b) Exogenously expressed Myc-DDX17 co-immunoprecipitates with endogenous U2AF65, SRSF1/SF2 and U1-C. IgG lane, immunoprecipitation of proteins treated with isotype control matched antibody. In RNase-treated lane, samples were subjected to digestion with RNase A. (c) HeLa M cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of siDDX17 rescue expressor construct. Expression of U2AF65, SRSF1/SF2 and U1-C, following knockdown and rescue of DDX17 was detected by Western blotting, using their respective antibodies. GAPDH was detected to monitor sample loading. (d) Effect of overexpression of DDX5 as attempted rescue of HIV-1 virus production following endogenous DDX17 depletion. Cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of DDX5 expressor construct. (e) Western blot for DDX17 and DDX5 expression. The graph is a representative of three independent experiments done in triplicate. Bars represent mean of triplicate samples ± SEM. Statistical significance: ** P
    Reaction Mix Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rnase a treated thin cuts
    DDX17 interacts with essential splicing factors. (a) Schematic representation of HIV-1 genome organization and mapping of the splice sites described in this manuscript. Other known sites have been omitted for simplicity. (b) Exogenously expressed Myc-DDX17 co-immunoprecipitates with endogenous U2AF65, SRSF1/SF2 and U1-C. IgG lane, immunoprecipitation of proteins treated with isotype control matched antibody. In RNase-treated lane, samples were subjected to digestion with RNase A. (c) HeLa M cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of siDDX17 rescue expressor construct. Expression of U2AF65, SRSF1/SF2 and U1-C, following knockdown and rescue of DDX17 was detected by Western blotting, using their respective antibodies. GAPDH was detected to monitor sample loading. (d) Effect of overexpression of DDX5 as attempted rescue of HIV-1 virus production following endogenous DDX17 depletion. Cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of DDX5 expressor construct. (e) Western blot for DDX17 and DDX5 expression. The graph is a representative of three independent experiments done in triplicate. Bars represent mean of triplicate samples ± SEM. Statistical significance: ** P
    Rnase A Treated Thin Cuts, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to RNase A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.

    Journal: PLoS ONE

    Article Title: Free Extracellular miRNA Functionally Targets Cells by Transfecting Exosomes from Their Companion Cells

    doi: 10.1371/journal.pone.0122991

    Figure Lengend Snippet: Enzymatic treatment of nucleic acids and associated proteins from PCE and QRNA of TNP Ts Sup eliminates suppressive activity. a . TNP Ts Sup-derived PCE suppression is sensitive to RNase A (Sigma 4375), but not DNase treatment (Group D vs C). b . Purer RNase A (Sigma 5250, Group E) and RNase III (Group H), as well as proteinase K with and without SDS (Groups F and G) treatment of QRNA from Sup of TNP Ts, eliminates its suppressive activity.

    Article Snippet: Reagents Picryl chloride (PCl/ trinitrophenyl (TNP)-Cl), oxazolone (OX), EDTA sodium salt, 2-mercaptoethanol (2ME), 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), trinitrobenzene sulfonic acid (TNBSA), cacodylic acid, sodium acetate, trypan blue, phenol-chloroform pH 4.7, phenol equilibrated with Tris-HCl buffer pH = 8.0, RNase A (4375 and purer 5250), DNase (D7231, Lot K1815), Proteinase K (P2308, Lot 65u8603), human recombinant IL-2, all were from [Sigma, St. Louis, MO].

    Techniques: Activity Assay, Derivative Assay

    Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and RNAse A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.

    Journal: RNA

    Article Title: Stereospecificity of short Rev-derived peptide interactions with RRE IIB RNA

    doi: 10.1261/rna.2172103

    Figure Lengend Snippet: Summary of RRE IIB footprinting studies. (Open circles) Nucleotides that were found to be protected in two different footprinting methods. Protection observed in lead acetate and RNAse A footprinting experiments. (Filled circles) Nucleotides appeared protected in all three footprinting methods. Protection observed in RNAse T1 footprinting experiments. (Arrows) Enhancement of cleavage observed in lead acetate and RNAse A footprinting experiments.

    Article Snippet: In a typical experiment, 10 μL of 10 mM HEPES buffer (pH 7.0) containing 50 mM KCl and 50–100 ng of 5′-32 P-labeled RRE IIB (~0.3–0.6 μM) was incubated with 200 pM RNase A (Sigma) at room temperature for 10 min in the presence of Rev peptides and neomycin B at various concentrations.

    Techniques: Footprinting

    RRE IIB footprinting studies of the Rev peptides binding sites on the RNA construct. ( A ) Lead acetate footprinting. ( B ) RNase T1 footprinting. ( C ) RNase A footprinting. (0) Untreated RRE IIB, 32 P-labeled at 5′; (Ctrl) control experiment in the absence of binders; (L-Rev, D-Rev, L-RevErse, D-RevErse) RNA footprinting in the presence of peptide binders; (NeoB) RNA footprinting in the presence of neomycin B. Concentrations of the peptides, 2.5 and 12.5 μM. Concentration of neomycin B 25 and 125 μM.

    Journal: RNA

    Article Title: Stereospecificity of short Rev-derived peptide interactions with RRE IIB RNA

    doi: 10.1261/rna.2172103

    Figure Lengend Snippet: RRE IIB footprinting studies of the Rev peptides binding sites on the RNA construct. ( A ) Lead acetate footprinting. ( B ) RNase T1 footprinting. ( C ) RNase A footprinting. (0) Untreated RRE IIB, 32 P-labeled at 5′; (Ctrl) control experiment in the absence of binders; (L-Rev, D-Rev, L-RevErse, D-RevErse) RNA footprinting in the presence of peptide binders; (NeoB) RNA footprinting in the presence of neomycin B. Concentrations of the peptides, 2.5 and 12.5 μM. Concentration of neomycin B 25 and 125 μM.

    Article Snippet: In a typical experiment, 10 μL of 10 mM HEPES buffer (pH 7.0) containing 50 mM KCl and 50–100 ng of 5′-32 P-labeled RRE IIB (~0.3–0.6 μM) was incubated with 200 pM RNase A (Sigma) at room temperature for 10 min in the presence of Rev peptides and neomycin B at various concentrations.

    Techniques: Footprinting, Binding Assay, Construct, Labeling, Concentration Assay

    Effect of osmolytes on K m of RNase-A. Plot of Δ K m versus [osmolyte]. Δ K m of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.

    Journal: PLoS ONE

    Article Title: Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes

    doi: 10.1371/journal.pone.0109408

    Figure Lengend Snippet: Effect of osmolytes on K m of RNase-A. Plot of Δ K m versus [osmolyte]. Δ K m of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.

    Article Snippet: Materials and Methods Commercially lyophilized preparation of Ribonuclease-A (type III-A) from bovine pancreas (RNase-A) was purchased from Sigma Chemical Co. Trimethylamine N-oxide (TMAO), betaine, sarcosine, proline, glycine, β-alanine and cytidine 2′–3′ cyclic monophosphate (C > p) were also purchased from Sigma Chemical Co. Guanidinium chloride (GdmCl) and urea were obtained from MP Biomedicals.

    Techniques:

    Secondary structural characteristic of the folded RNase-A at pH 7.0 and 25°C. Representative CD spectra of folded RNase-A (from heat-, GdmCl-, urea-induced denatured states) obtained from refolding in the presence of 1 M osmolytes. The CD spectra of the refolded RNase-A in the absence of osmolytes is identical with the native CD spectra and is omitted. Therefore, we have shown spectra only for the native (without refolding) control in this figure.

    Journal: PLoS ONE

    Article Title: Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes

    doi: 10.1371/journal.pone.0109408

    Figure Lengend Snippet: Secondary structural characteristic of the folded RNase-A at pH 7.0 and 25°C. Representative CD spectra of folded RNase-A (from heat-, GdmCl-, urea-induced denatured states) obtained from refolding in the presence of 1 M osmolytes. The CD spectra of the refolded RNase-A in the absence of osmolytes is identical with the native CD spectra and is omitted. Therefore, we have shown spectra only for the native (without refolding) control in this figure.

    Article Snippet: Materials and Methods Commercially lyophilized preparation of Ribonuclease-A (type III-A) from bovine pancreas (RNase-A) was purchased from Sigma Chemical Co. Trimethylamine N-oxide (TMAO), betaine, sarcosine, proline, glycine, β-alanine and cytidine 2′–3′ cyclic monophosphate (C > p) were also purchased from Sigma Chemical Co. Guanidinium chloride (GdmCl) and urea were obtained from MP Biomedicals.

    Techniques:

    Tertiary structural characteristic of folded RNase-A at pH 7.0 and 25°C. Representative CD spectra of folded RNase-A (from heat-, GdmCl-, urea-induced denatured states) obtained from refolding in the presence of 1 M osmolytes. The CD spectra of the refolded RNase-A in the absence of osmolytes is identical with the native CD spectra and is omitted. Therefore, we have shown spectra only for the native (without refolding) control in this figure.

    Journal: PLoS ONE

    Article Title: Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes

    doi: 10.1371/journal.pone.0109408

    Figure Lengend Snippet: Tertiary structural characteristic of folded RNase-A at pH 7.0 and 25°C. Representative CD spectra of folded RNase-A (from heat-, GdmCl-, urea-induced denatured states) obtained from refolding in the presence of 1 M osmolytes. The CD spectra of the refolded RNase-A in the absence of osmolytes is identical with the native CD spectra and is omitted. Therefore, we have shown spectra only for the native (without refolding) control in this figure.

    Article Snippet: Materials and Methods Commercially lyophilized preparation of Ribonuclease-A (type III-A) from bovine pancreas (RNase-A) was purchased from Sigma Chemical Co. Trimethylamine N-oxide (TMAO), betaine, sarcosine, proline, glycine, β-alanine and cytidine 2′–3′ cyclic monophosphate (C > p) were also purchased from Sigma Chemical Co. Guanidinium chloride (GdmCl) and urea were obtained from MP Biomedicals.

    Techniques:

    Secondary structural characteristic of various denatured states of RNase-A at pH 7.0. The GdmCl- and urea- induced denatured states were generated using 6.5 M GdmCl and 8.5 M urea respectively. The heat induced-denatured state was generated by incubating the protein at 85°C for 15 minutes.

    Journal: PLoS ONE

    Article Title: Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes

    doi: 10.1371/journal.pone.0109408

    Figure Lengend Snippet: Secondary structural characteristic of various denatured states of RNase-A at pH 7.0. The GdmCl- and urea- induced denatured states were generated using 6.5 M GdmCl and 8.5 M urea respectively. The heat induced-denatured state was generated by incubating the protein at 85°C for 15 minutes.

    Article Snippet: Materials and Methods Commercially lyophilized preparation of Ribonuclease-A (type III-A) from bovine pancreas (RNase-A) was purchased from Sigma Chemical Co. Trimethylamine N-oxide (TMAO), betaine, sarcosine, proline, glycine, β-alanine and cytidine 2′–3′ cyclic monophosphate (C > p) were also purchased from Sigma Chemical Co. Guanidinium chloride (GdmCl) and urea were obtained from MP Biomedicals.

    Techniques: Generated

    Effect of osmolytes on the stability of folded RNase-A at pH 7.0. Representative thermal denaturation curves of folded RNase-A obtained from refolding of various denatured states in the presence of 1 M osmolytes. Denaturation curves of the refolded RNase-A (from heat-, GdmCl-, urea-induced denatured states) in the absence of osmolytes are identical with the native (without refolding) transition curve. Therefore, we have shown only the transition curve of the native (without refolding) protein.

    Journal: PLoS ONE

    Article Title: Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes

    doi: 10.1371/journal.pone.0109408

    Figure Lengend Snippet: Effect of osmolytes on the stability of folded RNase-A at pH 7.0. Representative thermal denaturation curves of folded RNase-A obtained from refolding of various denatured states in the presence of 1 M osmolytes. Denaturation curves of the refolded RNase-A (from heat-, GdmCl-, urea-induced denatured states) in the absence of osmolytes are identical with the native (without refolding) transition curve. Therefore, we have shown only the transition curve of the native (without refolding) protein.

    Article Snippet: Materials and Methods Commercially lyophilized preparation of Ribonuclease-A (type III-A) from bovine pancreas (RNase-A) was purchased from Sigma Chemical Co. Trimethylamine N-oxide (TMAO), betaine, sarcosine, proline, glycine, β-alanine and cytidine 2′–3′ cyclic monophosphate (C > p) were also purchased from Sigma Chemical Co. Guanidinium chloride (GdmCl) and urea were obtained from MP Biomedicals.

    Techniques:

    Effect of osmolytes on k cat of RNase-A. Plot of Δ k cat versus [osmolyte]. Δ k cat of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.

    Journal: PLoS ONE

    Article Title: Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes

    doi: 10.1371/journal.pone.0109408

    Figure Lengend Snippet: Effect of osmolytes on k cat of RNase-A. Plot of Δ k cat versus [osmolyte]. Δ k cat of folded RNase-A obtained from refolding of heat-, GdmCl- and urea-induced denatured states are represented by (▴), (•) and (○), respectively.

    Article Snippet: Materials and Methods Commercially lyophilized preparation of Ribonuclease-A (type III-A) from bovine pancreas (RNase-A) was purchased from Sigma Chemical Co. Trimethylamine N-oxide (TMAO), betaine, sarcosine, proline, glycine, β-alanine and cytidine 2′–3′ cyclic monophosphate (C > p) were also purchased from Sigma Chemical Co. Guanidinium chloride (GdmCl) and urea were obtained from MP Biomedicals.

    Techniques:

    Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine RNase A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).

    Journal: International Journal of Molecular Sciences

    Article Title: Expression Patterns and Functional Novelty of Ribonuclease 1 in Herbivorous Megalobrama amblycephala

    doi: 10.3390/ijms17050786

    Figure Lengend Snippet: Ribonucleolytic activities of M. amblycephala recombinant protein RNase1. Comparison the ribonucleolytic activities of Ma- RNase1 and bovine RNase A at different amounts ( A ); RNase activity against yeast tRNA at different pH levels ( B ).

    Article Snippet: For comparison, in another experiment, we added a series of amounts of commercial bovine RNase A (Sigma-Aldrich, St. Louis, MO, USA).

    Techniques: Recombinant, Activity Assay

    Ribbon representations of 3D structures of four fish RNase1 and two mammals RNase A. The blue, light blue and green ribbons represent the three α-helices and ribbons with others colors represent the six β-strands.

    Journal: International Journal of Molecular Sciences

    Article Title: Expression Patterns and Functional Novelty of Ribonuclease 1 in Herbivorous Megalobrama amblycephala

    doi: 10.3390/ijms17050786

    Figure Lengend Snippet: Ribbon representations of 3D structures of four fish RNase1 and two mammals RNase A. The blue, light blue and green ribbons represent the three α-helices and ribbons with others colors represent the six β-strands.

    Article Snippet: For comparison, in another experiment, we added a series of amounts of commercial bovine RNase A (Sigma-Aldrich, St. Louis, MO, USA).

    Techniques: Fluorescence In Situ Hybridization

    Analysis of the synthetic glycoproteins. Panel A, SDS-PAGE: lane 1, natural RNase B; lane 2, GlcNAc-RNase; lane 3, glycoprotein  2 ; lane 4, glycoprotein 1. Panel B, ESI-MS of glycoprotein  2 ; Panel C, ESI-MS of glycoprotein  1 .

    Journal: Journal of the American Chemical Society

    Article Title: Convergent Synthesis of Homogeneous Glc1Man9GlcNAc2-Protein and Derivatives as Ligands of Molecular Chaperones in Protein Quality Control

    doi: 10.1021/ja204831z

    Figure Lengend Snippet: Analysis of the synthetic glycoproteins. Panel A, SDS-PAGE: lane 1, natural RNase B; lane 2, GlcNAc-RNase; lane 3, glycoprotein 2 ; lane 4, glycoprotein 1. Panel B, ESI-MS of glycoprotein 2 ; Panel C, ESI-MS of glycoprotein 1 .

    Article Snippet: Bovine pancreatic ribonuclease B was purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: SDS Page, Mass Spectrometry

    RNA-hydrolyzing activity of different glycoforms of ribonuclease B (RB). A solution of yeast RNA (0.5 mg/ml) was incubated with each of the RNase glycoforms (4 µg/ml) in a buffer (pH 5.0), and the UV absorbance (300 nm) of the solution was recorded.

    Journal: Journal of the American Chemical Society

    Article Title: Convergent Synthesis of Homogeneous Glc1Man9GlcNAc2-Protein and Derivatives as Ligands of Molecular Chaperones in Protein Quality Control

    doi: 10.1021/ja204831z

    Figure Lengend Snippet: RNA-hydrolyzing activity of different glycoforms of ribonuclease B (RB). A solution of yeast RNA (0.5 mg/ml) was incubated with each of the RNase glycoforms (4 µg/ml) in a buffer (pH 5.0), and the UV absorbance (300 nm) of the solution was recorded.

    Article Snippet: Bovine pancreatic ribonuclease B was purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: Activity Assay, Incubation

    The CD spectra of different glycoforms of ribonuclease. GN-RB, the GlcNAc-RB; LacM9GN2-RB, Gal 1 Glc 1 Man 9 GlcNAc 2 -RB; M9GN2-RB, Man 9 GlcNAc 2 -RB; GlcM9GN2-RB, Glc 1 Man 9 GlcNAc 2 -RB; M5–9GN2-RB, Man 5–9 GlcNAc 2 -RB (the natural bovine RNase B). Except

    Journal: Journal of the American Chemical Society

    Article Title: Convergent Synthesis of Homogeneous Glc1Man9GlcNAc2-Protein and Derivatives as Ligands of Molecular Chaperones in Protein Quality Control

    doi: 10.1021/ja204831z

    Figure Lengend Snippet: The CD spectra of different glycoforms of ribonuclease. GN-RB, the GlcNAc-RB; LacM9GN2-RB, Gal 1 Glc 1 Man 9 GlcNAc 2 -RB; M9GN2-RB, Man 9 GlcNAc 2 -RB; GlcM9GN2-RB, Glc 1 Man 9 GlcNAc 2 -RB; M5–9GN2-RB, Man 5–9 GlcNAc 2 -RB (the natural bovine RNase B). Except

    Article Snippet: Bovine pancreatic ribonuclease B was purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: Gas Chromatography

    Con A enrichment of Man8-abundant RNase B. Shown are the glycan profiles of RNase B from the commercial source before and after affinity enrichment with Con A lectin column.

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

    Article Title: Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

    doi: 10.1073/pnas.1608795113

    Figure Lengend Snippet: Con A enrichment of Man8-abundant RNase B. Shown are the glycan profiles of RNase B from the commercial source before and after affinity enrichment with Con A lectin column.

    Article Snippet: Crude bovine pancreatic RNase B (Sigma-Aldrich) was first enriched for the Man8 GlcNAc2 -abundant species.

    Techniques:

    Additional experiments of the demannosylation of RNase B variants by Htm1p–Pdi1p. ( A ) The change in the relative abundance of Man7 on RBsp and Carb-RB during the time course of incubation with Htm1p–Pdi1p. Shown are the mean values ±

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

    Article Title: Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

    doi: 10.1073/pnas.1608795113

    Figure Lengend Snippet: Additional experiments of the demannosylation of RNase B variants by Htm1p–Pdi1p. ( A ) The change in the relative abundance of Man7 on RBsp and Carb-RB during the time course of incubation with Htm1p–Pdi1p. Shown are the mean values ±

    Article Snippet: Crude bovine pancreatic RNase B (Sigma-Aldrich) was first enriched for the Man8 GlcNAc2 -abundant species.

    Techniques: Incubation

    Htm1p–Pdi1p preferentially demannosylates partially structured RNase B variants. ( A ) Schematic presentation of the generation of RNase B variants. RNase BS and RBsp were generated through subtilisin and TCA treatment. Additionally, RNase B was

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

    Article Title: Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

    doi: 10.1073/pnas.1608795113

    Figure Lengend Snippet: Htm1p–Pdi1p preferentially demannosylates partially structured RNase B variants. ( A ) Schematic presentation of the generation of RNase B variants. RNase BS and RBsp were generated through subtilisin and TCA treatment. Additionally, RNase B was

    Article Snippet: Crude bovine pancreatic RNase B (Sigma-Aldrich) was first enriched for the Man8 GlcNAc2 -abundant species.

    Techniques: Generated

    Htm1p–Pdi1p efficiently demannosylates RBsp. ( A ) Schematic presentation of the generation of RBsp. Native RNase B was treated with subtilisin in a 100:1 ratio at 4 °C for 24 h to generate RNase BS with a nick between the N-terminal S peptide

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

    Article Title: Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

    doi: 10.1073/pnas.1608795113

    Figure Lengend Snippet: Htm1p–Pdi1p efficiently demannosylates RBsp. ( A ) Schematic presentation of the generation of RBsp. Native RNase B was treated with subtilisin in a 100:1 ratio at 4 °C for 24 h to generate RNase BS with a nick between the N-terminal S peptide

    Article Snippet: Crude bovine pancreatic RNase B (Sigma-Aldrich) was first enriched for the Man8 GlcNAc2 -abundant species.

    Techniques:

    Folding states of RNase B variants. ( A ) Each RNase B variant (10 µM) was treated with 50 ng of trypsin in a total volume of 30 µL at room temperature. At the indicated time points, 10-µL samples were collected and mixed with PMSF

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

    Article Title: Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

    doi: 10.1073/pnas.1608795113

    Figure Lengend Snippet: Folding states of RNase B variants. ( A ) Each RNase B variant (10 µM) was treated with 50 ng of trypsin in a total volume of 30 µL at room temperature. At the indicated time points, 10-µL samples were collected and mixed with PMSF

    Article Snippet: Crude bovine pancreatic RNase B (Sigma-Aldrich) was first enriched for the Man8 GlcNAc2 -abundant species.

    Techniques: Variant Assay

    1 H-NMR analysis of the glycan released from RNase B before and after overnight incubation with Htm1p–Pdi1p. ( A ) Representative N-glycan structures that cover all potential monosaccharide linkages found on RBsp. The nomenclature and peak assignment

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

    Article Title: Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

    doi: 10.1073/pnas.1608795113

    Figure Lengend Snippet: 1 H-NMR analysis of the glycan released from RNase B before and after overnight incubation with Htm1p–Pdi1p. ( A ) Representative N-glycan structures that cover all potential monosaccharide linkages found on RBsp. The nomenclature and peak assignment

    Article Snippet: Crude bovine pancreatic RNase B (Sigma-Aldrich) was first enriched for the Man8 GlcNAc2 -abundant species.

    Techniques: Nuclear Magnetic Resonance, Incubation

    DDX17 interacts with essential splicing factors. (a) Schematic representation of HIV-1 genome organization and mapping of the splice sites described in this manuscript. Other known sites have been omitted for simplicity. (b) Exogenously expressed Myc-DDX17 co-immunoprecipitates with endogenous U2AF65, SRSF1/SF2 and U1-C. IgG lane, immunoprecipitation of proteins treated with isotype control matched antibody. In RNase-treated lane, samples were subjected to digestion with RNase A. (c) HeLa M cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of siDDX17 rescue expressor construct. Expression of U2AF65, SRSF1/SF2 and U1-C, following knockdown and rescue of DDX17 was detected by Western blotting, using their respective antibodies. GAPDH was detected to monitor sample loading. (d) Effect of overexpression of DDX5 as attempted rescue of HIV-1 virus production following endogenous DDX17 depletion. Cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of DDX5 expressor construct. (e) Western blot for DDX17 and DDX5 expression. The graph is a representative of three independent experiments done in triplicate. Bars represent mean of triplicate samples ± SEM. Statistical significance: ** P

    Journal: Journal of Molecular Biology

    Article Title: DDX17 Specifically, and Independently of DDX5, Controls Use of the HIV A4/5 Splice Acceptor Cluster and Is Essential for Efficient Replication of HIV

    doi: 10.1016/j.jmb.2018.06.052

    Figure Lengend Snippet: DDX17 interacts with essential splicing factors. (a) Schematic representation of HIV-1 genome organization and mapping of the splice sites described in this manuscript. Other known sites have been omitted for simplicity. (b) Exogenously expressed Myc-DDX17 co-immunoprecipitates with endogenous U2AF65, SRSF1/SF2 and U1-C. IgG lane, immunoprecipitation of proteins treated with isotype control matched antibody. In RNase-treated lane, samples were subjected to digestion with RNase A. (c) HeLa M cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of siDDX17 rescue expressor construct. Expression of U2AF65, SRSF1/SF2 and U1-C, following knockdown and rescue of DDX17 was detected by Western blotting, using their respective antibodies. GAPDH was detected to monitor sample loading. (d) Effect of overexpression of DDX5 as attempted rescue of HIV-1 virus production following endogenous DDX17 depletion. Cells were sequentially transfected with siControl or siDDX17 and then a second round of siRNA together with pLAI, with or without increasing concentrations of DDX5 expressor construct. (e) Western blot for DDX17 and DDX5 expression. The graph is a representative of three independent experiments done in triplicate. Bars represent mean of triplicate samples ± SEM. Statistical significance: ** P

    Article Snippet: This was followed by 5 μl per 500-μl reaction mix RNase A (Sigma) treatment for 10 min at 4 °C.

    Techniques: Immunoprecipitation, Transfection, Construct, Expressing, Western Blot, Over Expression