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  • 99
    New England Biolabs rnase inhibitor
    Rnase Inhibitor, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 2256 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rnase inhibitor
    Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 23259 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega rnase inhibitor
    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of <t>VTM.</t> RNaseAlert was added to viral transport media (VTM) with or without the addition of <t>RNasin</t> Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.
    Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 10606 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher ribolock rnase inhibitor
    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of <t>VTM.</t> RNaseAlert was added to viral transport media (VTM) with or without the addition of <t>RNasin</t> Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.
    Ribolock Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5169 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rnase inhibitor
    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of <t>VTM.</t> RNaseAlert was added to viral transport media (VTM) with or without the addition of <t>RNasin</t> Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.
    Rnase Inhibitor, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superase in rnase inhibitor
    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of <t>VTM.</t> RNaseAlert was added to viral transport media (VTM) with or without the addition of <t>RNasin</t> Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.
    Superase In Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 952 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superase• in rnase inhibitor
    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of <t>VTM.</t> RNaseAlert was added to viral transport media (VTM) with or without the addition of <t>RNasin</t> Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.
    Superase• In Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1031 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa recombinant rnase inhibitor
    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of <t>VTM.</t> RNaseAlert was added to viral transport media (VTM) with or without the addition of <t>RNasin</t> Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.
    Recombinant Rnase Inhibitor, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 608 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Boehringer Mannheim rnasin
    Elevated polyadenylation activity of the dark extract. Polyadenylation was assayed under the conditions described for the in vitro processing assays except that 2 mM <t>ATP</t> and 20 U <t>RNasin</t> were added to inactivate the endogenous nucleases. After the indicated times the reaction was stopped and the RNA products analyzed by electrophoresis and autoradiography. Control assays were incubated for 40 min in the presence of 4 mM cordycepin (Sigma; lanes 40′ + Cord.).
    Rnasin, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 207 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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 706 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Qiagen rnasein
    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
    Rnasein, supplied by Qiagen, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher rnase inhibitors
    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 Inhibitors, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 800 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    RNA safe reagent is a highly active RNase Inhibition It thoroughly removes RNase contamination to preserve the intactness of RNA Features: ■ complete removal of Rnase ■ Treated solution could
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    N/A
    RNasin is a special RNase inhibitor existing in human placenta It is essentially a protein with molecular weight of 51 000 Da and isoelectric point of pH 4 7 RNasin
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    Image Search Results


    Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of VTM. RNaseAlert was added to viral transport media (VTM) with or without the addition of RNasin Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.

    Journal: Nature Communications

    Article Title: An enhanced isothermal amplification assay for viral detection

    doi: 10.1038/s41467-020-19258-y

    Figure Lengend Snippet: Lysis and detection of SARS-CoV-2 N gene from contrived samples. a Viral particle temperature lysis determination. AccuPlex packaged SARS-CoV-2 virus was diluted into TCEP buffer and heated for 5 min at the given temperature (see “Methods” section). Released RNA was amplified by eRPA and product formation was quantified by qPCR. b Detection of RNase activity of VTM. RNaseAlert was added to viral transport media (VTM) with or without the addition of RNasin Plus before heating for 5 min at 94 °C or added to a 1:1 VTM and viral lysis buffer mix and incubating for 10 min at 25 °C. Data represent the average of four technical replicates and were determined by normalizing the fluorescence intensity 10 min after the heating step to a fully degraded control. c Schematic of sample processing of patient samples in VTM for input into eRPA. d Heatmap displaying eRPA test calls for detection of AccuPlex packaged SARS-CoV-2 lysed with conditions displayed in c . AccuPlex packaged SARS-CoV-2 virus was mixed 1:1 with VTM, PBS, or viral lysis buffer and incubated as shown. All samples included RNasin Plus. Values represent the number of positive test calls: number of negative test calls for each condition. e Inactivation of RNase activity in saliva by TCEP and heat. Saliva was first mixed 1:1 with a buffer containing 1 mM (black diamonds) or 100 mM (red triangles) TCEP and heated at the indicated temperature for 5 min. After cooling, RNaseAlert was added and degradation was assessed as in b . f The combined activities of an RNase inhibitor and TCEP protect RNA from degradation in saliva. RNaseAlert was added to saliva diluted 1:1 with TCEP buffer containing an RNase inhibitor and treated as shown. RNAseAlert degradation was assessed an in b . See additional data in Supplementary Fig. 3g . g Schematic of sample processing of patient saliva samples for input into eRPA. h Heatmap displaying eRPA test calls for detection of SARS-CoV-2 RNA or AccuPlex packaged virus from saliva treated as displayed in g . AccuPlex packaged SARS-CoV-2 virus or SARS-CoV-2 N gene IVT RNA were added to saliva and extracted as shown. Values represent the number of positive test calls: number of negative test calls for each condition. Each experiment was repeated three times with similar results. Source data are available in the Source Data file.

    Article Snippet: RNasin Plus (Promega) was added to VTM to a final concentration of 1 U/µL and was incubated for 5 min at 25 °C before addition of RNaseAlert.

    Techniques: Lysis, Amplification, Real-time Polymerase Chain Reaction, Activity Assay, Fluorescence, Incubation

    Elevated polyadenylation activity of the dark extract. Polyadenylation was assayed under the conditions described for the in vitro processing assays except that 2 mM ATP and 20 U RNasin were added to inactivate the endogenous nucleases. After the indicated times the reaction was stopped and the RNA products analyzed by electrophoresis and autoradiography. Control assays were incubated for 40 min in the presence of 4 mM cordycepin (Sigma; lanes 40′ + Cord.).

    Journal: Nucleic Acids Research

    Article Title: Endonucleolytic activation directs dark-induced chloroplast mRNA degradation

    doi:

    Figure Lengend Snippet: Elevated polyadenylation activity of the dark extract. Polyadenylation was assayed under the conditions described for the in vitro processing assays except that 2 mM ATP and 20 U RNasin were added to inactivate the endogenous nucleases. After the indicated times the reaction was stopped and the RNA products analyzed by electrophoresis and autoradiography. Control assays were incubated for 40 min in the presence of 4 mM cordycepin (Sigma; lanes 40′ + Cord.).

    Article Snippet: The assay contained 40 mM Tris–HCl pH 8.0, 6 mM MgCl2 , 2 mM spermidin, 10 mM DTT, 0.5 mM of GTP, CTP and ATP, 0.1 mM UTP, 10 U RNasin (Boehringer-Mannheim/Roche), 10 U T7-RNA polymerase (Boehringer-Mannheim/Roche) and 100 µCi [α-32 P]UTP (20 µCi/µl, 800 Ci/mmol).

    Techniques: Activity Assay, In Vitro, Electrophoresis, Autoradiography, Incubation

    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