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  • 99
    Thermo Fisher rnase inhibitor
    Ribonuclease activity of the recombinant <t>TcPR-4b</t> on tomato ( Solanum lycopersicum var. Micro-Tom) total RNA (5 μg). The incubation with TcPR-4b was carried out for 30 min at 25°C. The boiling conditions were 10 min at 95°C. The <t>RNase</t> inhibitor was the RiboLock (40 U; Thermo Scientific). The incubation conditions of the RNase A (Thermo Scientific) were 10 min at 25°C.
    Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 23322 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase inhibitor/product/Thermo Fisher
    Average 99 stars, based on 23322 article reviews
    Price from $9.99 to $1999.99
    rnase inhibitor - by Bioz Stars, 2020-07
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    98
    Qiagen rnase inhibitor
    (a) SDS-PAGE of <t>NLP.</t> Lane 1, protein molecular mass marker; lane 2, untreated VSV NLP; lane 3, empty NLP after <t>RNase</t> A treatment; lane 4, reconstituted VSV NLP containing poly(rA) RNA. (b) Image of crystals of NLP with encapsidated poly(rG) RNA.
    Rnase Inhibitor, supplied by Qiagen, used in various techniques. Bioz Stars score: 98/100, based on 814 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase inhibitor/product/Qiagen
    Average 98 stars, based on 814 article reviews
    Price from $9.99 to $1999.99
    rnase inhibitor - by Bioz Stars, 2020-07
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    92
    GE Healthcare rnasin rnase inhibitor
    (a) SDS-PAGE of <t>NLP.</t> Lane 1, protein molecular mass marker; lane 2, untreated VSV NLP; lane 3, empty NLP after <t>RNase</t> A treatment; lane 4, reconstituted VSV NLP containing poly(rA) RNA. (b) Image of crystals of NLP with encapsidated poly(rG) RNA.
    Rnasin Rnase Inhibitor, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnasin rnase inhibitor/product/GE Healthcare
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
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    99
    Promega rnase inhibitor rnasin
    Telomerase activity in kinetoplastid parasites. Lanes 1–6, T. brucei DEAE eluate; lanes 8–13, L. tarentolae DEAE eluate; lanes 15–20, L. major DEAE eluate. Telomerase products were fractionated in 10% sequencing gels to reveal the periodicity of banding pattern. In lanes 2, 9, and 16, extracts were pretreated with <t>RNase</t> A; lanes 3, 10, and 17, <t>RNasin</t> incubated with extract before addition of RNase; lanes 4, 11, and 18, RNase A was added after telomerase step incubation (+). nTS, reaction performed without the forward primer; nC, reaction performed in the absence of CX-ext; nE, reaction in which the extracts were omitted. ( A ) One-tube TRAP using primer CX-ext as reverse primer and semipurified extracts. ( B ) Two-tube modified TRAP using CX-ext reverse primer. The assays were performed with half the amount of DEAE fractions used in A .
    Rnase Inhibitor Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 643 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase inhibitor rnasin/product/Promega
    Average 99 stars, based on 643 article reviews
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    rnase inhibitor rnasin - by Bioz Stars, 2020-07
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    93
    TaKaRa rnasin plus rnase inhibitor
    Telomerase activity in kinetoplastid parasites. Lanes 1–6, T. brucei DEAE eluate; lanes 8–13, L. tarentolae DEAE eluate; lanes 15–20, L. major DEAE eluate. Telomerase products were fractionated in 10% sequencing gels to reveal the periodicity of banding pattern. In lanes 2, 9, and 16, extracts were pretreated with <t>RNase</t> A; lanes 3, 10, and 17, <t>RNasin</t> incubated with extract before addition of RNase; lanes 4, 11, and 18, RNase A was added after telomerase step incubation (+). nTS, reaction performed without the forward primer; nC, reaction performed in the absence of CX-ext; nE, reaction in which the extracts were omitted. ( A ) One-tube TRAP using primer CX-ext as reverse primer and semipurified extracts. ( B ) Two-tube modified TRAP using CX-ext reverse primer. The assays were performed with half the amount of DEAE fractions used in A .
    Rnasin Plus Rnase Inhibitor, supplied by TaKaRa, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GenBiotech rnase inhibitor rnasin
    Telomerase activity in kinetoplastid parasites. Lanes 1–6, T. brucei DEAE eluate; lanes 8–13, L. tarentolae DEAE eluate; lanes 15–20, L. major DEAE eluate. Telomerase products were fractionated in 10% sequencing gels to reveal the periodicity of banding pattern. In lanes 2, 9, and 16, extracts were pretreated with <t>RNase</t> A; lanes 3, 10, and 17, <t>RNasin</t> incubated with extract before addition of RNase; lanes 4, 11, and 18, RNase A was added after telomerase step incubation (+). nTS, reaction performed without the forward primer; nC, reaction performed in the absence of CX-ext; nE, reaction in which the extracts were omitted. ( A ) One-tube TRAP using primer CX-ext as reverse primer and semipurified extracts. ( B ) Two-tube modified TRAP using CX-ext reverse primer. The assays were performed with half the amount of DEAE fractions used in A .
    Rnase Inhibitor Rnasin, supplied by GenBiotech, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase inhibitor rnasin/product/GenBiotech
    Average 92 stars, based on 2 article reviews
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    rnase inhibitor rnasin - by Bioz Stars, 2020-07
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    Image Search Results


    Ribonuclease activity of the recombinant TcPR-4b on tomato ( Solanum lycopersicum var. Micro-Tom) total RNA (5 μg). The incubation with TcPR-4b was carried out for 30 min at 25°C. The boiling conditions were 10 min at 95°C. The RNase inhibitor was the RiboLock (40 U; Thermo Scientific). The incubation conditions of the RNase A (Thermo Scientific) were 10 min at 25°C.

    Journal: BMC Plant Biology

    Article Title: The pathogenesis-related protein PR-4b from Theobroma cacao presents RNase activity, Ca2+ and Mg2+ dependent-DNase activity and antifungal action on Moniliophthora perniciosa

    doi: 10.1186/1471-2229-14-161

    Figure Lengend Snippet: Ribonuclease activity of the recombinant TcPR-4b on tomato ( Solanum lycopersicum var. Micro-Tom) total RNA (5 μg). The incubation with TcPR-4b was carried out for 30 min at 25°C. The boiling conditions were 10 min at 95°C. The RNase inhibitor was the RiboLock (40 U; Thermo Scientific). The incubation conditions of the RNase A (Thermo Scientific) were 10 min at 25°C.

    Article Snippet: As observed in other works [ , , ], the RNase activity of TcPR-4b was inhibited by heating and in the presence of RNase inhibitor (RiboLock, Thermo Scientific) which is able to annul the activity of type A, B and C RNases.

    Techniques: Activity Assay, Recombinant, Incubation

    Action of TcPR-4b on dikaryotic M. perniciosa survival in relation to RNase and DNase activity. A . Action of TcPR-4b on dikaryotic M. perniciosa survival in presence of RNase inhibitor. The following concentrations were used: 40 μg/ml of TcPR-4b and 800 U of RNase inhibitor. B . Action of TcPR-4b on dikaryotic M. perniciosa survival in presence of MgCl 2 . The following concentrations were used: 40 μg/ml of TcPR-4b and 10 mM of MgCl 2 .

    Journal: BMC Plant Biology

    Article Title: The pathogenesis-related protein PR-4b from Theobroma cacao presents RNase activity, Ca2+ and Mg2+ dependent-DNase activity and antifungal action on Moniliophthora perniciosa

    doi: 10.1186/1471-2229-14-161

    Figure Lengend Snippet: Action of TcPR-4b on dikaryotic M. perniciosa survival in relation to RNase and DNase activity. A . Action of TcPR-4b on dikaryotic M. perniciosa survival in presence of RNase inhibitor. The following concentrations were used: 40 μg/ml of TcPR-4b and 800 U of RNase inhibitor. B . Action of TcPR-4b on dikaryotic M. perniciosa survival in presence of MgCl 2 . The following concentrations were used: 40 μg/ml of TcPR-4b and 10 mM of MgCl 2 .

    Article Snippet: As observed in other works [ , , ], the RNase activity of TcPR-4b was inhibited by heating and in the presence of RNase inhibitor (RiboLock, Thermo Scientific) which is able to annul the activity of type A, B and C RNases.

    Techniques: Activity Assay

    (a) SDS-PAGE of NLP. Lane 1, protein molecular mass marker; lane 2, untreated VSV NLP; lane 3, empty NLP after RNase A treatment; lane 4, reconstituted VSV NLP containing poly(rA) RNA. (b) Image of crystals of NLP with encapsidated poly(rG) RNA.

    Journal: Journal of Virology

    Article Title: Access to RNA Encapsidated in the Nucleocapsid of Vesicular Stomatitis Virus ▿

    doi: 10.1128/JVI.01927-10

    Figure Lengend Snippet: (a) SDS-PAGE of NLP. Lane 1, protein molecular mass marker; lane 2, untreated VSV NLP; lane 3, empty NLP after RNase A treatment; lane 4, reconstituted VSV NLP containing poly(rA) RNA. (b) Image of crystals of NLP with encapsidated poly(rG) RNA.

    Article Snippet: In the presence of RNase inhibitor (Qiagen), the empty NLP was incubated with poly(rA) (Midland) at a molar ratio of 1:5 for 15 min at 42°C.

    Techniques: SDS Page, Marker

    RNA analysis and electron microscopy of VSV nucleocapsid-like particles (NLP) and viral nucleocapsids digested with RNase A. (a) RNA electrophoresis. Purified VSV NLP treated with RNase A (1 mg/ml, final concentration) at room temperature (lane 3), 37°C

    Journal: Journal of Virology

    Article Title: Access to RNA Encapsidated in the Nucleocapsid of Vesicular Stomatitis Virus ▿

    doi: 10.1128/JVI.01927-10

    Figure Lengend Snippet: RNA analysis and electron microscopy of VSV nucleocapsid-like particles (NLP) and viral nucleocapsids digested with RNase A. (a) RNA electrophoresis. Purified VSV NLP treated with RNase A (1 mg/ml, final concentration) at room temperature (lane 3), 37°C

    Article Snippet: In the presence of RNase inhibitor (Qiagen), the empty NLP was incubated with poly(rA) (Midland) at a molar ratio of 1:5 for 15 min at 42°C.

    Techniques: Electron Microscopy, Electrophoresis, Purification, Concentration Assay

    Telomerase activity in kinetoplastid parasites. Lanes 1–6, T. brucei DEAE eluate; lanes 8–13, L. tarentolae DEAE eluate; lanes 15–20, L. major DEAE eluate. Telomerase products were fractionated in 10% sequencing gels to reveal the periodicity of banding pattern. In lanes 2, 9, and 16, extracts were pretreated with RNase A; lanes 3, 10, and 17, RNasin incubated with extract before addition of RNase; lanes 4, 11, and 18, RNase A was added after telomerase step incubation (+). nTS, reaction performed without the forward primer; nC, reaction performed in the absence of CX-ext; nE, reaction in which the extracts were omitted. ( A ) One-tube TRAP using primer CX-ext as reverse primer and semipurified extracts. ( B ) Two-tube modified TRAP using CX-ext reverse primer. The assays were performed with half the amount of DEAE fractions used in A .

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

    Article Title: Telomerase in kinetoplastid parasitic protozoa

    doi:

    Figure Lengend Snippet: Telomerase activity in kinetoplastid parasites. Lanes 1–6, T. brucei DEAE eluate; lanes 8–13, L. tarentolae DEAE eluate; lanes 15–20, L. major DEAE eluate. Telomerase products were fractionated in 10% sequencing gels to reveal the periodicity of banding pattern. In lanes 2, 9, and 16, extracts were pretreated with RNase A; lanes 3, 10, and 17, RNasin incubated with extract before addition of RNase; lanes 4, 11, and 18, RNase A was added after telomerase step incubation (+). nTS, reaction performed without the forward primer; nC, reaction performed in the absence of CX-ext; nE, reaction in which the extracts were omitted. ( A ) One-tube TRAP using primer CX-ext as reverse primer and semipurified extracts. ( B ) Two-tube modified TRAP using CX-ext reverse primer. The assays were performed with half the amount of DEAE fractions used in A .

    Article Snippet: Activity in the extracts was tested for RNase A sensitivity by incubation with 100 ng of RNase A (Sigma) for 5 min at 37°C before or after the telomerase reaction step and with or without 1 unit of RNase inhibitor RNasin (Promega) before addition of RNase A.

    Techniques: Activity Assay, Sequencing, Incubation, Modification

    T. brucei activity monitored directly by telomerase primer-extension assay. Reactions were performed with DEAE fraction and primer tel 2. Lane 1, standard reaction; lane 2, extract pretreated with 100 ng of RNase A; lane 3, extract incubated with RNasin before addition of RNase A; lane 4, RNase A treatment after telomerase reaction (+); lane 5, nP, no input primer, lane 6, nE, extract substituted by reaction buffer; lane M, terminal deoxynucleotidyltransferase used to label tel 6 with [α- 32 P]dCTP (19 indicates the position of the primer plus 1-nt molecular weight marker).

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

    Article Title: Telomerase in kinetoplastid parasitic protozoa

    doi:

    Figure Lengend Snippet: T. brucei activity monitored directly by telomerase primer-extension assay. Reactions were performed with DEAE fraction and primer tel 2. Lane 1, standard reaction; lane 2, extract pretreated with 100 ng of RNase A; lane 3, extract incubated with RNasin before addition of RNase A; lane 4, RNase A treatment after telomerase reaction (+); lane 5, nP, no input primer, lane 6, nE, extract substituted by reaction buffer; lane M, terminal deoxynucleotidyltransferase used to label tel 6 with [α- 32 P]dCTP (19 indicates the position of the primer plus 1-nt molecular weight marker).

    Article Snippet: Activity in the extracts was tested for RNase A sensitivity by incubation with 100 ng of RNase A (Sigma) for 5 min at 37°C before or after the telomerase reaction step and with or without 1 unit of RNase inhibitor RNasin (Promega) before addition of RNase A.

    Techniques: Activity Assay, Primer Extension Assay, Incubation, Molecular Weight, Marker

    FUS forms a complex with itself, PABP and RNA. ( A ) Co-immunoprecipitation of HA-FUS, Myc-FUS and PABP from HEK293T cells. Immunoprecipitation with a Myc (mouse anti-Myc, CST) antibody pulled down PABP (mouse anti-PABP, Sigma) along with anti-HA-FUS (rabbit HA, CST). RNasin was added to block all RNase activity. ( B ) The interaction between HA-FUS and Myc-FUS was not altered by the addition of RNase, while the co-immunoprecipitation of PABP was completely abolished. ( C ) Immunoprecipitation of FUS (mouse anti-FUS, Santa Cruz) from untransfected cells shows that endogenous FUS (rabbit anti-FUS, Novus Biologicals) also interacts with PABP (mouse anti-PABP, Sigma) and treatment with RNase shows that this interaction is also dependent on RNA. ( D ) Mock immunoprecipitation experiments with either untransfected cells or a single transfection of either HA-FUS WT or Myc-FUS WT with no antibody showed that neither endogenous nor tagged FUS binds to the beads. ( E ) Immunoprecipitation of single transfections with an antibody to the wrong tag showed that a Myc antibody does not pull down HA-FUS and a HA antibody does not precipitate Myc-FUS. FT indicates flow-through of proteins that did not bind to the beads.

    Journal: Human Molecular Genetics

    Article Title: ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules

    doi: 10.1093/hmg/ddt117

    Figure Lengend Snippet: FUS forms a complex with itself, PABP and RNA. ( A ) Co-immunoprecipitation of HA-FUS, Myc-FUS and PABP from HEK293T cells. Immunoprecipitation with a Myc (mouse anti-Myc, CST) antibody pulled down PABP (mouse anti-PABP, Sigma) along with anti-HA-FUS (rabbit HA, CST). RNasin was added to block all RNase activity. ( B ) The interaction between HA-FUS and Myc-FUS was not altered by the addition of RNase, while the co-immunoprecipitation of PABP was completely abolished. ( C ) Immunoprecipitation of FUS (mouse anti-FUS, Santa Cruz) from untransfected cells shows that endogenous FUS (rabbit anti-FUS, Novus Biologicals) also interacts with PABP (mouse anti-PABP, Sigma) and treatment with RNase shows that this interaction is also dependent on RNA. ( D ) Mock immunoprecipitation experiments with either untransfected cells or a single transfection of either HA-FUS WT or Myc-FUS WT with no antibody showed that neither endogenous nor tagged FUS binds to the beads. ( E ) Immunoprecipitation of single transfections with an antibody to the wrong tag showed that a Myc antibody does not pull down HA-FUS and a HA antibody does not precipitate Myc-FUS. FT indicates flow-through of proteins that did not bind to the beads.

    Article Snippet: 5 µl of an RNase A/T1 mix (Fermentas, Yorkshire, UK) or RNasin Plus RNase inhibitor (Promega, Southampton, UK) was added to the tubes and incubated at 37°C for 5 min, then placed back on ice.

    Techniques: Immunoprecipitation, Blocking Assay, Activity Assay, Transfection, Flow Cytometry

    Regulation of IL-8 mRNA expression in immortalized human gingival keratinocytes. (A) A representative storage phosphor scan demonstrates that, by using quantitative RNase protection assay, moderate IL-8 mRNA expression was detected in 8 μg of total RNA from immortalized keratinocytes under normal control conditions as seen at time zero. Following treatment of separate flasks of the same culture over 24 h with 50 ng of PMA per ml, IL-8 mRNA expression dramatically increases over a 6-h period, returning to nearly constitutive levels by 12 h. Test lanes, hours 0 to 24, show the protected probes after binding to IL-8 (374 bp) and GAPDH (220 bp) mRNA, respectively, within the sample, followed by RNase treatment. An increase in the band intensity of GAPDH at 2 to 6 h reflects an increase in the total amount of mRNA, as expected with PMA stimulation. This did not affect quantitation (see panel B, below), since the ratio of GAPDH to IL-8 was still proportionally constant. Control lanes (C1 and C2) show the two probes GAPDH (C1, 266 bp) and IL-8 (C2, 420 bp) to which no RNase has been added. The results are representative of three experiments. (B) Quantitation of IL-8 mRNA in immortalized keratinocytes following induction with PMA. From panel A the signal intensity determined for the IL-8 protected fragment was normalized to the abundance of the internal control GAPDH at each time point. The data shown are the mean ± the standard deviation ( n = 3).

    Journal: Infection and Immunity

    Article Title: Calprotectin Expression by Gingival Epithelial Cells

    doi: 10.1128/IAI.69.5.3248-3254.2001

    Figure Lengend Snippet: Regulation of IL-8 mRNA expression in immortalized human gingival keratinocytes. (A) A representative storage phosphor scan demonstrates that, by using quantitative RNase protection assay, moderate IL-8 mRNA expression was detected in 8 μg of total RNA from immortalized keratinocytes under normal control conditions as seen at time zero. Following treatment of separate flasks of the same culture over 24 h with 50 ng of PMA per ml, IL-8 mRNA expression dramatically increases over a 6-h period, returning to nearly constitutive levels by 12 h. Test lanes, hours 0 to 24, show the protected probes after binding to IL-8 (374 bp) and GAPDH (220 bp) mRNA, respectively, within the sample, followed by RNase treatment. An increase in the band intensity of GAPDH at 2 to 6 h reflects an increase in the total amount of mRNA, as expected with PMA stimulation. This did not affect quantitation (see panel B, below), since the ratio of GAPDH to IL-8 was still proportionally constant. Control lanes (C1 and C2) show the two probes GAPDH (C1, 266 bp) and IL-8 (C2, 420 bp) to which no RNase has been added. The results are representative of three experiments. (B) Quantitation of IL-8 mRNA in immortalized keratinocytes following induction with PMA. From panel A the signal intensity determined for the IL-8 protected fragment was normalized to the abundance of the internal control GAPDH at each time point. The data shown are the mean ± the standard deviation ( n = 3).

    Article Snippet: The radiolabeled probes were synthesized under the following reaction conditions: 500 μM concentrations each of rCTP, rGTP, and rATP, and 1 μM rUTP; 3 μM [α-32 P]UTP (800 Ci/mmol, 10 mCi/ml) (DuPont NEN Research Products, Boston, Mass.); 0.5 μl of PCR template; 1 U of T7 or T3 RNA polymerase (Stratagene); 2 μl of transcription buffer (Stratagene); 40 U of RNase inhibitor (Promega, Madison, Wis.); and distilled H2 O to a total volume of 10 μl.

    Techniques: Expressing, Rnase Protection Assay, Binding Assay, Quantitation Assay, Standard Deviation