rnasin Promega Search Results


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  • 99
    Thermo Fisher rnase inhibitor
    Rnase Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 18588 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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 1141 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Promega ribonuclease
    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 .
    Ribonuclease, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Promega super rnasein
    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 .
    Super Rnasein, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega rnasin lcb promega
    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 Lcb Promega, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Promega rnasin promega 5
    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 Promega 5, supplied by Promega, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher 11836170001 superasin thermo am2696 rnasin promega n2515
    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 .
    11836170001 Superasin Thermo Am2696 Rnasin Promega N2515, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Promega isoamyl alcohol 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 .
    Isoamyl Alcohol Rnasin Plus Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 87/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega rnasin promega 1
    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 Promega 1, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Promega protector 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 .
    Protector Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Promega superase• in 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 .
    Superase• In Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Promega thermostable 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 .
    Thermostable Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Promega rq1 rnase free dnase
    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 .
    Rq1 Rnase Free Dnase, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 12727 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Promega iu 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 .
    Iu Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Promega rnasin 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 Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 266 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Promega rnasin enzyme
    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 Enzyme, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega placental 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 .
    Placental Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega prime 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 .
    Prime Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Promega 1ul 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 .
    1ul Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Promega rnaase 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 .
    Rnaase Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 81/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Promega ll 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 .
    Ll Rnasin, supplied by Promega, used in various techniques. Bioz Stars score: 84/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega hybridization buffer 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 .
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    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 .
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    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 .
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    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 .
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    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 .
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    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 .
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    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 .
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    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 .
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    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 .
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    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 .
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    Image Search Results


    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

    Coligo topology is necessary but not sufficient to template the synthesis of stable released sRNA transcripts in human WCE. ( A ) Circularization stabilizes oligonucleotides in human WCE. Circular (C) or linear (L) templates (Input) were recovered (Post) from HEK293T WCE IVT, digested with RNase cocktail to reduce cellular RNA, and stained after DPAGE. Linear forms were degraded during IVT; coligos were stable. Coligo 19aRL sequence is shown in Supplementary Figure S2 . ( B ) DPAGE separation of HEK293T WCE IVT of the three coligos and linear precursors from the reactions shown in panel A. ( C ) Transcripts are released from the coligo template during IVT. RNase H (RH) was added to (+) or withheld from (−) the indicated coligo IVT reactions at the end of a typical 90-min incubation period. Following additional incubation, the RNA products were separated by DPAGE. Lanes 1 and 2, validation of exhaustive RNase H activity on a 32 P-RNA:DNA hybrid. Reaction in lane 2 was supplemented with total HEK293T cellular RNA to normalize non-specific competing RNAs among all RNase H reactions. The result shows that the coligo 19aTAR ’s transcripts do not remain hybridized to the coligo template, while ∼20% of coligo 122 ’s transcripts do remain bound to the coligo template.

    Journal: Nucleic Acids Research

    Article Title: Circularized synthetic oligodeoxynucleotides serve as promoterless RNA polymerase III templates for small RNA generation in human cells

    doi: 10.1093/nar/gks1334

    Figure Lengend Snippet: Coligo topology is necessary but not sufficient to template the synthesis of stable released sRNA transcripts in human WCE. ( A ) Circularization stabilizes oligonucleotides in human WCE. Circular (C) or linear (L) templates (Input) were recovered (Post) from HEK293T WCE IVT, digested with RNase cocktail to reduce cellular RNA, and stained after DPAGE. Linear forms were degraded during IVT; coligos were stable. Coligo 19aRL sequence is shown in Supplementary Figure S2 . ( B ) DPAGE separation of HEK293T WCE IVT of the three coligos and linear precursors from the reactions shown in panel A. ( C ) Transcripts are released from the coligo template during IVT. RNase H (RH) was added to (+) or withheld from (−) the indicated coligo IVT reactions at the end of a typical 90-min incubation period. Following additional incubation, the RNA products were separated by DPAGE. Lanes 1 and 2, validation of exhaustive RNase H activity on a 32 P-RNA:DNA hybrid. Reaction in lane 2 was supplemented with total HEK293T cellular RNA to normalize non-specific competing RNAs among all RNase H reactions. The result shows that the coligo 19aTAR ’s transcripts do not remain hybridized to the coligo template, while ∼20% of coligo 122 ’s transcripts do remain bound to the coligo template.

    Article Snippet: A typical 20 µl reaction mixture contained 25 µg total WCE protein, 20 units RNase inhibitor (Promega), 1.25 mM each adenosine triphosphate (ATP), cytidine triphosphate (CTP), guanosine triphosphate (GTP), 0.2 mM uridine triphosphate (UTP), [except B, which contained 1.25 mM each nucleotide triphosphate (NTP)], ∼2 μCi [α-32 P]-UTP, 40 mM Tris–HCl pH 7.9, 6 mM MgCl2 , 10 mM dithiothreitol (DTT), 2 mM spermidine, 100 µM NaCl, 100 nM coligo template unless otherwise indicated.

    Techniques: Staining, Sequencing, Incubation, Activity Assay

    Characterization of MRPP3 ΔMTS alone and in complex with MRPP1 ΔMTS and MRPP2. A , domain organization for MRPP3 ΔMTS indicating the N extension (residues 50–206), PPR domain (residues 207–329, red ), core domain (residues 330–361 and 542–583, yellow ), NYN domain (residues 362–541, brown ), and structural zinc ion bound in a Cys-Cys-His-Cys motif in the core domain. B , top , analytical SEC profiles for the mixture of MRPP1 ΔMTS , MRPP2, and MRPP3 ΔMTS ( green line ) and the mixture of MRPP1 ΔMTS , MRPP2, MRPP3 ΔMTS , and pre-(mt)tRNA Ile ( black line ) applied to a Superdex S200 column. A replicate of this experiment is shown in Fig. S5 . The elution volumes for individual MRPP1 ΔMTS (from Fig. 3 A ), MRPP2 (from Fig. 3 A ), and MRPP3 ΔMTS (from Fig. S4 F ) proteins, as well as the mixture of MRPP1 ΔMTS and MRPP2 (from Fig. 3 A ), are indicated with arrows above the chromatogram ( blue , orange , red , and pink , respectively). Bottom , SDS-PAGE ( first two gel panels ) and urea-PAGE ( last two gel panels ) analysis of eluted fractions to visualize proteins and pre-(mt)tRNA Ile , respectively. The black dashed box indicates lanes where the complex containing MRPP1 ΔMTS , MRPP2, MRPP3, and pre-(mt)tRNA Ile would be found on the SDS-PAGE. C , urea-polyacrylamide denaturing gels showing the RNase P reaction of pre-(mt)tRNA Ile set up, for mixtures of MRPP2 and MRPP3 ΔMTS with different MRPP1 truncated proteins (MRPP1 ΔMTS , MRPP1 MT+C(Δ202) , MRPP1 N ). All lanes shown are taken from one experimental gel only. A downward shift in band location of processed (mt)tRNA Ile relative to that of pre-(mt)tRNA Ile and the concomitant appearance of a band corresponding to the removed 5′-leader indicate RNase P activity. D , urea-polyacrylamide denaturing gels showing the RNase P reaction of pre-(mt)tRNA Ile set up for the complex of MRPP1 ΔMTS and MRPP2 without MRPP3 ( lane 2 ) and in the presence of different truncated MRPP3 proteins ( lanes 3–6 ). A negative control of MRPP1 ΔMTS , MRPP2, and MRPP3 ΔMTS mixed with EDTA ( lane 1 ) is included. M r RNA markers are shown ( lane M ). All lanes shown are taken from one experimental gel only. Reactions in C and D were run for 30 min at protein concentrations of 300 n m MRPP1–MRPP2 and 150 n m MRPP3.

    Journal: The Journal of Biological Chemistry

    Article Title: Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes

    doi: 10.1074/jbc.RA117.001286

    Figure Lengend Snippet: Characterization of MRPP3 ΔMTS alone and in complex with MRPP1 ΔMTS and MRPP2. A , domain organization for MRPP3 ΔMTS indicating the N extension (residues 50–206), PPR domain (residues 207–329, red ), core domain (residues 330–361 and 542–583, yellow ), NYN domain (residues 362–541, brown ), and structural zinc ion bound in a Cys-Cys-His-Cys motif in the core domain. B , top , analytical SEC profiles for the mixture of MRPP1 ΔMTS , MRPP2, and MRPP3 ΔMTS ( green line ) and the mixture of MRPP1 ΔMTS , MRPP2, MRPP3 ΔMTS , and pre-(mt)tRNA Ile ( black line ) applied to a Superdex S200 column. A replicate of this experiment is shown in Fig. S5 . The elution volumes for individual MRPP1 ΔMTS (from Fig. 3 A ), MRPP2 (from Fig. 3 A ), and MRPP3 ΔMTS (from Fig. S4 F ) proteins, as well as the mixture of MRPP1 ΔMTS and MRPP2 (from Fig. 3 A ), are indicated with arrows above the chromatogram ( blue , orange , red , and pink , respectively). Bottom , SDS-PAGE ( first two gel panels ) and urea-PAGE ( last two gel panels ) analysis of eluted fractions to visualize proteins and pre-(mt)tRNA Ile , respectively. The black dashed box indicates lanes where the complex containing MRPP1 ΔMTS , MRPP2, MRPP3, and pre-(mt)tRNA Ile would be found on the SDS-PAGE. C , urea-polyacrylamide denaturing gels showing the RNase P reaction of pre-(mt)tRNA Ile set up, for mixtures of MRPP2 and MRPP3 ΔMTS with different MRPP1 truncated proteins (MRPP1 ΔMTS , MRPP1 MT+C(Δ202) , MRPP1 N ). All lanes shown are taken from one experimental gel only. A downward shift in band location of processed (mt)tRNA Ile relative to that of pre-(mt)tRNA Ile and the concomitant appearance of a band corresponding to the removed 5′-leader indicate RNase P activity. D , urea-polyacrylamide denaturing gels showing the RNase P reaction of pre-(mt)tRNA Ile set up for the complex of MRPP1 ΔMTS and MRPP2 without MRPP3 ( lane 2 ) and in the presence of different truncated MRPP3 proteins ( lanes 3–6 ). A negative control of MRPP1 ΔMTS , MRPP2, and MRPP3 ΔMTS mixed with EDTA ( lane 1 ) is included. M r RNA markers are shown ( lane M ). All lanes shown are taken from one experimental gel only. Reactions in C and D were run for 30 min at protein concentrations of 300 n m MRPP1–MRPP2 and 150 n m MRPP3.

    Article Snippet: RNase P activity assay RNase P cleavage was performed by mixing 300 nm MRPP1–MRPP2, 150 nm MRPP3, 10 units of RNase inhibitors (RNasin from Promega), and 400 nm in vitro transcribed pre-(mt) tRNAIle in a buffer of 30 mm Tris-HCl, pH 8, 40 mm NaCl, 4.5 mm MgCl2 , and 2 mm DTT to a total reaction volume of 8.25 μl.

    Techniques: Size-exclusion Chromatography, SDS Page, Polyacrylamide Gel Electrophoresis, Activity Assay, Negative Control

    Ex-miRNA Are Stable and Protected from RNases in BALF (A) qPCR of synthetic miRNAs (“calibrators” Cal1 and Cal2) spiked into Trizol or BALF with or without an RNase inhibitor (RNAsin) (n = 3 from 1–2 independent experiments, 1-way ANOVA with Bonferroni’s multiple comparison test). (B) qPCR of analysis of miRNAs from BALF and RNA pellets treated with RNaseA (n = 3 from 3 independent experiments, 2-way ANOVA with Bonferroni’s multiple comparison test). Error bars are mean + SD; *p

    Journal: Cell reports

    Article Title: Increased Hematopoietic Extracellular RNAs and Vesicles in the Lung during Allergic Airway Responses

    doi: 10.1016/j.celrep.2019.01.002

    Figure Lengend Snippet: Ex-miRNA Are Stable and Protected from RNases in BALF (A) qPCR of synthetic miRNAs (“calibrators” Cal1 and Cal2) spiked into Trizol or BALF with or without an RNase inhibitor (RNAsin) (n = 3 from 1–2 independent experiments, 1-way ANOVA with Bonferroni’s multiple comparison test). (B) qPCR of analysis of miRNAs from BALF and RNA pellets treated with RNaseA (n = 3 from 3 independent experiments, 2-way ANOVA with Bonferroni’s multiple comparison test). Error bars are mean + SD; *p

    Article Snippet: To test whether synthetic miRNA-like oligoribonucleotide sequences were intrinsically stable in BALF, 22 nucleotide RNA calibrators (calibrators 1-4 ( )) were spiked into BALF and incubated for 5min at 37°C with or without RNAsin ribonuclease inhibitor (Promega) before RNA extraction.

    Techniques: Real-time Polymerase Chain Reaction

    2′-F modified siRNA inhibits gene expression in living mice. Representative bioluminescence images of light emitted from living mice transfected, 2 d earlier, with the luciferase expression plasmids pGL3-control. Mice ( N = 4–5 mice per group) received pGL3-control alone ( A ) or were cotransfected with ( B ) 2′-OH GL3 siRNA, ( C ) 2′-OH GL3 siRNA and the RNase inhibitor, RNasin, ( D ) 2′-F GL3 siRNA, ( E ) 2′-F inverted GL2 siRNA. The mouse in panel F received a low pressure i.v. injection of 2′-F GL3 siRNA on day 1 to test if stabilized siRNAs could be taken up by the liver without hydrodynamic transfection. Mice in panels B , C , and D show significant reductions in emitted light as a result of RNA. Hydrodynamic transfection with 2′-F inverted GL2 siRNA and low pressure i.v. transfection of 2′-F GL3 siRNA did not result in significant RNAi.

    Journal: RNA

    Article Title: In vivo activity of nuclease-resistant siRNAs

    doi: 10.1261/rna.5239604

    Figure Lengend Snippet: 2′-F modified siRNA inhibits gene expression in living mice. Representative bioluminescence images of light emitted from living mice transfected, 2 d earlier, with the luciferase expression plasmids pGL3-control. Mice ( N = 4–5 mice per group) received pGL3-control alone ( A ) or were cotransfected with ( B ) 2′-OH GL3 siRNA, ( C ) 2′-OH GL3 siRNA and the RNase inhibitor, RNasin, ( D ) 2′-F GL3 siRNA, ( E ) 2′-F inverted GL2 siRNA. The mouse in panel F received a low pressure i.v. injection of 2′-F GL3 siRNA on day 1 to test if stabilized siRNAs could be taken up by the liver without hydrodynamic transfection. Mice in panels B , C , and D show significant reductions in emitted light as a result of RNA. Hydrodynamic transfection with 2′-F inverted GL2 siRNA and low pressure i.v. transfection of 2′-F GL3 siRNA did not result in significant RNAi.

    Article Snippet: Briefly, 1.8 mL of DPBS (with no MgCl2 or CaCl2 ) was mixed with 3 μg of pGL3-Control (Promega), 3 μg of pThAAT , 10 μg of indicated siRNA, and if indicated, 20 μL of recombinant RNasin (Promega).

    Techniques: Modification, Expressing, Mouse Assay, Transfection, Luciferase, Injection

    Comparison of chromatograms illustrating RNA18 cleavage by synthetic c-Jun LZ36 and full-length 40 kDa recombinant c-Jun. Reactions were performed in 20 m M Tris-HCl/80 m M KCl, pH 7.2, at 37°C. (A) c-Jun LZ36 (60 µ M ) + RNA18 (170 µ M ); reaction time, 4 h; column, 3.14 mL Nucleosil C-18 300-5 (Macherey Nagel). (B) Recombinant c-Jun (20 µ M ) + RNA18 (90 µ M ); reaction time, 48 h; column, 2.5 mL Eclipse XDB C-18 (Agilent). (C) c-Jun + RNA18 (as in B) in the presence of 1 U of the ribonuclease A inhibitor RNasin. (D) RNA18; incubation time, 48 h. Resolution of the digestion products by the two different HPLC columns required a different gradient set-up (30-mL gradient in panel A versus 13-mL gradient in panels B, C and D). The elution profiles are presented relative to the percentage of acetonitrile in the two gradients (dashed blue lines). Asterisk (*) marks the position of intact RNA18.

    Journal: PLoS ONE

    Article Title: The Leucine Zipper Domains of the Transcription Factors GCN4 and c-Jun Have Ribonuclease Activity

    doi: 10.1371/journal.pone.0010765

    Figure Lengend Snippet: Comparison of chromatograms illustrating RNA18 cleavage by synthetic c-Jun LZ36 and full-length 40 kDa recombinant c-Jun. Reactions were performed in 20 m M Tris-HCl/80 m M KCl, pH 7.2, at 37°C. (A) c-Jun LZ36 (60 µ M ) + RNA18 (170 µ M ); reaction time, 4 h; column, 3.14 mL Nucleosil C-18 300-5 (Macherey Nagel). (B) Recombinant c-Jun (20 µ M ) + RNA18 (90 µ M ); reaction time, 48 h; column, 2.5 mL Eclipse XDB C-18 (Agilent). (C) c-Jun + RNA18 (as in B) in the presence of 1 U of the ribonuclease A inhibitor RNasin. (D) RNA18; incubation time, 48 h. Resolution of the digestion products by the two different HPLC columns required a different gradient set-up (30-mL gradient in panel A versus 13-mL gradient in panels B, C and D). The elution profiles are presented relative to the percentage of acetonitrile in the two gradients (dashed blue lines). Asterisk (*) marks the position of intact RNA18.

    Article Snippet: Ribonuclease assays of GCN4 LZ35 in presence of RNase A inhibitor Five units of the recombinant RNase A inhibitor RNasin (Promega) did not affect the RNA18-cleaving activity of 12.5 µL of a 50 µM solution of GCN4 LZ35 whereas 150 units of the inhibitor lowered the activity by approximately 60%.

    Techniques: Recombinant, Incubation, High Performance Liquid Chromatography