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Promega rnasin ribounclease inhibitor
Rnasin Ribounclease Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 77/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rnasin ribounclease inhibitor/product/Promega
Average 77 stars, based on 1 article reviews
Price from $9.99 to $1999.99
rnasin ribounclease inhibitor - by Bioz Stars, 2020-03
77/100 stars

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gotaq flexi dna polymerase

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Polymerase Chain Reaction:

Article Title: Mitochondrial dysfunction may explain the cardiomyopathy of chronic iron overload
Article Snippet: The r Tth DNA Polymerase XL (eXtra Long) designed for generating long PCR products was obtained from Applied Biosystems (Foster City, CA). .. GoTaq® Flexi DNA Polymerase and RNasin® ribounclease inhibitor were obtained from Promega (Madison WI).

Preserving:

Article Title: Mitochondrial dysfunction may explain the cardiomyopathy of chronic iron overload
Article Snippet: Iron dextran (batch 018H251711; ferric hydroxide dextran complex, elemental iron content 100 mg/ml containing 0.5% phenol as a preservation), trichloroacetic acid (TCA), Ferene S (3-(2-pyridyl)-5,6-di(2-furyl)-1,2,4-triazine-5',5"-disulfonic acid), Hanks balanced salt solution (HBSS), bovine heart cytochrome c , sodium citrate, potassium phosphate, ethyl acetate, porcine heart isocitrate dehydrogenase, β-NADH, MnCl2 , sucrose, potassium phosphate, ethylenediaminetetraacetic acid (EDTA), tris (hydroxymethyl) aminomethane, tris (hydroxymethyl) aminomethane (Tris) and the acid salt tris-HCl, ethylene glycol-bis (β-aminoethyl ether) N,N,N’,N’-tetraacetic acid (EGTA), 3-(N-morpholino)propanesulfoniic acid (MOPS) and ethyl acetate, were purchased from Sigma Chemical Co. (St. Louis, MO). .. GoTaq® Flexi DNA Polymerase and RNasin® ribounclease inhibitor were obtained from Promega (Madison WI).

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  • 83
    Promega rnase h buffer
    <t>RNase</t> H activation by LNA/DNA and 2′- O -methyl gapmers. (Top) Results of RNase H assay. Full-length VR1 mRNA was incubated with a 5-fold excess of oligonucleotides in the presence of RNase H for 7.5 min at 37°C. Substrate (S) and cleavage products (P1 + P2) were separated on a 1.5% agarose gel and stained with ethidium bromide. Lane 1, control; lane 2, DNA 1; lane 3, LNA 9; lane 4, LNA 12; lane 5, LNA 13; lane 6, LNA 14; lane 7, LNA 15; lane 8, OMe 1; Lane 9, OMe 2; lane 10, OMe 3. (Bottom) Quantitative evaluation of the gel. All values are averages and standard deviations of at least three independent experiments and were normalized.
    Rnase H Buffer, supplied by Promega, used in various techniques. Bioz Stars score: 83/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase h buffer/product/Promega
    Average 83 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    rnase h buffer - by Bioz Stars, 2020-03
    83/100 stars
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    83
    Promega human placental rnase inhibitor
    Figure 4. <t>RNase</t> activity in the presence of human placental RNase inhibitor. RNase activity of ( A ) MN-IgG-RNase and ( B ) CTX-IgG-RNase was measured in the presence of RNase inhibitor. 10 −10 M RNase incubated with up to 50-fold molar excess of RI (RNasin). ( C ) Bovine RNase was tested as control.
    Human Placental Rnase Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 83/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human placental rnase inhibitor/product/Promega
    Average 83 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    human placental rnase inhibitor - by Bioz Stars, 2020-03
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    93
    Promega rnase out
    SL RNA expression. (A) Northern blot, with arrows in the schema at the top indicating regions used as probes. A 1% denaturing agarose gel (left panels) and a 6% polyacrylamide denaturing gel (right panels) were probed with oligonucleotides specific to the SL RNA exon (upper gels) and 5S rRNA (lower gels). Lanes: 1, oocyte RNA; 2, day 4 RNA; M, molecular size marker (with sizes given in thousands on the left); ACGT, dideoxy sequencing reaction. Sizes of bands indicated by asterisks are given. Intense smearing in the upper portion of lane 1 in the right panel may be partially due to nonspecific binding of polysaccharides in addition to the specific detection of trans -spliced RNAs seen in lane 2 or the left panel. (B) <t>RNase</t> protection, with schema at the top showing the antisense probes used for full-length SL RNA (lanes 1, 2, and 3) and the 5′ end of RPL31 RNA (lanes 4, 5, and 6). Lanes: 1 and 4, yeast tRNA control; 2 and 5, oocyte total RNA; 3 and 6, day 4 total RNA; M and ACGT, as explained for panel A. Diagrams to the right of the autoradiograph indicate protected fragments corresponding to visualized bands. Minor variation in band lengths observed for full-length SL RNA likely results from slight sequence differences in the 3′-terminal region, yielding alteration over a few base pairs in the length of the protected fragments.
    Rnase Out, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase out/product/Promega
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase out - by Bioz Stars, 2020-03
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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 19 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 19 article reviews
    Price from $9.99 to $1999.99
    rnase inhibitor rnasin - by Bioz Stars, 2020-03
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    RNase H activation by LNA/DNA and 2′- O -methyl gapmers. (Top) Results of RNase H assay. Full-length VR1 mRNA was incubated with a 5-fold excess of oligonucleotides in the presence of RNase H for 7.5 min at 37°C. Substrate (S) and cleavage products (P1 + P2) were separated on a 1.5% agarose gel and stained with ethidium bromide. Lane 1, control; lane 2, DNA 1; lane 3, LNA 9; lane 4, LNA 12; lane 5, LNA 13; lane 6, LNA 14; lane 7, LNA 15; lane 8, OMe 1; Lane 9, OMe 2; lane 10, OMe 3. (Bottom) Quantitative evaluation of the gel. All values are averages and standard deviations of at least three independent experiments and were normalized.

    Journal: Nucleic Acids Research

    Article Title: Design of antisense oligonucleotides stabilized by locked nucleic acids

    doi:

    Figure Lengend Snippet: RNase H activation by LNA/DNA and 2′- O -methyl gapmers. (Top) Results of RNase H assay. Full-length VR1 mRNA was incubated with a 5-fold excess of oligonucleotides in the presence of RNase H for 7.5 min at 37°C. Substrate (S) and cleavage products (P1 + P2) were separated on a 1.5% agarose gel and stained with ethidium bromide. Lane 1, control; lane 2, DNA 1; lane 3, LNA 9; lane 4, LNA 12; lane 5, LNA 13; lane 6, LNA 14; lane 7, LNA 15; lane 8, OMe 1; Lane 9, OMe 2; lane 10, OMe 3. (Bottom) Quantitative evaluation of the gel. All values are averages and standard deviations of at least three independent experiments and were normalized.

    Article Snippet: The standard RNase H assay was performed as described previously ( ): 100 nM VR1 mRNA were incubated with a 5-fold excess of an antisense oligonucleotide in a total volume of 10 µl in RNase H buffer (40 mM Tris–HCl pH 7.2, 4 mM MgCl2 , 1 mM DTT, 150 mM NaCl and 1.25 U/µl RNasin; Promega, Madison, WI) for 7.5 min at 37°C in the presence of 0.4 U E.coli RNase H (Promega).

    Techniques: Activation Assay, Rnase H Assay, Incubation, Agarose Gel Electrophoresis, Staining

    RNase H assays with a short RNA target. Lane 1, one base ladder produced by alkaline hydrolysis; lane 2, cleavage products after incubation with RNase T1; lane 3, 18mer RNA; lanes 4 and 5, products after incubation of target RNA with all DNA antisense oligonucleotide (DNA 1) in the presence of RNase H after 10 and 30 min, respectively; lanes 6 and 7, products after incubation of target RNA with end-block LNA/DNA/LNA oligonucleotide (LNA 17) in the presence of RNase H after 10 and 30 min; lanes 8 and 9, products after incubation of target RNA with LNA/DNA mixmer (LNA 9) in the presence of RNase H after 10 and 30 min; lanes 10 and 11, products after incubation of target RNA with phosphorothioate in the presence of RNase H after 10 and 30 min. For further details see text.

    Journal: Nucleic Acids Research

    Article Title: Design of antisense oligonucleotides stabilized by locked nucleic acids

    doi:

    Figure Lengend Snippet: RNase H assays with a short RNA target. Lane 1, one base ladder produced by alkaline hydrolysis; lane 2, cleavage products after incubation with RNase T1; lane 3, 18mer RNA; lanes 4 and 5, products after incubation of target RNA with all DNA antisense oligonucleotide (DNA 1) in the presence of RNase H after 10 and 30 min, respectively; lanes 6 and 7, products after incubation of target RNA with end-block LNA/DNA/LNA oligonucleotide (LNA 17) in the presence of RNase H after 10 and 30 min; lanes 8 and 9, products after incubation of target RNA with LNA/DNA mixmer (LNA 9) in the presence of RNase H after 10 and 30 min; lanes 10 and 11, products after incubation of target RNA with phosphorothioate in the presence of RNase H after 10 and 30 min. For further details see text.

    Article Snippet: The standard RNase H assay was performed as described previously ( ): 100 nM VR1 mRNA were incubated with a 5-fold excess of an antisense oligonucleotide in a total volume of 10 µl in RNase H buffer (40 mM Tris–HCl pH 7.2, 4 mM MgCl2 , 1 mM DTT, 150 mM NaCl and 1.25 U/µl RNasin; Promega, Madison, WI) for 7.5 min at 37°C in the presence of 0.4 U E.coli RNase H (Promega).

    Techniques: Produced, Incubation, Blocking Assay

    Figure 4. RNase activity in the presence of human placental RNase inhibitor. RNase activity of ( A ) MN-IgG-RNase and ( B ) CTX-IgG-RNase was measured in the presence of RNase inhibitor. 10 −10 M RNase incubated with up to 50-fold molar excess of RI (RNasin). ( C ) Bovine RNase was tested as control.

    Journal: mAbs

    Article Title: Evaluation of human pancreatic RNase as effector molecule in a therapeutic antibody platform

    doi: 10.4161/mabs.27830

    Figure Lengend Snippet: Figure 4. RNase activity in the presence of human placental RNase inhibitor. RNase activity of ( A ) MN-IgG-RNase and ( B ) CTX-IgG-RNase was measured in the presence of RNase inhibitor. 10 −10 M RNase incubated with up to 50-fold molar excess of RI (RNasin). ( C ) Bovine RNase was tested as control.

    Article Snippet: In addition, RNase activity of MN-IgG-RNase was also tested in the presence of a concentration series of up to 50 fold molar excess of human placental RNase inhibitor (RNasin Plus, Promega).

    Techniques: Activity Assay, Incubation

    SL RNA expression. (A) Northern blot, with arrows in the schema at the top indicating regions used as probes. A 1% denaturing agarose gel (left panels) and a 6% polyacrylamide denaturing gel (right panels) were probed with oligonucleotides specific to the SL RNA exon (upper gels) and 5S rRNA (lower gels). Lanes: 1, oocyte RNA; 2, day 4 RNA; M, molecular size marker (with sizes given in thousands on the left); ACGT, dideoxy sequencing reaction. Sizes of bands indicated by asterisks are given. Intense smearing in the upper portion of lane 1 in the right panel may be partially due to nonspecific binding of polysaccharides in addition to the specific detection of trans -spliced RNAs seen in lane 2 or the left panel. (B) RNase protection, with schema at the top showing the antisense probes used for full-length SL RNA (lanes 1, 2, and 3) and the 5′ end of RPL31 RNA (lanes 4, 5, and 6). Lanes: 1 and 4, yeast tRNA control; 2 and 5, oocyte total RNA; 3 and 6, day 4 total RNA; M and ACGT, as explained for panel A. Diagrams to the right of the autoradiograph indicate protected fragments corresponding to visualized bands. Minor variation in band lengths observed for full-length SL RNA likely results from slight sequence differences in the 3′-terminal region, yielding alteration over a few base pairs in the length of the protected fragments.

    Journal: Molecular and Cellular Biology

    Article Title: Spliced-Leader RNA trans Splicing in a Chordate, Oikopleura dioica, with a Compact Genome †

    doi: 10.1128/MCB.24.17.7795-7805.2004

    Figure Lengend Snippet: SL RNA expression. (A) Northern blot, with arrows in the schema at the top indicating regions used as probes. A 1% denaturing agarose gel (left panels) and a 6% polyacrylamide denaturing gel (right panels) were probed with oligonucleotides specific to the SL RNA exon (upper gels) and 5S rRNA (lower gels). Lanes: 1, oocyte RNA; 2, day 4 RNA; M, molecular size marker (with sizes given in thousands on the left); ACGT, dideoxy sequencing reaction. Sizes of bands indicated by asterisks are given. Intense smearing in the upper portion of lane 1 in the right panel may be partially due to nonspecific binding of polysaccharides in addition to the specific detection of trans -spliced RNAs seen in lane 2 or the left panel. (B) RNase protection, with schema at the top showing the antisense probes used for full-length SL RNA (lanes 1, 2, and 3) and the 5′ end of RPL31 RNA (lanes 4, 5, and 6). Lanes: 1 and 4, yeast tRNA control; 2 and 5, oocyte total RNA; 3 and 6, day 4 total RNA; M and ACGT, as explained for panel A. Diagrams to the right of the autoradiograph indicate protected fragments corresponding to visualized bands. Minor variation in band lengths observed for full-length SL RNA likely results from slight sequence differences in the 3′-terminal region, yielding alteration over a few base pairs in the length of the protected fragments.

    Article Snippet: Unfertilized oocytes (1,000) were rinsed once in 40 mM Tris (pH 7.4)-400 mM NaCl and then crushed on ice in NET-2 supplemented with a protease inhibitor cocktail (Sigma), RNase-out (Promega), and protein G-Sepharose.

    Techniques: RNA Expression, Northern Blot, Agarose Gel Electrophoresis, Marker, Sequencing, Binding Assay, Autoradiography

    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