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Promega rnasin ribonulcease inhibitor
Rnasin Ribonulcease Inhibitor, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rnasin ribonulcease inhibitor/product/Promega
Average 92 stars, based on 1 article reviews
Price from $9.99 to $1999.99
rnasin ribonulcease inhibitor - by Bioz Stars, 2020-04
92/100 stars

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Related Articles

Real-time Polymerase Chain Reaction:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT. .. The synthesized cDNA was aliquoted into small volumes and stored at -84°C, and subsequently amplified in a qPCR reaction (CFX Connect; Bio-Rad Laboratories, Hercules, CA).

RNA Extraction:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Finally, prior to RNA extraction, the tissue pellets were dissociated with 200 μl of proteinase K by incubating at 56°C for 1 h. Total tissue RNA was extracted with Trizol Reagent (Invitrogen; Austin, TX) per the manufacturer’s instructions. .. Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT.

Amplification:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT. .. The synthesized cDNA was aliquoted into small volumes and stored at -84°C, and subsequently amplified in a qPCR reaction (CFX Connect; Bio-Rad Laboratories, Hercules, CA).

Synthesized:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT. .. The synthesized cDNA was aliquoted into small volumes and stored at -84°C, and subsequently amplified in a qPCR reaction (CFX Connect; Bio-Rad Laboratories, Hercules, CA).

Isolation:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: After DNase treatment, the purity and quantity of RNA isolated from the samples were determined using an Agilent Bioanalyzer (Agilent Technologies, Inc., Santa Clara, CA). .. Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT.

Quantitative RT-PCR:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Paragraph title: Quantification of Desmin Gene Transcripts in Muscle Homogenates by RT-qPCR ... Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT.

SYBR Green Assay:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT. .. For qPCR, 10% of the cDNA was used with the desmin or myosin primer pairs (below) at 100 pmol each in DyNAmo SYBR Green qPCR reaction mix (Fisher Scientific; Pittsburgh PA) according to the manufacturer’s instructions.

Incubation:

Article Title: Abnormal Accumulation of Desmin in Gastrocnemius Myofibers of Patients with Peripheral Artery Disease
Article Snippet: Approximately 200 ng per sample was used for the synthesis of cDNA in a 20 μl reaction volume containing RNA, random hexamers (Promega; Madison, WI), 0.5 mM dNTPs, 1 U RNAsin Ribonulcease Inhibitor (Promega) and 1 U Improm-II Reverse Transcriptase (Promega) in a buffer containing 50 mM Tris-HCl, pH 8.3, 75 mM KCl, 3 mM MgCl2 , and 2 mM DTT. .. RT reactions were incubated at 42°C for 1 h, followed by inactivation at 75°C for 15 min. After a brief chilling on ice, RNase H (Promega) was added to remove RNA strands from RT reactions, which subsequently were diluted 5-fold with nuclease-free water.

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  • 91
    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: 91/100, 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 91 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    rnase h buffer - by Bioz Stars, 2020-04
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    87
    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: 87/100, 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 87 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    human placental rnase inhibitor - by Bioz Stars, 2020-04
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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, 2020-04
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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, 2020-04
    99/100 stars
      Buy from Supplier

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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