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  • 99
    Thermo Fisher dnase free rnase
    Northern analysis and <t>RNase</t> H and <t>DNase</t> I sensitivity of R-loops within mtDNA coding regions. Mitochondrial RNA remains bound to CsCl-purified mtDNA. Samples were prepared as described in the legend for Fig. 2 and treated with nucleases as indicated by (+) and (-). pA is poly(A)+-purified RNA. Gene-specific riboprobes were generated from PCR products as described under “Experimental Procedures.”
    Dnase Free Rnase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 400 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore dnase free rnase a
    In vivo interaction of Hrp59 and Hrp65. (A) RNA-mediated association of Hrp59 and Hrp65. Protein complexes were immunoprecipitated from native nuclear extracts of C. tentans tissue culture cells using mAb 4E9 against Hrp65. Mock IPs were performed in parallel in the absence of primary antibody (lanes 4 and 8). The immunoprecipitated material bound to Sepharose was incubated with or without <t>RNase</t> A and washed in order to remove RNase-released material. Proteins still bound after RNase digestion were analyzed by SDS-PAGE and Western blotting with antibodies against either Hrp59 (lanes 1–4) or Hrp65 (lanes 5–8). Nuclear extract was loaded as input (lanes 1 and 5). (B) Native coIP followed by <t>DNase</t> I digestion. The experiment was performed as in A and the bound proteins were incubated with (lane 3) or without (lane 2) DNase I and washed in order to remove DNase-released material. Nuclear extract was loaded as input (lane 1). (C) Direct interaction of Hrp59 and Hrp65: coimmunoprecipitation after in vivo cross-linking. C. tentans tissue culture cells were treated with (lanes 2 and 5) or without (lanes 3 and 6) DSP. Nuclear extracts were prepared in 8 M urea and used for IP with mAb 4E9 against hrp65 (lanes 2 and 3, and 5 and 6). Bound proteins were analyzed by SDS-PAGE and Western blotting with antibodies against either Hrp59 (lanes 1–3) or U2B′′ as a negative control (lanes 4–6). Nuclear extract from DSP-treated cells was loaded as input (lanes 1 and 4). HC and LC indicate cross-reactivity of the secondary antibodies used for Western blotting with the heavy and light chains, respectively, of the rabbit anti–mouse immunoglobulin used for IP.
    Dnase Free Rnase A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1446 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1446 article reviews
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    99
    Qiagen rnasefree dnase
    Enzymatic digestion of decellularized ECM scaffolds releases small RNA molecules. ( A ) Nucleic acid extracted from untreated UBM (no digest) and pepsin-, proteinase K–, or collagenase-treated UBM was exposed to <t>RNase</t> A, <t>DNase</t> I, or no-nuclease treatment (control). ( B ) Electropherogram depicting the small RNA pattern of nucleic acid in fluorescence units (FU) before (top panel) and after (bottom panel) DNase I treatment. ( C ) Electropherogram depicting small RNA pattern from the indicated samples in FU. ( D ) A subset of nucleic molecules in biologic scaffolds is protected from nuclease degradation.
    Rnasefree Dnase, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega rq1 rnasefree dnase
    Enzymatic digestion of decellularized ECM scaffolds releases small RNA molecules. ( A ) Nucleic acid extracted from untreated UBM (no digest) and pepsin-, proteinase K–, or collagenase-treated UBM was exposed to <t>RNase</t> A, <t>DNase</t> I, or no-nuclease treatment (control). ( B ) Electropherogram depicting the small RNA pattern of nucleic acid in fluorescence units (FU) before (top panel) and after (bottom panel) DNase I treatment. ( C ) Electropherogram depicting small RNA pattern from the indicated samples in FU. ( D ) A subset of nucleic molecules in biologic scaffolds is protected from nuclease degradation.
    Rq1 Rnasefree Dnase, 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
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    Millipore rnase free dnase
    DAPI-positivity of tau deposits is not affected by <t>RNase</t> A and/or <t>DNase</t> I treatments. (A and E) DNase I (–)/RNase A (–); (B and F) DNase I (+)/RNase A (–); (C and G) DNase I (–)/RNase A (+); (D and H) DNase I (+)/RNase A (+). (A–D) All sections were double-stained with ThS (green) and DAPI (blue). (E–H) All sections were stained with DAPI (blue) alone. Calibration bars = 10 µm. Abbreviations: DAPI, 4′,6-diamidino-2-phenylindole; ThS, thioflavin-S.
    Rnase Free Dnase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 584 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher rnase free dnase
    miC Variants Inhibit RNA Foci Formation in (G 4 C 2 ) 44 -Expressing Cells (A) RNA foci detected in HEK293T cells expressing (G 4 C 2 ) 44 . Cells were transfected with 250 ng (G 4 C 2 ) 44 and (G 4 C 2 ) 3 plasmid and fixed 2 days post-transfection after treatment with <t>DNase</t> or <t>RNase.</t> RNA FISH was performed using a TYE563-(CCCCGG) 3 LNA probe (red), and nuclei were stained with DAPI (blue). Nuclear foci were resistant to DNase but degraded by RNase indicating RNA foci. (B) Reduction of RNA foci by miC4_101 and miC32_101. Cells were co-transfected with 250 ng (G 4 C 2 ) 44 and 100 ng miC4_101, miC32_101, or miScr plasmid. Cells were fixed 2 days post-transfection, and RNA FISH was performed as described in (A). (C) Quantification of RNA foci in miC4_101- and miC32_101-transfected cells. A series of five images was made using 10× magnification to quantify the number of cells containing nuclear foci using ImageJ (mean ± SD, one-way ANOVA, multiple-comparison test, ***p
    Rnase Free Dnase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 7991 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase free dnase/product/Thermo Fisher
    Average 99 stars, based on 7991 article reviews
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    rnase free dnase - by Bioz Stars, 2020-07
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    Image Search Results


    Northern analysis and RNase H and DNase I sensitivity of R-loops within mtDNA coding regions. Mitochondrial RNA remains bound to CsCl-purified mtDNA. Samples were prepared as described in the legend for Fig. 2 and treated with nucleases as indicated by (+) and (-). pA is poly(A)+-purified RNA. Gene-specific riboprobes were generated from PCR products as described under “Experimental Procedures.”

    Journal: The Journal of Biological Chemistry

    Article Title: Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome *Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome * S⃞

    doi: 10.1074/jbc.M806174200

    Figure Lengend Snippet: Northern analysis and RNase H and DNase I sensitivity of R-loops within mtDNA coding regions. Mitochondrial RNA remains bound to CsCl-purified mtDNA. Samples were prepared as described in the legend for Fig. 2 and treated with nucleases as indicated by (+) and (-). pA is poly(A)+-purified RNA. Gene-specific riboprobes were generated from PCR products as described under “Experimental Procedures.”

    Article Snippet: DNase-free RNase A purchased from Ambion was used at a final concentration of 0.04 ng/μl for 10 min at 37 °C.

    Techniques: Northern Blot, Purification, Generated, Polymerase Chain Reaction

    Northern analysis and DNase and RNase sensitivity of mtDNA-bound nascent H-strand RNA and DNA at O H . EtBr-CsCl-purified closed circular mtDNA was analyzed by Northern analysis to detect stable R-loops. RNA size markers are in lane 1 . Poly(A)+-purified RNA is in the lane denoted by pA +. DNase I and RNase H sample treatments are indicated above the panels. A , probing for CSB-proximal RNA with T3#4 riboprobe (shown in D ). B , less exposed film of view shown in A , revealing the increased intensity of ∼150-nt species in lane 3 after DNase treatment. C , probing for CSB-distal RNA with T3#1 riboprobe as shown in D. D , reference diagram showing the major noncoding region of mtDNA. This region is identified in Fig. 1 as the area encompassing O H . The transcription start site is shown with a bent arrow followed by several relevant DNA sequence features, including CSBs III, II, and I. The termination-associated sequences ( TAS ) region is shown at the promoter distal end of the DNA. T3#4 and T#31 riboprobe positions are shown above. Below the DNA map are nucleic acids identified in the Northern blots shown in A-C . RNA is shown by thick black lines , and RNA primers in transition with DNA are shown in gray . DNA alone is in shown by thin black lines . The lines are to scale, with size interruptions shown by breaks .

    Journal: The Journal of Biological Chemistry

    Article Title: Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome *Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome * S⃞

    doi: 10.1074/jbc.M806174200

    Figure Lengend Snippet: Northern analysis and DNase and RNase sensitivity of mtDNA-bound nascent H-strand RNA and DNA at O H . EtBr-CsCl-purified closed circular mtDNA was analyzed by Northern analysis to detect stable R-loops. RNA size markers are in lane 1 . Poly(A)+-purified RNA is in the lane denoted by pA +. DNase I and RNase H sample treatments are indicated above the panels. A , probing for CSB-proximal RNA with T3#4 riboprobe (shown in D ). B , less exposed film of view shown in A , revealing the increased intensity of ∼150-nt species in lane 3 after DNase treatment. C , probing for CSB-distal RNA with T3#1 riboprobe as shown in D. D , reference diagram showing the major noncoding region of mtDNA. This region is identified in Fig. 1 as the area encompassing O H . The transcription start site is shown with a bent arrow followed by several relevant DNA sequence features, including CSBs III, II, and I. The termination-associated sequences ( TAS ) region is shown at the promoter distal end of the DNA. T3#4 and T#31 riboprobe positions are shown above. Below the DNA map are nucleic acids identified in the Northern blots shown in A-C . RNA is shown by thick black lines , and RNA primers in transition with DNA are shown in gray . DNA alone is in shown by thin black lines . The lines are to scale, with size interruptions shown by breaks .

    Article Snippet: DNase-free RNase A purchased from Ambion was used at a final concentration of 0.04 ng/μl for 10 min at 37 °C.

    Techniques: Northern Blot, Purification, Sequencing

    In vivo interaction of Hrp59 and Hrp65. (A) RNA-mediated association of Hrp59 and Hrp65. Protein complexes were immunoprecipitated from native nuclear extracts of C. tentans tissue culture cells using mAb 4E9 against Hrp65. Mock IPs were performed in parallel in the absence of primary antibody (lanes 4 and 8). The immunoprecipitated material bound to Sepharose was incubated with or without RNase A and washed in order to remove RNase-released material. Proteins still bound after RNase digestion were analyzed by SDS-PAGE and Western blotting with antibodies against either Hrp59 (lanes 1–4) or Hrp65 (lanes 5–8). Nuclear extract was loaded as input (lanes 1 and 5). (B) Native coIP followed by DNase I digestion. The experiment was performed as in A and the bound proteins were incubated with (lane 3) or without (lane 2) DNase I and washed in order to remove DNase-released material. Nuclear extract was loaded as input (lane 1). (C) Direct interaction of Hrp59 and Hrp65: coimmunoprecipitation after in vivo cross-linking. C. tentans tissue culture cells were treated with (lanes 2 and 5) or without (lanes 3 and 6) DSP. Nuclear extracts were prepared in 8 M urea and used for IP with mAb 4E9 against hrp65 (lanes 2 and 3, and 5 and 6). Bound proteins were analyzed by SDS-PAGE and Western blotting with antibodies against either Hrp59 (lanes 1–3) or U2B′′ as a negative control (lanes 4–6). Nuclear extract from DSP-treated cells was loaded as input (lanes 1 and 4). HC and LC indicate cross-reactivity of the secondary antibodies used for Western blotting with the heavy and light chains, respectively, of the rabbit anti–mouse immunoglobulin used for IP.

    Journal: The Journal of Cell Biology

    Article Title: Hrp59, an hnRNP M protein in Chironomus and Drosophila, binds to exonic splicing enhancers and is required for expression of a subset of mRNAs

    doi: 10.1083/jcb.200407173

    Figure Lengend Snippet: In vivo interaction of Hrp59 and Hrp65. (A) RNA-mediated association of Hrp59 and Hrp65. Protein complexes were immunoprecipitated from native nuclear extracts of C. tentans tissue culture cells using mAb 4E9 against Hrp65. Mock IPs were performed in parallel in the absence of primary antibody (lanes 4 and 8). The immunoprecipitated material bound to Sepharose was incubated with or without RNase A and washed in order to remove RNase-released material. Proteins still bound after RNase digestion were analyzed by SDS-PAGE and Western blotting with antibodies against either Hrp59 (lanes 1–4) or Hrp65 (lanes 5–8). Nuclear extract was loaded as input (lanes 1 and 5). (B) Native coIP followed by DNase I digestion. The experiment was performed as in A and the bound proteins were incubated with (lane 3) or without (lane 2) DNase I and washed in order to remove DNase-released material. Nuclear extract was loaded as input (lane 1). (C) Direct interaction of Hrp59 and Hrp65: coimmunoprecipitation after in vivo cross-linking. C. tentans tissue culture cells were treated with (lanes 2 and 5) or without (lanes 3 and 6) DSP. Nuclear extracts were prepared in 8 M urea and used for IP with mAb 4E9 against hrp65 (lanes 2 and 3, and 5 and 6). Bound proteins were analyzed by SDS-PAGE and Western blotting with antibodies against either Hrp59 (lanes 1–3) or U2B′′ as a negative control (lanes 4–6). Nuclear extract from DSP-treated cells was loaded as input (lanes 1 and 4). HC and LC indicate cross-reactivity of the secondary antibodies used for Western blotting with the heavy and light chains, respectively, of the rabbit anti–mouse immunoglobulin used for IP.

    Article Snippet: RNase treatment of C. tentans salivary glands Salivary glands were dissected and preextracted as for BrUTP incorporation, washed in TBS and incubated for 30 min with 0.1 mg/ml DNase-free RNase A (Sigma-Aldrich) in TBS, or with TBS alone.

    Techniques: In Vivo, Immunoprecipitation, Incubation, SDS Page, Western Blot, Co-Immunoprecipitation Assay, Negative Control

    Enzymatic digestion of decellularized ECM scaffolds releases small RNA molecules. ( A ) Nucleic acid extracted from untreated UBM (no digest) and pepsin-, proteinase K–, or collagenase-treated UBM was exposed to RNase A, DNase I, or no-nuclease treatment (control). ( B ) Electropherogram depicting the small RNA pattern of nucleic acid in fluorescence units (FU) before (top panel) and after (bottom panel) DNase I treatment. ( C ) Electropherogram depicting small RNA pattern from the indicated samples in FU. ( D ) A subset of nucleic molecules in biologic scaffolds is protected from nuclease degradation.

    Journal: Science Advances

    Article Title: Matrix-bound nanovesicles within ECM bioscaffolds

    doi: 10.1126/sciadv.1600502

    Figure Lengend Snippet: Enzymatic digestion of decellularized ECM scaffolds releases small RNA molecules. ( A ) Nucleic acid extracted from untreated UBM (no digest) and pepsin-, proteinase K–, or collagenase-treated UBM was exposed to RNase A, DNase I, or no-nuclease treatment (control). ( B ) Electropherogram depicting the small RNA pattern of nucleic acid in fluorescence units (FU) before (top panel) and after (bottom panel) DNase I treatment. ( C ) Electropherogram depicting small RNA pattern from the indicated samples in FU. ( D ) A subset of nucleic molecules in biologic scaffolds is protected from nuclease degradation.

    Article Snippet: RNase-free DNase was obtained from Qiagen.

    Techniques: Fluorescence

    DAPI-positivity of tau deposits is not affected by RNase A and/or DNase I treatments. (A and E) DNase I (–)/RNase A (–); (B and F) DNase I (+)/RNase A (–); (C and G) DNase I (–)/RNase A (+); (D and H) DNase I (+)/RNase A (+). (A–D) All sections were double-stained with ThS (green) and DAPI (blue). (E–H) All sections were stained with DAPI (blue) alone. Calibration bars = 10 µm. Abbreviations: DAPI, 4′,6-diamidino-2-phenylindole; ThS, thioflavin-S.

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: 4′,6-Diamidino-2-Phenylindole Distinctly Labels Tau Deposits

    doi: 10.1369/0022155418793600

    Figure Lengend Snippet: DAPI-positivity of tau deposits is not affected by RNase A and/or DNase I treatments. (A and E) DNase I (–)/RNase A (–); (B and F) DNase I (+)/RNase A (–); (C and G) DNase I (–)/RNase A (+); (D and H) DNase I (+)/RNase A (+). (A–D) All sections were double-stained with ThS (green) and DAPI (blue). (E–H) All sections were stained with DAPI (blue) alone. Calibration bars = 10 µm. Abbreviations: DAPI, 4′,6-diamidino-2-phenylindole; ThS, thioflavin-S.

    Article Snippet: To investigate the nuclease effect, the deparaffinized sections were incubated in RNase-free DNase I solution (400 U/ml, Sigma-Aldrich), DNase-free RNase A solution (200 μg/ml, Sigma-Aldrich), or a combination of DNase I and RNase A for 3.5 hr, and the efficacy of nucleic acid elimination was validated by staining with 2 μg/ml DAPI and 10 μg/ml ethidium bromide (EtBr; Nippon Gene, Tokyo, Japan).

    Techniques: Staining

    miC Variants Inhibit RNA Foci Formation in (G 4 C 2 ) 44 -Expressing Cells (A) RNA foci detected in HEK293T cells expressing (G 4 C 2 ) 44 . Cells were transfected with 250 ng (G 4 C 2 ) 44 and (G 4 C 2 ) 3 plasmid and fixed 2 days post-transfection after treatment with DNase or RNase. RNA FISH was performed using a TYE563-(CCCCGG) 3 LNA probe (red), and nuclei were stained with DAPI (blue). Nuclear foci were resistant to DNase but degraded by RNase indicating RNA foci. (B) Reduction of RNA foci by miC4_101 and miC32_101. Cells were co-transfected with 250 ng (G 4 C 2 ) 44 and 100 ng miC4_101, miC32_101, or miScr plasmid. Cells were fixed 2 days post-transfection, and RNA FISH was performed as described in (A). (C) Quantification of RNA foci in miC4_101- and miC32_101-transfected cells. A series of five images was made using 10× magnification to quantify the number of cells containing nuclear foci using ImageJ (mean ± SD, one-way ANOVA, multiple-comparison test, ***p

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: Artificial MicroRNAs Targeting C9orf72 Can Reduce Accumulation of Intra-nuclear Transcripts in ALS and FTD Patients

    doi: 10.1016/j.omtn.2019.01.010

    Figure Lengend Snippet: miC Variants Inhibit RNA Foci Formation in (G 4 C 2 ) 44 -Expressing Cells (A) RNA foci detected in HEK293T cells expressing (G 4 C 2 ) 44 . Cells were transfected with 250 ng (G 4 C 2 ) 44 and (G 4 C 2 ) 3 plasmid and fixed 2 days post-transfection after treatment with DNase or RNase. RNA FISH was performed using a TYE563-(CCCCGG) 3 LNA probe (red), and nuclei were stained with DAPI (blue). Nuclear foci were resistant to DNase but degraded by RNase indicating RNA foci. (B) Reduction of RNA foci by miC4_101 and miC32_101. Cells were co-transfected with 250 ng (G 4 C 2 ) 44 and 100 ng miC4_101, miC32_101, or miScr plasmid. Cells were fixed 2 days post-transfection, and RNA FISH was performed as described in (A). (C) Quantification of RNA foci in miC4_101- and miC32_101-transfected cells. A series of five images was made using 10× magnification to quantify the number of cells containing nuclear foci using ImageJ (mean ± SD, one-way ANOVA, multiple-comparison test, ***p

    Article Snippet: Optionally, cells were treated for 30 min with 5 mg/mL RNase A (QIAGEN) or 100 U RNase-free DNase (Invitrogen).

    Techniques: Expressing, Transfection, Plasmid Preparation, Fluorescence In Situ Hybridization, Staining