dnase i Thermo Fisher Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    New England Biolabs dnase
    Dnase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 922 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase/product/New England Biolabs
    Average 95 stars, based on 922 article reviews
    Price from $9.99 to $1999.99
    dnase - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    95
    Millipore dnase i
    Dnase I, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 26477 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i/product/Millipore
    Average 95 stars, based on 26477 article reviews
    Price from $9.99 to $1999.99
    dnase i - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    90
    Thermo Fisher dnase i
    TUNEL staining in necrotic spots . Transmitted light images  (A,E,I,M) , sytox orange nuclear staining  (B,F,J,N)  and TUNEL staining  (C,G,K,O)  on cross-sections of 5-week-old wild-type  (A–D) , and  sns-D  leaves  (I–L) . As positive controls, DNase I-treated cross-sections of wild-type  (E–H)  and  sns-D  leaf  (M–P)  are shown.  (D,H,L,P)  are merged images of  (B)  with  (C), (F)  with  (G), (J)  with  (K), (N)  with  (O) , respectively. TUNEL-positive nuclei are indicated by arrows. The bar is 25 μm.
    Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 56681 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i/product/Thermo Fisher
    Average 90 stars, based on 56681 article reviews
    Price from $9.99 to $1999.99
    dnase i - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    78
    Thermo Fisher a594 dnaase i
    TUNEL staining in necrotic spots . Transmitted light images  (A,E,I,M) , sytox orange nuclear staining  (B,F,J,N)  and TUNEL staining  (C,G,K,O)  on cross-sections of 5-week-old wild-type  (A–D) , and  sns-D  leaves  (I–L) . As positive controls, DNase I-treated cross-sections of wild-type  (E–H)  and  sns-D  leaf  (M–P)  are shown.  (D,H,L,P)  are merged images of  (B)  with  (C), (F)  with  (G), (J)  with  (K), (N)  with  (O) , respectively. TUNEL-positive nuclei are indicated by arrows. The bar is 25 μm.
    A594 Dnaase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/a594 dnaase i/product/Thermo Fisher
    Average 78 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    a594 dnaase i - by Bioz Stars, 2020-02
    78/100 stars
      Buy from Supplier

    90
    Thermo Fisher dnase
    TERRA accumulation requires HSF1 upon heat shock. ( A ) Western blot analysis of HSF1 WT and KD unstressed and stressed cells. Tubulin is shown as a loading control. ( B ) Dot blot analysis of TERRA. Total <t>RNA</t> was extracted from WT and HSF1 KD cells before and after HS and treated with <t>DNAse.</t> Various amount of total RNA fractions were subjected to RNA dot blot analysis using a radiolabelled TERRA probe. RNA were treated with RNase in parallel.The same blot was also hybridized after staining with a control probe specific for U2 transcripts. ( C ) Quantification of TERRA and U2 levels in WT and HSF1 KD cells before and after HS normalized with 37°C conditions. Standard deviation (SD) was calculated from 3 independent experiments. P -value = 0.0213 ( D ) Representative confocal images of FISH analyses of TERRA expression in WT and HSF1 KD cells before and after HS. RNase treatment induces an elimination of TERRA signal. Scale bar: 10 μm. ( E ) 3D quantification analysis of mean TERRA foci volume in the different conditions tested by RNA FISH using volocity software. The P -values calculated by unpaired Student's t -test with Welch's corrections at 37°C and at 43°C for WT and HSF1 KD cells are respectively P
    Dnase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 15731 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase/product/Thermo Fisher
    Average 90 stars, based on 15731 article reviews
    Price from $9.99 to $1999.99
    dnase - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    97
    Thermo Fisher dnaase i treatment
    TERRA accumulation requires HSF1 upon heat shock. ( A ) Western blot analysis of HSF1 WT and KD unstressed and stressed cells. Tubulin is shown as a loading control. ( B ) Dot blot analysis of TERRA. Total <t>RNA</t> was extracted from WT and HSF1 KD cells before and after HS and treated with <t>DNAse.</t> Various amount of total RNA fractions were subjected to RNA dot blot analysis using a radiolabelled TERRA probe. RNA were treated with RNase in parallel.The same blot was also hybridized after staining with a control probe specific for U2 transcripts. ( C ) Quantification of TERRA and U2 levels in WT and HSF1 KD cells before and after HS normalized with 37°C conditions. Standard deviation (SD) was calculated from 3 independent experiments. P -value = 0.0213 ( D ) Representative confocal images of FISH analyses of TERRA expression in WT and HSF1 KD cells before and after HS. RNase treatment induces an elimination of TERRA signal. Scale bar: 10 μm. ( E ) 3D quantification analysis of mean TERRA foci volume in the different conditions tested by RNA FISH using volocity software. The P -values calculated by unpaired Student's t -test with Welch's corrections at 37°C and at 43°C for WT and HSF1 KD cells are respectively P
    Dnaase I Treatment, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 64 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnaase i treatment/product/Thermo Fisher
    Average 97 stars, based on 64 article reviews
    Price from $9.99 to $1999.99
    dnaase i treatment - by Bioz Stars, 2020-02
    97/100 stars
      Buy from Supplier

    90
    Thermo Fisher anti dnase x
    Both EndoG and bleomycin induce DNase I and <t>DNase</t> X transcription in isolated rat brain cell nuclei. (A, B) In vitro transcription of DNase I and DNase X genes in isolated rat brain nuclei exposed with varying concentrations of recombinant EndoG (recEndoG)
    Anti Dnase X, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti dnase x/product/Thermo Fisher
    Average 90 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    anti dnase x - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    90
    Thermo Fisher amplification grade dnase i
    Transfection of total RNA harvested from poly(dA–dT) transfected cells results in IFN- β expression. 293T cells were transfected with 12 μg total RNA extracted from 293T cells that had been transfected with 12 μg poly(dA–dT) for 24 h. Induction of IFN- β mRNA was confirmed to be specific for an immunostimulatory RNA species by treating total RNA with either (a) 0.1 mg RNase A ml −1 or (b) 0.1 U amplification grade <t>DNase</t> I μl −1 . Total RNA was then extracted 24 h post-transfection and real-time qPCR performed for IFN- β . These data were normalized against GAPDH mRNA levels. Error bars indicate the mean± sem (* P
    Amplification Grade Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 2382 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/amplification grade dnase i/product/Thermo Fisher
    Average 90 stars, based on 2382 article reviews
    Price from $9.99 to $1999.99
    amplification grade dnase i - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    90
    Thermo Fisher dnase i buffer
    <t>DNase</t> I treatment is effective against C. jejuni biofilms on stainless steel surfaces and in the presence of organic materials in aerobic conditions . The ability of DNase I to inhibit biofilm formation of C. jejuni NCTC 11168 on sterile, stainless steel coupons (A) or in the presence of chicken juice, mimicking a conditioned surface (B) . TTC staining was used to measure biofilm formation in the presence of chicken juice (B) . DNase I is able to significantly decrease biofilm formation in both conditions. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P
    Dnase I Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 444 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i buffer/product/Thermo Fisher
    Average 90 stars, based on 444 article reviews
    Price from $9.99 to $1999.99
    dnase i buffer - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    90
    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: 90/100, based on 6521 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase free dnase/product/Thermo Fisher
    Average 90 stars, based on 6521 article reviews
    Price from $9.99 to $1999.99
    rnase free dnase - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    95
    Thermo Fisher turbo dnase i
    Viral gene transcription of BAC36 and BAC-stop45 viruses after a de novo infection. HFF were infected with BAC36 and BAC-stop45 viruses (50 genome copies per cell). Six hours after infection, total RNAs were extracted, treated with DNase I, and reverse
    Turbo Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 110 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/turbo dnase i/product/Thermo Fisher
    Average 95 stars, based on 110 article reviews
    Price from $9.99 to $1999.99
    turbo dnase i - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    79
    Thermo Fisher dnase i inhibitor
    Viral gene transcription of BAC36 and BAC-stop45 viruses after a de novo infection. HFF were infected with BAC36 and BAC-stop45 viruses (50 genome copies per cell). Six hours after infection, total RNAs were extracted, treated with DNase I, and reverse
    Dnase I Inhibitor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i inhibitor/product/Thermo Fisher
    Average 79 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    dnase i inhibitor - by Bioz Stars, 2020-02
    79/100 stars
      Buy from Supplier

    89
    Thermo Fisher ambion dnase i
    <t>DNase</t> I footprinting analysis of PdxR binding to the mutant pdxRS regulatory regions pdxRSp1 (A), pdxRSp2 (B, D), and pdxRSp4 (C, D) <t>DNA</t> fragments, radioactively labeled on the bottom (A, B, C) or top (D) strand, were incubated with increasing concentrations of purified PdxR and in the absence or presence of 100 μM PLP. PdxR monomer concentrations used (nM) are indicated below each lane. The corresponding A + G sequencing ladder is shown in the left and right lanes. The protected areas are indicated by vertical lines.
    Ambion Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ambion dnase i/product/Thermo Fisher
    Average 89 stars, based on 32 article reviews
    Price from $9.99 to $1999.99
    ambion dnase i - by Bioz Stars, 2020-02
    89/100 stars
      Buy from Supplier

    89
    MACHEREY NAGEL dnase i digestion
    <t>DNase</t> I footprinting analysis of PdxR binding to the mutant pdxRS regulatory regions pdxRSp1 (A), pdxRSp2 (B, D), and pdxRSp4 (C, D) <t>DNA</t> fragments, radioactively labeled on the bottom (A, B, C) or top (D) strand, were incubated with increasing concentrations of purified PdxR and in the absence or presence of 100 μM PLP. PdxR monomer concentrations used (nM) are indicated below each lane. The corresponding A + G sequencing ladder is shown in the left and right lanes. The protected areas are indicated by vertical lines.
    Dnase I Digestion, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 89/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i digestion/product/MACHEREY NAGEL
    Average 89 stars, based on 21 article reviews
    Price from $9.99 to $1999.99
    dnase i digestion - by Bioz Stars, 2020-02
    89/100 stars
      Buy from Supplier

    78
    Thermo Fisher dnase i stock
    <t>DNase</t> I footprinting analysis of PdxR binding to the mutant pdxRS regulatory regions pdxRSp1 (A), pdxRSp2 (B, D), and pdxRSp4 (C, D) <t>DNA</t> fragments, radioactively labeled on the bottom (A, B, C) or top (D) strand, were incubated with increasing concentrations of purified PdxR and in the absence or presence of 100 μM PLP. PdxR monomer concentrations used (nM) are indicated below each lane. The corresponding A + G sequencing ladder is shown in the left and right lanes. The protected areas are indicated by vertical lines.
    Dnase I Stock, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i stock/product/Thermo Fisher
    Average 78 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    dnase i stock - by Bioz Stars, 2020-02
    78/100 stars
      Buy from Supplier

    79
    Thermo Fisher deoxyribonuclease dnase i
    <t>DNase</t> I footprinting analysis of PdxR binding to the mutant pdxRS regulatory regions pdxRSp1 (A), pdxRSp2 (B, D), and pdxRSp4 (C, D) <t>DNA</t> fragments, radioactively labeled on the bottom (A, B, C) or top (D) strand, were incubated with increasing concentrations of purified PdxR and in the absence or presence of 100 μM PLP. PdxR monomer concentrations used (nM) are indicated below each lane. The corresponding A + G sequencing ladder is shown in the left and right lanes. The protected areas are indicated by vertical lines.
    Deoxyribonuclease Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/deoxyribonuclease dnase i/product/Thermo Fisher
    Average 79 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    deoxyribonuclease dnase i - by Bioz Stars, 2020-02
    79/100 stars
      Buy from Supplier

    93
    Thermo Fisher dnase i endonuclease
    Effect of calpain-like silencing during PCD. (A) DNA fragmentation in calpain-like silenced trophozoites after PCD induction by G418. Confocal microscopy analysis of trophozoites showing the TUNEL staining, samples were counter-stained with DAPI. (A) Negative control, untreated trophozoites; (B) Positive control, trophozoites treated with 20 μg of <t>DNase</t> I endonuclease for 30 min; (C) Trophozoites after a 9-h incubation with 10 μg/ml of G418; (D,E) Trophozoites pre-incubated for 24 h with NRS (D) or calpain-like (E) siRNAs sequences and then 9 h with 10 μg/ml G418; (B) Densitometric analysis of (A). (C) Effect of calpain-like silencing on the cell viability of E. histolytica incubated with G418; (A) Negative control, untreated trophozoites; (B) Trophozoites after a 9-h incubation with 10 μg/ml of G418; (C,D) Trophozoites pre-incubated for 24 h with NRS (C) or calpain-like (D) siRNAs sequences and then 9 h with 10 μg/ml G418. *indicate statistically significant difference: P
    Dnase I Endonuclease, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i endonuclease/product/Thermo Fisher
    Average 93 stars, based on 24 article reviews
    Price from $9.99 to $1999.99
    dnase i endonuclease - by Bioz Stars, 2020-02
    93/100 stars
      Buy from Supplier

    90
    Thermo Fisher rnase dnase treatment
    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of <t>RNase/DNase</t> treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).
    Rnase Dnase Treatment, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase dnase treatment/product/Thermo Fisher
    Average 90 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    rnase dnase treatment - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    99
    Thermo Fisher recombinant dnase i
    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of <t>RNase/DNase</t> treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).
    Recombinant Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 338 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant dnase i/product/Thermo Fisher
    Average 99 stars, based on 338 article reviews
    Price from $9.99 to $1999.99
    recombinant dnase i - by Bioz Stars, 2020-02
    99/100 stars
      Buy from Supplier

    80
    Thermo Fisher dnase i ribolock ri
    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of <t>RNase/DNase</t> treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).
    Dnase I Ribolock Ri, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i ribolock ri/product/Thermo Fisher
    Average 80 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    dnase i ribolock ri - by Bioz Stars, 2020-02
    80/100 stars
      Buy from Supplier

    84
    Thermo Fisher m v dnase i
    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of <t>RNase/DNase</t> treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).
    M V Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m v dnase i/product/Thermo Fisher
    Average 84 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    m v dnase i - by Bioz Stars, 2020-02
    84/100 stars
      Buy from Supplier

    89
    Thermo Fisher turbo dnase i kit
    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of <t>RNase/DNase</t> treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).
    Turbo Dnase I Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/turbo dnase i kit/product/Thermo Fisher
    Average 89 stars, based on 37 article reviews
    Price from $9.99 to $1999.99
    turbo dnase i kit - by Bioz Stars, 2020-02
    89/100 stars
      Buy from Supplier

    79
    Thermo Fisher dnase i amplification kit
    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of <t>RNase/DNase</t> treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).
    Dnase I Amplification Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i amplification kit/product/Thermo Fisher
    Average 79 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    dnase i amplification kit - by Bioz Stars, 2020-02
    79/100 stars
      Buy from Supplier

    90
    Thermo Fisher human dnase i
    Enzymatic resistance of phosphorothioate-modified Au-TDNNs. (A, B) Fluorescence time graph depicting terminal-modified Au-TDNN and overall-modified Au-TDNN degradation by DNase I. (C, D) Fluorescence time graph depicting terminal-modified Au-TDNN and overall-modified Au-TDNN degradation by Exo III.
    Human Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human dnase i/product/Thermo Fisher
    Average 90 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    human dnase i - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    79
    Thermo Fisher dnase i fitc
    The spatial distribution of actin in RBC ghosts revealed by fluorescent probes of phalloidin-rhodamine and DNase <t>I–FITC.</t> The spatial distribution of the fluorescent probes was analyzed via a three-dimensional optical sectioning by a confocal inverted laser scanning microscope. ( A ) Optical sections ( a–h , 0.6 μm apart) of RBC ghost labeled by phalloidin-rhodamine (4.4 μM). Each square of the gallery of images possesses a dimension of 9.5 μm × 9.5 μm. ( B ) The distribution of phalloidin-rhodamine and DNase I–FITC in RBC ghosts in an optical section taken at the middle (half thickness) of the RBC ghost. Inset , The separate distribution of phalloidin-rhodamine ( red ) and <t>DNase</t> I ( green ) in a RBC ghost that was labeled with both phalloidin-rhodamine and DNase I–FITC. Bars: ( A ) 5 μm; ( B ) 10 μm.
    Dnase I Fitc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i fitc/product/Thermo Fisher
    Average 79 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    dnase i fitc - by Bioz Stars, 2020-02
    79/100 stars
      Buy from Supplier

    84
    Thermo Fisher bovine dnase i
    The spatial distribution of actin in RBC ghosts revealed by fluorescent probes of phalloidin-rhodamine and DNase <t>I–FITC.</t> The spatial distribution of the fluorescent probes was analyzed via a three-dimensional optical sectioning by a confocal inverted laser scanning microscope. ( A ) Optical sections ( a–h , 0.6 μm apart) of RBC ghost labeled by phalloidin-rhodamine (4.4 μM). Each square of the gallery of images possesses a dimension of 9.5 μm × 9.5 μm. ( B ) The distribution of phalloidin-rhodamine and DNase I–FITC in RBC ghosts in an optical section taken at the middle (half thickness) of the RBC ghost. Inset , The separate distribution of phalloidin-rhodamine ( red ) and <t>DNase</t> I ( green ) in a RBC ghost that was labeled with both phalloidin-rhodamine and DNase I–FITC. Bars: ( A ) 5 μm; ( B ) 10 μm.
    Bovine Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine dnase i/product/Thermo Fisher
    Average 84 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    bovine dnase i - by Bioz Stars, 2020-02
    84/100 stars
      Buy from Supplier

    97
    Fisher Scientific dnase i
    ChIP analysis indicates that ethanol exposure increases BRG1 binding to DNAse I-resistant/CpG island containing region 3 and the pre-miR-9-2 coding exon Bar graph shows the effect of ethanol on BRG1-association with regions 1 to 5 and the pre-miR-9-2 exon-coding region of the primary (pri)-miR-9-2 coding locus. Primers for a gene desert on chromosome 6 (not predicted to bind any transcription factors) shows the specificity of the immuno-precipitation. Vertical axis shows the fold change of the specific associated DNA region to BRG1 in ethanol treated group relative to control group. Error bars indicate standard error of the mean.
    Dnase I, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 97/100, based on 158 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i/product/Fisher Scientific
    Average 97 stars, based on 158 article reviews
    Price from $9.99 to $1999.99
    dnase i - by Bioz Stars, 2020-02
    97/100 stars
      Buy from Supplier

    90
    Bio-Rad dnase treatment
    ChIP analysis indicates that ethanol exposure increases BRG1 binding to DNAse I-resistant/CpG island containing region 3 and the pre-miR-9-2 coding exon Bar graph shows the effect of ethanol on BRG1-association with regions 1 to 5 and the pre-miR-9-2 exon-coding region of the primary (pri)-miR-9-2 coding locus. Primers for a gene desert on chromosome 6 (not predicted to bind any transcription factors) shows the specificity of the immuno-precipitation. Vertical axis shows the fold change of the specific associated DNA region to BRG1 in ethanol treated group relative to control group. Error bars indicate standard error of the mean.
    Dnase Treatment, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 450 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase treatment/product/Bio-Rad
    Average 90 stars, based on 450 article reviews
    Price from $9.99 to $1999.99
    dnase treatment - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    85
    Thermo Fisher dna polymerase i dnase i mixture
    ChIP analysis indicates that ethanol exposure increases BRG1 binding to DNAse I-resistant/CpG island containing region 3 and the pre-miR-9-2 coding exon Bar graph shows the effect of ethanol on BRG1-association with regions 1 to 5 and the pre-miR-9-2 exon-coding region of the primary (pri)-miR-9-2 coding locus. Primers for a gene desert on chromosome 6 (not predicted to bind any transcription factors) shows the specificity of the immuno-precipitation. Vertical axis shows the fold change of the specific associated DNA region to BRG1 in ethanol treated group relative to control group. Error bars indicate standard error of the mean.
    Dna Polymerase I Dnase I Mixture, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dna polymerase i dnase i mixture/product/Thermo Fisher
    Average 85 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    dna polymerase i dnase i mixture - by Bioz Stars, 2020-02
    85/100 stars
      Buy from Supplier

    82
    Thermo Fisher invitrogentm dnase i amplification grade
    ChIP analysis indicates that ethanol exposure increases BRG1 binding to DNAse I-resistant/CpG island containing region 3 and the pre-miR-9-2 coding exon Bar graph shows the effect of ethanol on BRG1-association with regions 1 to 5 and the pre-miR-9-2 exon-coding region of the primary (pri)-miR-9-2 coding locus. Primers for a gene desert on chromosome 6 (not predicted to bind any transcription factors) shows the specificity of the immuno-precipitation. Vertical axis shows the fold change of the specific associated DNA region to BRG1 in ethanol treated group relative to control group. Error bars indicate standard error of the mean.
    Invitrogentm Dnase I Amplification Grade, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 82/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/invitrogentm dnase i amplification grade/product/Thermo Fisher
    Average 82 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    invitrogentm dnase i amplification grade - by Bioz Stars, 2020-02
    82/100 stars
      Buy from Supplier

    Image Search Results


    TUNEL staining in necrotic spots . Transmitted light images  (A,E,I,M) , sytox orange nuclear staining  (B,F,J,N)  and TUNEL staining  (C,G,K,O)  on cross-sections of 5-week-old wild-type  (A–D) , and  sns-D  leaves  (I–L) . As positive controls, DNase I-treated cross-sections of wild-type  (E–H)  and  sns-D  leaf  (M–P)  are shown.  (D,H,L,P)  are merged images of  (B)  with  (C), (F)  with  (G), (J)  with  (K), (N)  with  (O) , respectively. TUNEL-positive nuclei are indicated by arrows. The bar is 25 μm.

    Journal: Frontiers in plant science

    Article Title: Programmed Cell Death in the Leaves of the Arabidopsis Spontaneous Necrotic Spots (sns-D) Mutant Correlates with Increased Expression of the Eukaryotic Translation Initiation Factor eIF4B2

    doi: 10.3389/fpls.2011.00009

    Figure Lengend Snippet: TUNEL staining in necrotic spots . Transmitted light images (A,E,I,M) , sytox orange nuclear staining (B,F,J,N) and TUNEL staining (C,G,K,O) on cross-sections of 5-week-old wild-type (A–D) , and sns-D leaves (I–L) . As positive controls, DNase I-treated cross-sections of wild-type (E–H) and sns-D leaf (M–P) are shown. (D,H,L,P) are merged images of (B) with (C), (F) with (G), (J) with (K), (N) with (O) , respectively. TUNEL-positive nuclei are indicated by arrows. The bar is 25 μm.

    Article Snippet: Residual DNA was removed from the RNA samples with DNase I (Ambion) in the presence of the RNase inhibitor RNasin (Promega). cDNA was produced on 1 μg of RNA using iScript cDNA synthesis kit according to the manufacturer's instructions (Bio-Rad).

    Techniques: TUNEL Assay, Staining

    Changes in DNase I accessibility at the HB-EGF promoter. BMMϕs were stimulated with LPS plus IC for 0, 15, 30, 60, or 120 min and then fixed with paraformaldehyde. Nuclei were isolated and treated with DNase for 1 h on ice. DNA was then purified

    Journal:

    Article Title: The Expression of Heparin-Binding Epidermal Growth Factor-Like Growth Factor by Regulatory Macrophages

    doi: 10.4049/jimmunol.0802703

    Figure Lengend Snippet: Changes in DNase I accessibility at the HB-EGF promoter. BMMϕs were stimulated with LPS plus IC for 0, 15, 30, 60, or 120 min and then fixed with paraformaldehyde. Nuclei were isolated and treated with DNase for 1 h on ice. DNA was then purified

    Article Snippet: TRIzol reagent and DNase I were purchased from Invitrogen Life Technologies.

    Techniques: Isolation, Purification

    c-Abl knockout inhibits actin filament polymerization in response to ACh stimulation.  a  Mouse tracheal rings from c-Abl -lox  and c-Abl smko  mice were treated with acetylcholine (ACh) (100 μM, 5 min) or left untreated (UT). F/G-actin ratios were evaluated using the fractionation assay. Data are mean ± SE ( n  = 5).  b  Representative images illustrating the effects of c-Abl knockout on F/G-actin ratios. Sections of trachealis from c-Abl -lox  and c-Abl smko  mice were stained with DNase I (for G-actin) or phalloidin (for F-actin).  c  ACh-induced increases in F/G-actin ratios evaluated by fluorescent microscopy are reduced in c-Abl smko  mice ( n  = 4). * P

    Journal: Respiratory Research

    Article Title: Role and regulation of Abelson tyrosine kinase in Crk-associated substrate/profilin-1 interaction and airway smooth muscle contraction

    doi: 10.1186/s12931-017-0709-4

    Figure Lengend Snippet: c-Abl knockout inhibits actin filament polymerization in response to ACh stimulation. a Mouse tracheal rings from c-Abl -lox and c-Abl smko mice were treated with acetylcholine (ACh) (100 μM, 5 min) or left untreated (UT). F/G-actin ratios were evaluated using the fractionation assay. Data are mean ± SE ( n  = 5). b Representative images illustrating the effects of c-Abl knockout on F/G-actin ratios. Sections of trachealis from c-Abl -lox and c-Abl smko mice were stained with DNase I (for G-actin) or phalloidin (for F-actin). c ACh-induced increases in F/G-actin ratios evaluated by fluorescent microscopy are reduced in c-Abl smko mice ( n  = 4). * P

    Article Snippet: Fluorophores used were rhodamine-phalloidin (Life Technologies, #R415, L/N 1738179) and Alexa fluor-488 DNase I (Life Technologies, #D12371, L/N 38965A).

    Techniques: Knock-Out, Mouse Assay, Fractionation, Staining, Microscopy

    TERRA accumulation requires HSF1 upon heat shock. ( A ) Western blot analysis of HSF1 WT and KD unstressed and stressed cells. Tubulin is shown as a loading control. ( B ) Dot blot analysis of TERRA. Total RNA was extracted from WT and HSF1 KD cells before and after HS and treated with DNAse. Various amount of total RNA fractions were subjected to RNA dot blot analysis using a radiolabelled TERRA probe. RNA were treated with RNase in parallel.The same blot was also hybridized after staining with a control probe specific for U2 transcripts. ( C ) Quantification of TERRA and U2 levels in WT and HSF1 KD cells before and after HS normalized with 37°C conditions. Standard deviation (SD) was calculated from 3 independent experiments. P -value = 0.0213 ( D ) Representative confocal images of FISH analyses of TERRA expression in WT and HSF1 KD cells before and after HS. RNase treatment induces an elimination of TERRA signal. Scale bar: 10 μm. ( E ) 3D quantification analysis of mean TERRA foci volume in the different conditions tested by RNA FISH using volocity software. The P -values calculated by unpaired Student's t -test with Welch's corrections at 37°C and at 43°C for WT and HSF1 KD cells are respectively P

    Journal: Nucleic Acids Research

    Article Title: Heat shock factor 1 promotes TERRA transcription and telomere protection upon heat stress

    doi: 10.1093/nar/gkx208

    Figure Lengend Snippet: TERRA accumulation requires HSF1 upon heat shock. ( A ) Western blot analysis of HSF1 WT and KD unstressed and stressed cells. Tubulin is shown as a loading control. ( B ) Dot blot analysis of TERRA. Total RNA was extracted from WT and HSF1 KD cells before and after HS and treated with DNAse. Various amount of total RNA fractions were subjected to RNA dot blot analysis using a radiolabelled TERRA probe. RNA were treated with RNase in parallel.The same blot was also hybridized after staining with a control probe specific for U2 transcripts. ( C ) Quantification of TERRA and U2 levels in WT and HSF1 KD cells before and after HS normalized with 37°C conditions. Standard deviation (SD) was calculated from 3 independent experiments. P -value = 0.0213 ( D ) Representative confocal images of FISH analyses of TERRA expression in WT and HSF1 KD cells before and after HS. RNase treatment induces an elimination of TERRA signal. Scale bar: 10 μm. ( E ) 3D quantification analysis of mean TERRA foci volume in the different conditions tested by RNA FISH using volocity software. The P -values calculated by unpaired Student's t -test with Welch's corrections at 37°C and at 43°C for WT and HSF1 KD cells are respectively P

    Article Snippet: RNA was treated with DNase (Ambion) for 30 min at 37°C.

    Techniques: Western Blot, Dot Blot, Staining, Standard Deviation, Fluorescence In Situ Hybridization, Expressing, Software

    Both EndoG and bleomycin induce DNase I and DNase X transcription in isolated rat brain cell nuclei. (A, B) In vitro transcription of DNase I and DNase X genes in isolated rat brain nuclei exposed with varying concentrations of recombinant EndoG (recEndoG)

    Journal: DNA and Cell Biology

    Article Title: Regulation of Apoptotic Endonucleases by EndoG

    doi: 10.1089/dna.2014.2772

    Figure Lengend Snippet: Both EndoG and bleomycin induce DNase I and DNase X transcription in isolated rat brain cell nuclei. (A, B) In vitro transcription of DNase I and DNase X genes in isolated rat brain nuclei exposed with varying concentrations of recombinant EndoG (recEndoG)

    Article Snippet: Primary antibodies, anti-DNase I, anti-CAD, and anti-GAPDH were detected with anti-rabbit IgG-horseradish peroxidase (HRP) while anti-DNase X, anti-DNase I-like 2, and anti-DNase γ were detected with donkey anti-goat IgG-HRP using SuperSignal chemiluminescent kit (Pierce Biotechnology).

    Techniques: Isolation, In Vitro, Recombinant

    Induction of DNase I-like endonucleases in EndoG-overexpressing cells. (A) Western blotting for DNase I, DNase X (both at 8 h), DNase 1-like 2, DNase γ (both at 12 h), caspase-activated DNase (CAD) (at 8 h post-transfection),

    Journal: DNA and Cell Biology

    Article Title: Regulation of Apoptotic Endonucleases by EndoG

    doi: 10.1089/dna.2014.2772

    Figure Lengend Snippet: Induction of DNase I-like endonucleases in EndoG-overexpressing cells. (A) Western blotting for DNase I, DNase X (both at 8 h), DNase 1-like 2, DNase γ (both at 12 h), caspase-activated DNase (CAD) (at 8 h post-transfection),

    Article Snippet: Primary antibodies, anti-DNase I, anti-CAD, and anti-GAPDH were detected with anti-rabbit IgG-horseradish peroxidase (HRP) while anti-DNase X, anti-DNase I-like 2, and anti-DNase γ were detected with donkey anti-goat IgG-HRP using SuperSignal chemiluminescent kit (Pierce Biotechnology).

    Techniques: Western Blot, Transfection

    Transfection of total RNA harvested from poly(dA–dT) transfected cells results in IFN- β expression. 293T cells were transfected with 12 μg total RNA extracted from 293T cells that had been transfected with 12 μg poly(dA–dT) for 24 h. Induction of IFN- β mRNA was confirmed to be specific for an immunostimulatory RNA species by treating total RNA with either (a) 0.1 mg RNase A ml −1 or (b) 0.1 U amplification grade DNase I μl −1 . Total RNA was then extracted 24 h post-transfection and real-time qPCR performed for IFN- β . These data were normalized against GAPDH mRNA levels. Error bars indicate the mean± sem (* P

    Journal: The Journal of General Virology

    Article Title: Inhibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3

    doi: 10.1099/vir.0.021998-0

    Figure Lengend Snippet: Transfection of total RNA harvested from poly(dA–dT) transfected cells results in IFN- β expression. 293T cells were transfected with 12 μg total RNA extracted from 293T cells that had been transfected with 12 μg poly(dA–dT) for 24 h. Induction of IFN- β mRNA was confirmed to be specific for an immunostimulatory RNA species by treating total RNA with either (a) 0.1 mg RNase A ml −1 or (b) 0.1 U amplification grade DNase I μl −1 . Total RNA was then extracted 24 h post-transfection and real-time qPCR performed for IFN- β . These data were normalized against GAPDH mRNA levels. Error bars indicate the mean± sem (* P

    Article Snippet: Nucleic acids were treated either with RNase A using the conditions described previously ( ) or with amplification grade DNase I following the manufacturer's instructions (Invitrogen).

    Techniques: Transfection, Expressing, Amplification, Real-time Polymerase Chain Reaction

    NETs contribute to the pathogenesis of myocarditis. (a) Confocal immunofluorescence images of an EMB of patient 6 suffering from PVB19-positive myocarditis (see Table 1 ). Top: Images show staining of H2A-H2B-DNA, MPO, and H3Cit as well as the merged image. Bar, 20 µm. Bottom: Magnification of a selected area of the merged confocal image (box) from the top panel. Arrows indicate NETs. Bar, 10 µm. (b and c) EAM score (b) as well as evaluation of the heart/body weight ratio (c) at day 21 after induction of EAM or sham immunization (sham; mean EAM score, 0.5 ± 0.19; mean heart/body weight ratio, 0.57 ± 0.01). Mice were treated with DNase (EAM + DNase: mean EAM score, 0.8 ± 0.19; mean heart/body weight ratio, 0.62 ± 0.005), Cl-amid (EAM + Cl-amid: mean EAM score, 0.9 ± 0.20; mean heart/body weight ratio, 0.62 ± 0.01), or vehicle as control (EAM + vehicle: mean EAM score, 1.7 ± 0.25; mean heart/body weight ratio, 0.71 ± 0.04) as indicated. n = 8 for sham group; n = 26 for EAM groups. (d) Left: Representative confocal images of cardiac sections of immunized WT mice at day 21 after induction of EAM (EAM + vehicle). Images show staining of DNA, NE, and H3Cit as well as the merged image. Bars, 20 µm. Right: Representative confocal magnified image of NETs. Images show staining of DNA, NE, and H3Cit as well as the merged image, colocalization (coloc) of DNA/NE, and DNA/H3Cit as indicated. Bars, 10 µm. (e) Representative confocal images of cardiac sections of EAM mice at day 21 after induction of EAM and blockade of MK for 21 d. Images show staining of DNA, NE, and H3Cit as well as the merged image. Bars, 20 µm. (f–h) Histological analysis of extravasated PMN into the cardiac tissue at day 21 after induction of EAM without blocking MK (EAM + vehicle) or after application of an anti-N-MK blocking Ab (EAM + anti-N-MK). Diagrams show the number of extravasated PMNs per mm 2 (f: vehicle, 768 ± 55 PMN/mm 2 ; anti-N-MK, 158 ± 86 PMN/mm 2 ), the number of NET + PMNs per mm 2 (g: vehicle, 40 ± 6 NET + PMN; anti-N-MK = 5 ± 2 NET + PMN), and the number of NET + PMNs as a percentage of all extravasated PMNs (h: vehicle, 5.1 ± 0.5 NET + PMN [%]; anti-N-MK, 0.9 ± 0.6 NET + PMN [%]). n = 6 mice. To determine P values, ANOVA on ranks with Dunn’s multiple comparisons test was performed for c and d, and an unpaired Student's t test was used for f–h. For all panels, *, P

    Journal: The Journal of Experimental Medicine

    Article Title: Midkine drives cardiac inflammation by promoting neutrophil trafficking and NETosis in myocarditis

    doi: 10.1084/jem.20181102

    Figure Lengend Snippet: NETs contribute to the pathogenesis of myocarditis. (a) Confocal immunofluorescence images of an EMB of patient 6 suffering from PVB19-positive myocarditis (see Table 1 ). Top: Images show staining of H2A-H2B-DNA, MPO, and H3Cit as well as the merged image. Bar, 20 µm. Bottom: Magnification of a selected area of the merged confocal image (box) from the top panel. Arrows indicate NETs. Bar, 10 µm. (b and c) EAM score (b) as well as evaluation of the heart/body weight ratio (c) at day 21 after induction of EAM or sham immunization (sham; mean EAM score, 0.5 ± 0.19; mean heart/body weight ratio, 0.57 ± 0.01). Mice were treated with DNase (EAM + DNase: mean EAM score, 0.8 ± 0.19; mean heart/body weight ratio, 0.62 ± 0.005), Cl-amid (EAM + Cl-amid: mean EAM score, 0.9 ± 0.20; mean heart/body weight ratio, 0.62 ± 0.01), or vehicle as control (EAM + vehicle: mean EAM score, 1.7 ± 0.25; mean heart/body weight ratio, 0.71 ± 0.04) as indicated. n = 8 for sham group; n = 26 for EAM groups. (d) Left: Representative confocal images of cardiac sections of immunized WT mice at day 21 after induction of EAM (EAM + vehicle). Images show staining of DNA, NE, and H3Cit as well as the merged image. Bars, 20 µm. Right: Representative confocal magnified image of NETs. Images show staining of DNA, NE, and H3Cit as well as the merged image, colocalization (coloc) of DNA/NE, and DNA/H3Cit as indicated. Bars, 10 µm. (e) Representative confocal images of cardiac sections of EAM mice at day 21 after induction of EAM and blockade of MK for 21 d. Images show staining of DNA, NE, and H3Cit as well as the merged image. Bars, 20 µm. (f–h) Histological analysis of extravasated PMN into the cardiac tissue at day 21 after induction of EAM without blocking MK (EAM + vehicle) or after application of an anti-N-MK blocking Ab (EAM + anti-N-MK). Diagrams show the number of extravasated PMNs per mm 2 (f: vehicle, 768 ± 55 PMN/mm 2 ; anti-N-MK, 158 ± 86 PMN/mm 2 ), the number of NET + PMNs per mm 2 (g: vehicle, 40 ± 6 NET + PMN; anti-N-MK = 5 ± 2 NET + PMN), and the number of NET + PMNs as a percentage of all extravasated PMNs (h: vehicle, 5.1 ± 0.5 NET + PMN [%]; anti-N-MK, 0.9 ± 0.6 NET + PMN [%]). n = 6 mice. To determine P values, ANOVA on ranks with Dunn’s multiple comparisons test was performed for c and d, and an unpaired Student's t test was used for f–h. For all panels, *, P

    Article Snippet: RNA was isolated using TRIzol (15596026; Thermo Fisher) according to the manufacturer’s protocol, and genomic DNA was digested using the DNase I Amplification Grade kit (18068015; Thermo Fisher).

    Techniques: Immunofluorescence, Staining, Mouse Assay, Blocking Assay

    DNase I treatment is effective against C. jejuni biofilms on stainless steel surfaces and in the presence of organic materials in aerobic conditions . The ability of DNase I to inhibit biofilm formation of C. jejuni NCTC 11168 on sterile, stainless steel coupons (A) or in the presence of chicken juice, mimicking a conditioned surface (B) . TTC staining was used to measure biofilm formation in the presence of chicken juice (B) . DNase I is able to significantly decrease biofilm formation in both conditions. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Journal: Frontiers in Microbiology

    Article Title: Campylobacter jejuni biofilms contain extracellular DNA and are sensitive to DNase I treatment

    doi: 10.3389/fmicb.2015.00699

    Figure Lengend Snippet: DNase I treatment is effective against C. jejuni biofilms on stainless steel surfaces and in the presence of organic materials in aerobic conditions . The ability of DNase I to inhibit biofilm formation of C. jejuni NCTC 11168 on sterile, stainless steel coupons (A) or in the presence of chicken juice, mimicking a conditioned surface (B) . TTC staining was used to measure biofilm formation in the presence of chicken juice (B) . DNase I is able to significantly decrease biofilm formation in both conditions. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Article Snippet: Enzyme treatment of C. jejuni biofilms For DNase I treatments, unless otherwise stated, a volume of 4 μl DNase I enzyme (Fermentas), giving a final concentration within the biofilm of 4 U/ml v/v and 4 μl of DNase I buffer (Fermentas) were added to each test tube, along with 1 ml of diluted cell suspension at either the start of the static incubation or after 12, 24, 36, or 48 h of static incubation.

    Techniques: Staining, Standard Deviation, MANN-WHITNEY

    DNase I is able to rapidly degrade C. jejuni NCTC 11168 biofilms . (A) DNase I (4 units/ml) was added at defined intervals to aerobically incubated NCTC 11168 cultures over a 48 h static incubation and biofilm degradation assessed by crystal violet staining. (B) Following a 48 h static incubation to allow biofilm formation, DNase I was added to biofilms for between 5 and 120 min before biofilm degradation was assessed. (C) The concentration of DNase I required for biofilm control was also assessed using DNase I concentrations of between 0.01 and 5 U/ml. In each graph, “11168” represents an untreated biofilm culture of C. jejuni NCTC 11168 and “control” represents a tube containing sterile Brucella medium only. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Journal: Frontiers in Microbiology

    Article Title: Campylobacter jejuni biofilms contain extracellular DNA and are sensitive to DNase I treatment

    doi: 10.3389/fmicb.2015.00699

    Figure Lengend Snippet: DNase I is able to rapidly degrade C. jejuni NCTC 11168 biofilms . (A) DNase I (4 units/ml) was added at defined intervals to aerobically incubated NCTC 11168 cultures over a 48 h static incubation and biofilm degradation assessed by crystal violet staining. (B) Following a 48 h static incubation to allow biofilm formation, DNase I was added to biofilms for between 5 and 120 min before biofilm degradation was assessed. (C) The concentration of DNase I required for biofilm control was also assessed using DNase I concentrations of between 0.01 and 5 U/ml. In each graph, “11168” represents an untreated biofilm culture of C. jejuni NCTC 11168 and “control” represents a tube containing sterile Brucella medium only. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Article Snippet: Enzyme treatment of C. jejuni biofilms For DNase I treatments, unless otherwise stated, a volume of 4 μl DNase I enzyme (Fermentas), giving a final concentration within the biofilm of 4 U/ml v/v and 4 μl of DNase I buffer (Fermentas) were added to each test tube, along with 1 ml of diluted cell suspension at either the start of the static incubation or after 12, 24, 36, or 48 h of static incubation.

    Techniques: Incubation, Staining, Concentration Assay, Standard Deviation, MANN-WHITNEY

    Treatment of pre-existing biofilms with DNase I leads to inhibition of biofilm regrowth . C. jejuni NCTC 11168 biofilms were allowed to form for 48 h in sterile borosilicate glass test tubes. To assess biofilm re-growth following DNase I treatment, two sets of tubes were treated with 4 U/ml DNase I for 15 min then washed with sterile PBS. Tubes were then supplemented with either fresh Brucella media (fifth bar) or fresh C. jejuni NCTC 11168 culture (sixth bar) and incubated for a further 48 h. The following controls were also prepared: C. jejuni NCTC 11168 biofilm formation following primary culture (first bar, white), tubes supplemented with sterile Brucella media (second bar, black), C. jejuni NCTC 11168 biofilm formation following only secondary culture (third bar, light gray), and 48 h-old C. jejuni NCTC 11168 biofilm, washed with PBS, then supplemented with fresh C. jejuni NCTC 11168 culture (fourth bar, dark gray). Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Journal: Frontiers in Microbiology

    Article Title: Campylobacter jejuni biofilms contain extracellular DNA and are sensitive to DNase I treatment

    doi: 10.3389/fmicb.2015.00699

    Figure Lengend Snippet: Treatment of pre-existing biofilms with DNase I leads to inhibition of biofilm regrowth . C. jejuni NCTC 11168 biofilms were allowed to form for 48 h in sterile borosilicate glass test tubes. To assess biofilm re-growth following DNase I treatment, two sets of tubes were treated with 4 U/ml DNase I for 15 min then washed with sterile PBS. Tubes were then supplemented with either fresh Brucella media (fifth bar) or fresh C. jejuni NCTC 11168 culture (sixth bar) and incubated for a further 48 h. The following controls were also prepared: C. jejuni NCTC 11168 biofilm formation following primary culture (first bar, white), tubes supplemented with sterile Brucella media (second bar, black), C. jejuni NCTC 11168 biofilm formation following only secondary culture (third bar, light gray), and 48 h-old C. jejuni NCTC 11168 biofilm, washed with PBS, then supplemented with fresh C. jejuni NCTC 11168 culture (fourth bar, dark gray). Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Article Snippet: Enzyme treatment of C. jejuni biofilms For DNase I treatments, unless otherwise stated, a volume of 4 μl DNase I enzyme (Fermentas), giving a final concentration within the biofilm of 4 U/ml v/v and 4 μl of DNase I buffer (Fermentas) were added to each test tube, along with 1 ml of diluted cell suspension at either the start of the static incubation or after 12, 24, 36, or 48 h of static incubation.

    Techniques: Inhibition, Incubation, Standard Deviation, MANN-WHITNEY

    Restriction endonuclease treatment of C. jejuni biofilms reduces biofilm formation . Static cultures of C. jejuni NCTC 11168 (A,B) and 81116 (C,D) were prepared then supplemented with either DNase I, RNase, or a single restriction endonuclease. Cultures were incubated for 48 h at 37°C in aerobic conditions. A range of restriction enzymes was selected, based on varying levels of DNA fragmentation following digestion of C. jejuni NCTC 11168 (B) and 81116 (D) genomic DNA. Restriction enzyme and DNase I treatment of NCTC 11168 biofilms lead to a reduction in biofilm formation. The same trend was observed for C. jejuni 81116, although only DNase I and Hae III digestion were significantly different from the control. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Journal: Frontiers in Microbiology

    Article Title: Campylobacter jejuni biofilms contain extracellular DNA and are sensitive to DNase I treatment

    doi: 10.3389/fmicb.2015.00699

    Figure Lengend Snippet: Restriction endonuclease treatment of C. jejuni biofilms reduces biofilm formation . Static cultures of C. jejuni NCTC 11168 (A,B) and 81116 (C,D) were prepared then supplemented with either DNase I, RNase, or a single restriction endonuclease. Cultures were incubated for 48 h at 37°C in aerobic conditions. A range of restriction enzymes was selected, based on varying levels of DNA fragmentation following digestion of C. jejuni NCTC 11168 (B) and 81116 (D) genomic DNA. Restriction enzyme and DNase I treatment of NCTC 11168 biofilms lead to a reduction in biofilm formation. The same trend was observed for C. jejuni 81116, although only DNase I and Hae III digestion were significantly different from the control. Error bars show standard deviation. Statistically significant results, as determined using the Mann–Whitney U test, are indicated using an asterisk ( * P

    Article Snippet: Enzyme treatment of C. jejuni biofilms For DNase I treatments, unless otherwise stated, a volume of 4 μl DNase I enzyme (Fermentas), giving a final concentration within the biofilm of 4 U/ml v/v and 4 μl of DNase I buffer (Fermentas) were added to each test tube, along with 1 ml of diluted cell suspension at either the start of the static incubation or after 12, 24, 36, or 48 h of static incubation.

    Techniques: Incubation, Standard Deviation, MANN-WHITNEY

    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

    Consensus GGUG-containing RNA oligonucleotide promotes the inhibitory effect of TLS on CBP/p300 HAT activities a , Co-immunoprecipitation (IP) of p300 and TLS from RNase A-treated HeLa cells. b, P300 HAT activity was measured using micrococcal nuclease (MNase) or DNase I pre-treated GST and GST-TLS in the presence of GGUG- or CCUC-oligonucleotide. * p

    Journal: Nature

    Article Title: Induced ncRNAs Allosterically Modify RNA Binding Proteins in cis to Inhibit Transcription

    doi: 10.1038/nature06992

    Figure Lengend Snippet: Consensus GGUG-containing RNA oligonucleotide promotes the inhibitory effect of TLS on CBP/p300 HAT activities a , Co-immunoprecipitation (IP) of p300 and TLS from RNase A-treated HeLa cells. b, P300 HAT activity was measured using micrococcal nuclease (MNase) or DNase I pre-treated GST and GST-TLS in the presence of GGUG- or CCUC-oligonucleotide. * p

    Article Snippet: The soluble DNA-bound RNA fraction was collected after centrifugation at 4,000 g for 15 min. RNA was extracted using Trizol (Invitrogen) and treated with RNase-free DNase I (DNA-free; Ambion).

    Techniques: HAT Assay, Immunoprecipitation, Activity Assay

    Viral gene transcription of BAC36 and BAC-stop45 viruses after a de novo infection. HFF were infected with BAC36 and BAC-stop45 viruses (50 genome copies per cell). Six hours after infection, total RNAs were extracted, treated with DNase I, and reverse

    Journal:

    Article Title: Functional Characterization of Kaposi's Sarcoma-Associated Herpesvirus ORF45 by Bacterial Artificial Chromosome-Based Mutagenesis ▿

    doi: 10.1128/JVI.01275-06

    Figure Lengend Snippet: Viral gene transcription of BAC36 and BAC-stop45 viruses after a de novo infection. HFF were infected with BAC36 and BAC-stop45 viruses (50 genome copies per cell). Six hours after infection, total RNAs were extracted, treated with DNase I, and reverse

    Article Snippet: Turbo DNase I was obtained from Ambion (Austin, TX).

    Techniques: BAC Assay, Infection

    Analysis of the oocyte nucleolus components.  (A) The compact structure of the oocyte nucleolus prevents antibody inflow into the structure. EGFP-NPM2 signals (green) in the oocyte nucleolus could not be stained by anti-GFP antibody (red). DNA was stained by DAPI (gray). DIC, differential interference contrast. (B) Components in the oocyte nucleolus were assessed by proteinase K, DNase I, and RNase A (left). The activity of the enzymes was checked at each time point indicated above the gel image. Digestion of DNA and RNA was checked by using 1% agarose gel electrophoresis (right). (C) The method of MS analysis using isolated nucleoli by enucleolation from GV-oocytes. The isolated nucleoli were kept in evacuated zona pellucidae and used for MS analysis. (D) List of identified nucleolus proteins. (E) Localization of MS candidate proteins tagged with eGFP (green) at the N-terminus. DIC, differential interference contrast. (F) NPM2 localization in the oocyte nucleolus was confirmed by western blotting. The oocyte number in each sample is indicated above the blots and α-tubulin (TUB) was used as a loading control ( n =3). (G) NPM1 (green) localized at the nucleoplasm and NPM2 localized at the nucleolus in cryosections. DNA was stained by DAPI (gray).

    Journal: Journal of Cell Science

    Article Title: Reconstitution of the oocyte nucleolus in mice through a single nucleolar protein, NPM2

    doi: 10.1242/jcs.195875

    Figure Lengend Snippet: Analysis of the oocyte nucleolus components. (A) The compact structure of the oocyte nucleolus prevents antibody inflow into the structure. EGFP-NPM2 signals (green) in the oocyte nucleolus could not be stained by anti-GFP antibody (red). DNA was stained by DAPI (gray). DIC, differential interference contrast. (B) Components in the oocyte nucleolus were assessed by proteinase K, DNase I, and RNase A (left). The activity of the enzymes was checked at each time point indicated above the gel image. Digestion of DNA and RNA was checked by using 1% agarose gel electrophoresis (right). (C) The method of MS analysis using isolated nucleoli by enucleolation from GV-oocytes. The isolated nucleoli were kept in evacuated zona pellucidae and used for MS analysis. (D) List of identified nucleolus proteins. (E) Localization of MS candidate proteins tagged with eGFP (green) at the N-terminus. DIC, differential interference contrast. (F) NPM2 localization in the oocyte nucleolus was confirmed by western blotting. The oocyte number in each sample is indicated above the blots and α-tubulin (TUB) was used as a loading control ( n =3). (G) NPM1 (green) localized at the nucleoplasm and NPM2 localized at the nucleolus in cryosections. DNA was stained by DAPI (gray).

    Article Snippet: To determine the components of the oocyte nucleoli, isolated nucleoli were treated with proteinase K (Roche) at 2 μg/10 μl, Turbo DNase I (Ambion) 1 U/ 10 μl and RNase A at 0.25 U/10 μl in modified HTF medium without BSA, and were observed under an inverted microscope (Olympus IX71).

    Techniques: Staining, Activity Assay, Agarose Gel Electrophoresis, Mass Spectrometry, Isolation, Western Blot

    DNase I footprinting analysis of PdxR binding to the mutant pdxRS regulatory regions pdxRSp1 (A), pdxRSp2 (B, D), and pdxRSp4 (C, D) DNA fragments, radioactively labeled on the bottom (A, B, C) or top (D) strand, were incubated with increasing concentrations of purified PdxR and in the absence or presence of 100 μM PLP. PdxR monomer concentrations used (nM) are indicated below each lane. The corresponding A + G sequencing ladder is shown in the left and right lanes. The protected areas are indicated by vertical lines.

    Journal: Molecular microbiology

    Article Title: Role of PdxR in the activation of vitamin B6 biosynthesis in Listeria monocytogenes

    doi: 10.1111/mmi.12618

    Figure Lengend Snippet: DNase I footprinting analysis of PdxR binding to the mutant pdxRS regulatory regions pdxRSp1 (A), pdxRSp2 (B, D), and pdxRSp4 (C, D) DNA fragments, radioactively labeled on the bottom (A, B, C) or top (D) strand, were incubated with increasing concentrations of purified PdxR and in the absence or presence of 100 μM PLP. PdxR monomer concentrations used (nM) are indicated below each lane. The corresponding A + G sequencing ladder is shown in the left and right lanes. The protected areas are indicated by vertical lines.

    Article Snippet: For real-time RT-PCR experiments, purified RNA (~10 μg) was further treated with Turbo DNA- free DNase I (Ambion) according to the manufacturer’s instructions.

    Techniques: Footprinting, Binding Assay, Mutagenesis, Labeling, Incubation, Purification, Plasmid Purification, Sequencing

    Effect of calpain-like silencing during PCD. (A) DNA fragmentation in calpain-like silenced trophozoites after PCD induction by G418. Confocal microscopy analysis of trophozoites showing the TUNEL staining, samples were counter-stained with DAPI. (A) Negative control, untreated trophozoites; (B) Positive control, trophozoites treated with 20 μg of DNase I endonuclease for 30 min; (C) Trophozoites after a 9-h incubation with 10 μg/ml of G418; (D,E) Trophozoites pre-incubated for 24 h with NRS (D) or calpain-like (E) siRNAs sequences and then 9 h with 10 μg/ml G418; (B) Densitometric analysis of (A). (C) Effect of calpain-like silencing on the cell viability of E. histolytica incubated with G418; (A) Negative control, untreated trophozoites; (B) Trophozoites after a 9-h incubation with 10 μg/ml of G418; (C,D) Trophozoites pre-incubated for 24 h with NRS (C) or calpain-like (D) siRNAs sequences and then 9 h with 10 μg/ml G418. *indicate statistically significant difference: P

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: A Calpain-Like Protein Is Involved in the Execution Phase of Programmed Cell Death of Entamoeba histolytica

    doi: 10.3389/fcimb.2018.00339

    Figure Lengend Snippet: Effect of calpain-like silencing during PCD. (A) DNA fragmentation in calpain-like silenced trophozoites after PCD induction by G418. Confocal microscopy analysis of trophozoites showing the TUNEL staining, samples were counter-stained with DAPI. (A) Negative control, untreated trophozoites; (B) Positive control, trophozoites treated with 20 μg of DNase I endonuclease for 30 min; (C) Trophozoites after a 9-h incubation with 10 μg/ml of G418; (D,E) Trophozoites pre-incubated for 24 h with NRS (D) or calpain-like (E) siRNAs sequences and then 9 h with 10 μg/ml G418; (B) Densitometric analysis of (A). (C) Effect of calpain-like silencing on the cell viability of E. histolytica incubated with G418; (A) Negative control, untreated trophozoites; (B) Trophozoites after a 9-h incubation with 10 μg/ml of G418; (C,D) Trophozoites pre-incubated for 24 h with NRS (C) or calpain-like (D) siRNAs sequences and then 9 h with 10 μg/ml G418. *indicate statistically significant difference: P

    Article Snippet: As a positive control, trophozoites were treated with 20 mg/ml DNase I endonuclease (Invitrogen) for 30 min, and non-treated trophozoites were used as a negative control.

    Techniques: Confocal Microscopy, TUNEL Assay, Staining, Negative Control, Positive Control, Incubation

    Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of RNase/DNase treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).

    Journal: Virology Journal

    Article Title: Packaging of viral RNAs in virions of adenoviruses

    doi: 10.1186/1743-422X-6-16

    Figure Lengend Snippet: Analysis of viral protein and DNA in HAV5.EGFP capsids . (A) Proteins from lysates of RNase/DNase treated or untreated mature and empty/intermediate capsids were separated by 10% SDS-PAGE, and stained by SYPRO Ruby protein stains. A 100 kDa hexon protein band was used for determining the capsid protein concentration using Kodak IM Network software. (B) Total yields of DNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. ( C ) EGFP expression. 293 cells were transduced by 10 fold serially diluted mature and empty/intermediate capsids with or without RNase/DNase treatment. At 48 h post transduction, cells were analysed for EGFP expression by a fluorescent microscope (i) EGFP, (ii) Phase contrast. Presence (+). Absence (-). Mature (Ma); Empty/Intermediate (E-I).

    Article Snippet: To analyze the amount of viral RNAs present in the total RNAs isolated from mature and empty/intermediate capsids, 2 μg of RNA isolated from mature or empty/intermediate capsids without RNase/DNase treatment was reversely transcribed by reverse transcriptase II (Invitrogen) in the presence of [32 P]-dCTP.

    Techniques: SDS Page, Staining, Protein Concentration, Software, Isolation, Expressing, Transduction, Microscopy

    Analysis of RNA in HAV5.EGFP capsids with or without RNase/DNase treatment . (A) Total yields of RNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. (B) The [ 32 P]-labeled cDNAs were made by reverse transcription of 2 μg, RNase-free DNase treated RNAs from mature and empty/intermediate capsids with or without RNase/DNase treatment and hybridized to Hind III-digested pFHAV5, which contains E1A-deleted HAdV-5 genome. RT was primed by oligo-dT/hexamers. (C) Viral RNAs detected in RNAs from mature (Ma) and empty/intermediate (E-I) capsids after RNase/DNase treatment in Southern hybridization in panel B were quantitated by using PhosphorImager software.

    Journal: Virology Journal

    Article Title: Packaging of viral RNAs in virions of adenoviruses

    doi: 10.1186/1743-422X-6-16

    Figure Lengend Snippet: Analysis of RNA in HAV5.EGFP capsids with or without RNase/DNase treatment . (A) Total yields of RNAs isolated from mature and empty/intermediate capsids with or without RNase/DNase treatment. (B) The [ 32 P]-labeled cDNAs were made by reverse transcription of 2 μg, RNase-free DNase treated RNAs from mature and empty/intermediate capsids with or without RNase/DNase treatment and hybridized to Hind III-digested pFHAV5, which contains E1A-deleted HAdV-5 genome. RT was primed by oligo-dT/hexamers. (C) Viral RNAs detected in RNAs from mature (Ma) and empty/intermediate (E-I) capsids after RNase/DNase treatment in Southern hybridization in panel B were quantitated by using PhosphorImager software.

    Article Snippet: To analyze the amount of viral RNAs present in the total RNAs isolated from mature and empty/intermediate capsids, 2 μg of RNA isolated from mature or empty/intermediate capsids without RNase/DNase treatment was reversely transcribed by reverse transcriptase II (Invitrogen) in the presence of [32 P]-dCTP.

    Techniques: Isolation, Labeling, Hybridization, Software

    Enzymatic resistance of phosphorothioate-modified Au-TDNNs. (A, B) Fluorescence time graph depicting terminal-modified Au-TDNN and overall-modified Au-TDNN degradation by DNase I. (C, D) Fluorescence time graph depicting terminal-modified Au-TDNN and overall-modified Au-TDNN degradation by Exo III.

    Journal: Theranostics

    Article Title: High-Discrimination Factor Nanosensor Based on Tetrahedral DNA Nanostructures and Gold Nanoparticles for Detection of MiRNA-21 in Live Cells

    doi: 10.7150/thno.23852

    Figure Lengend Snippet: Enzymatic resistance of phosphorothioate-modified Au-TDNNs. (A, B) Fluorescence time graph depicting terminal-modified Au-TDNN and overall-modified Au-TDNN degradation by DNase I. (C, D) Fluorescence time graph depicting terminal-modified Au-TDNN and overall-modified Au-TDNN degradation by Exo III.

    Article Snippet: For both human DNase I (Thermo Scientific) and exonuclease III (New England Biolabs) digestion, a common concentration of 3 U/mL was used to digest 2 nM Au-TDNNs samples in PBS.

    Techniques: Modification, Fluorescence

    The spatial distribution of actin in RBC ghosts revealed by fluorescent probes of phalloidin-rhodamine and DNase I–FITC. The spatial distribution of the fluorescent probes was analyzed via a three-dimensional optical sectioning by a confocal inverted laser scanning microscope. ( A ) Optical sections ( a–h , 0.6 μm apart) of RBC ghost labeled by phalloidin-rhodamine (4.4 μM). Each square of the gallery of images possesses a dimension of 9.5 μm × 9.5 μm. ( B ) The distribution of phalloidin-rhodamine and DNase I–FITC in RBC ghosts in an optical section taken at the middle (half thickness) of the RBC ghost. Inset , The separate distribution of phalloidin-rhodamine ( red ) and DNase I ( green ) in a RBC ghost that was labeled with both phalloidin-rhodamine and DNase I–FITC. Bars: ( A ) 5 μm; ( B ) 10 μm.

    Journal: The Journal of Cell Biology

    Article Title: Mechanical Fluctuations of the Membrane-Skeleton Are Dependent on F-Actin ATPase in Human Erythrocytes

    doi:

    Figure Lengend Snippet: The spatial distribution of actin in RBC ghosts revealed by fluorescent probes of phalloidin-rhodamine and DNase I–FITC. The spatial distribution of the fluorescent probes was analyzed via a three-dimensional optical sectioning by a confocal inverted laser scanning microscope. ( A ) Optical sections ( a–h , 0.6 μm apart) of RBC ghost labeled by phalloidin-rhodamine (4.4 μM). Each square of the gallery of images possesses a dimension of 9.5 μm × 9.5 μm. ( B ) The distribution of phalloidin-rhodamine and DNase I–FITC in RBC ghosts in an optical section taken at the middle (half thickness) of the RBC ghost. Inset , The separate distribution of phalloidin-rhodamine ( red ) and DNase I ( green ) in a RBC ghost that was labeled with both phalloidin-rhodamine and DNase I–FITC. Bars: ( A ) 5 μm; ( B ) 10 μm.

    Article Snippet: The RBC ghosts were washed twice with a KCl solution, and then incubated with 4.4 μM phalloidin-rhodamine (Molecular Probes, Inc., Eugene, OR) alone or with a combination of 4.4 μM phalloidin-rhodamine and 35 nM DNase I–FITC (Molecular Probes, Inc.).

    Techniques: Laser-Scanning Microscopy, Labeling

    ChIP analysis indicates that ethanol exposure increases BRG1 binding to DNAse I-resistant/CpG island containing region 3 and the pre-miR-9-2 coding exon Bar graph shows the effect of ethanol on BRG1-association with regions 1 to 5 and the pre-miR-9-2 exon-coding region of the primary (pri)-miR-9-2 coding locus. Primers for a gene desert on chromosome 6 (not predicted to bind any transcription factors) shows the specificity of the immuno-precipitation. Vertical axis shows the fold change of the specific associated DNA region to BRG1 in ethanol treated group relative to control group. Error bars indicate standard error of the mean.

    Journal: Alcohol (Fayetteville, N.Y.)

    Article Title: The BAF (BRG1/BRM-Associated Factor) Chromatin-Remodeling Complex Exhibits Ethanol Sensitivity in Fetal Neural Progenitor Cells and Regulates Transcription at the Mir-9-2 Encoding Gene Locus

    doi: 10.1016/j.alcohol.2017.01.003

    Figure Lengend Snippet: ChIP analysis indicates that ethanol exposure increases BRG1 binding to DNAse I-resistant/CpG island containing region 3 and the pre-miR-9-2 coding exon Bar graph shows the effect of ethanol on BRG1-association with regions 1 to 5 and the pre-miR-9-2 exon-coding region of the primary (pri)-miR-9-2 coding locus. Primers for a gene desert on chromosome 6 (not predicted to bind any transcription factors) shows the specificity of the immuno-precipitation. Vertical axis shows the fold change of the specific associated DNA region to BRG1 in ethanol treated group relative to control group. Error bars indicate standard error of the mean.

    Article Snippet: As described in , nuclear pellets were treated with either 0, 20, 60 or 120U of DNAse I (Ambion/Thermo Fisher Scientific) for one hour on ice.

    Techniques: Chromatin Immunoprecipitation, Binding Assay, Immunoprecipitation

    BRG1-containing complexes associate with both DNAse I-hypersensitive and insensitive sites on the miR-9-2 gene locus (a) Positional representation of POU5F1/Oct4, c-myc and REST transcription regulatory factor binding sites along the human pre-miR-9-2 gene locus identified with the UCSC genome browser ENCODE analysis hub track. Colored circles indicate locations for primer pairs for pri-miR-9-2 regions 1,2,3,4 and 5 and the pre-miR-9-2 coding region. (b) qPCR results of BRG1-ChIP from neurospheres. Primers were used to amplify 6 distinct positions along the pri-miR-9-2 gene locus and a genetically sparse region on mouse chromosome 6. Vertical axis shows fold change relative to an IgG pulldown control. Error bars indicate standard error of the mean. (c) qPCR of neurosphere DNA following digestion with 20, 60 and 120U of DNAse I at the 6 positions along the pri-miR-9-2 gene locus. The vertical axis shows fold amplification relative to DNAse I-untreated neurosphere DNA.

    Journal: Alcohol (Fayetteville, N.Y.)

    Article Title: The BAF (BRG1/BRM-Associated Factor) Chromatin-Remodeling Complex Exhibits Ethanol Sensitivity in Fetal Neural Progenitor Cells and Regulates Transcription at the Mir-9-2 Encoding Gene Locus

    doi: 10.1016/j.alcohol.2017.01.003

    Figure Lengend Snippet: BRG1-containing complexes associate with both DNAse I-hypersensitive and insensitive sites on the miR-9-2 gene locus (a) Positional representation of POU5F1/Oct4, c-myc and REST transcription regulatory factor binding sites along the human pre-miR-9-2 gene locus identified with the UCSC genome browser ENCODE analysis hub track. Colored circles indicate locations for primer pairs for pri-miR-9-2 regions 1,2,3,4 and 5 and the pre-miR-9-2 coding region. (b) qPCR results of BRG1-ChIP from neurospheres. Primers were used to amplify 6 distinct positions along the pri-miR-9-2 gene locus and a genetically sparse region on mouse chromosome 6. Vertical axis shows fold change relative to an IgG pulldown control. Error bars indicate standard error of the mean. (c) qPCR of neurosphere DNA following digestion with 20, 60 and 120U of DNAse I at the 6 positions along the pri-miR-9-2 gene locus. The vertical axis shows fold amplification relative to DNAse I-untreated neurosphere DNA.

    Article Snippet: As described in , nuclear pellets were treated with either 0, 20, 60 or 120U of DNAse I (Ambion/Thermo Fisher Scientific) for one hour on ice.

    Techniques: Binding Assay, Real-time Polymerase Chain Reaction, Chromatin Immunoprecipitation, Amplification