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    Promega rq1 rnasefree dnase
    Nuclear RNAs triggered FUS oligomerization. ( A ) Addition of <t>RNase</t> A in the mixture of CB and NCB fractions inhibited the oligomerization of FUS. In contrast, <t>DNase</t> did not have any effect on FUS oligomerization. Fifty units per milliliter RNase-free DNase
    Rq1 Rnasefree Dnase, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 1990 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rq1 rnasefree dnase/product/Promega
    Average 99 stars, based on 1990 article reviews
    Price from $9.99 to $1999.99
    rq1 rnasefree dnase - by Bioz Stars, 2020-07
    99/100 stars
      Buy from Supplier

    88
    Promega rq 1 rnase free dnase
    Nuclear RNAs triggered FUS oligomerization. ( A ) Addition of <t>RNase</t> A in the mixture of CB and NCB fractions inhibited the oligomerization of FUS. In contrast, <t>DNase</t> did not have any effect on FUS oligomerization. Fifty units per milliliter RNase-free DNase
    Rq 1 Rnase Free Dnase, supplied by Promega, used in various techniques. Bioz Stars score: 88/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rq 1 rnase free dnase/product/Promega
    Average 88 stars, based on 83 article reviews
    Price from $9.99 to $1999.99
    rq 1 rnase free dnase - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

    Image Search Results


    Nuclear RNAs triggered FUS oligomerization. ( A ) Addition of RNase A in the mixture of CB and NCB fractions inhibited the oligomerization of FUS. In contrast, DNase did not have any effect on FUS oligomerization. Fifty units per milliliter RNase-free DNase

    Journal: Human Molecular Genetics

    Article Title: Subcellular localization and RNAs determine FUS architecture in different cellular compartments

    doi: 10.1093/hmg/ddv239

    Figure Lengend Snippet: Nuclear RNAs triggered FUS oligomerization. ( A ) Addition of RNase A in the mixture of CB and NCB fractions inhibited the oligomerization of FUS. In contrast, DNase did not have any effect on FUS oligomerization. Fifty units per milliliter RNase-free DNase

    Article Snippet: RNase-free DNase (catalog no. M6101) was purchased from Promega.

    Techniques:

    Quality of root-extracted RNA. The analysis of the total RNA extracted from inoculated roots was performed using an Agilent Bioanalyser 2100. One microlitre of RQ1 DNase-treated total RNA was analysed for each sample. The days post-inoculation with Gaeumannomyces graminis var. tritici ( Ggt ) are indicated. M, RNA size marker; lanes 1, 3, 6, 9, RNA from uninfected wheat roots; lanes 2, 4, 7, 10, RNA from wheat roots infected with Ggt ; lanes 5, 8, 11, RNA from wheat roots infected with Ggt and Pf29Arp; lane 12, RNA from soil-borne pathogenic fungus IV-26/00.

    Journal: Molecular Plant Pathology

    Article Title: The biocontrol bacterium Pseudomonas fluorescens Pf29Arp strain affects the pathogenesis-related gene expression of the take-all fungus Gaeumannomyces graminis var. tritici on wheat roots

    doi: 10.1111/j.1364-3703.2011.00715.x

    Figure Lengend Snippet: Quality of root-extracted RNA. The analysis of the total RNA extracted from inoculated roots was performed using an Agilent Bioanalyser 2100. One microlitre of RQ1 DNase-treated total RNA was analysed for each sample. The days post-inoculation with Gaeumannomyces graminis var. tritici ( Ggt ) are indicated. M, RNA size marker; lanes 1, 3, 6, 9, RNA from uninfected wheat roots; lanes 2, 4, 7, 10, RNA from wheat roots infected with Ggt ; lanes 5, 8, 11, RNA from wheat roots infected with Ggt and Pf29Arp; lane 12, RNA from soil-borne pathogenic fungus IV-26/00.

    Article Snippet: Total RNA was extracted from ground tissue in 1 mL of Trizol (Invitrogen, Paisley, Renfrewshire, UK), and contaminating DNA was removed using the RNase-free RQ1 DNase (Promega Corp., Madison, WI, USA) according to the manufacturer's instructions.

    Techniques: Marker, Infection

    A fraction of hsMOK2 protein is associated with nuclear matrix. HeLa cells transfected with CMV-hsMOK2 ( A ), CMV-hsMOK2Δ ( B ) or CMV-NH 2 hsMOK2 ( C ) vectors were sequentially extracted as described in Materials and Methods. The various protein fractions correspond to 1% Triton X-100 (fraction 1), DNase I at 37°C and 0.25 M (NH 4 ) 2 SO 4 (fraction 2), 2 M NaCl (fraction 3), RNase A (fraction 4) and, finally, the pellet containing nuclear matrix (fraction 5) resuspended in SDS sample buffer. Four micrograms of proteins from fractions 1–4 and 20 µg of proteins from fraction 5, corresponding to the nuclear matrix, were subjected to SDS–PAGE and western blot analysis. Probing was realized with polyclonal anti-hsMOK2 antibody to detect hsMOK2 and truncated proteins or monoclonal anti-lamin A/C(636) antibody to detect the two nuclear matrix lamins A and C. Western blots were visualized with a Fluor-S Max MultiImager and quantified with Quantity One software (Bio-Rad). The percentages indicated below each panel were normalized at 4 µg of proteins. The molecular weights of the proteins are indicated on the right.

    Journal: Nucleic Acids Research

    Article Title: In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C

    doi:

    Figure Lengend Snippet: A fraction of hsMOK2 protein is associated with nuclear matrix. HeLa cells transfected with CMV-hsMOK2 ( A ), CMV-hsMOK2Δ ( B ) or CMV-NH 2 hsMOK2 ( C ) vectors were sequentially extracted as described in Materials and Methods. The various protein fractions correspond to 1% Triton X-100 (fraction 1), DNase I at 37°C and 0.25 M (NH 4 ) 2 SO 4 (fraction 2), 2 M NaCl (fraction 3), RNase A (fraction 4) and, finally, the pellet containing nuclear matrix (fraction 5) resuspended in SDS sample buffer. Four micrograms of proteins from fractions 1–4 and 20 µg of proteins from fraction 5, corresponding to the nuclear matrix, were subjected to SDS–PAGE and western blot analysis. Probing was realized with polyclonal anti-hsMOK2 antibody to detect hsMOK2 and truncated proteins or monoclonal anti-lamin A/C(636) antibody to detect the two nuclear matrix lamins A and C. Western blots were visualized with a Fluor-S Max MultiImager and quantified with Quantity One software (Bio-Rad). The percentages indicated below each panel were normalized at 4 µg of proteins. The molecular weights of the proteins are indicated on the right.

    Article Snippet: In brief, transfected HeLa cells were sequentially extracted with: 1% Triton X-100 in TMS buffer (50 mM Tris–HCl pH 7.4, 5 mM MgSO4 , 250 mM sucrose) for 5 min at RT (fraction 1); 50 U/ml RNase-free DNase RQ1 (Promega) in TMS at 37°C for 30 min and adding ammonium sulfate to a final concentration of 0.25 M (fraction 2); 2 M NaCl in TM buffer (10 mM Tris–HCl pH 7.4, 0.02 mM MgSO4 ) twice for 15 min at RT (fraction 3); 50 µg/ml RNase A in TM for 15 min at RT (fraction 4).

    Techniques: Transfection, SDS Page, Western Blot, Software