dnasei  (Millipore)

 
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    Name:
    DNase I
    Description:
    Deoxyribonuclease I DNase I is an endonuclease isolated from bovine pancreas that digests double and single stranded DNA into oligo and mononucleotides Amplification Grade DNase I has been purified to remove RNase activity and is suitable for eliminating DNA from RNA preparations prior to sensitive applications such as RT PCR Reverse Transcriptase Polymerase Chain Reaction DNase I digests double and single stranded DNA into oligo and mononucleotides Using the Reaction Buffer provided DNA is removed from RNA preparations in a 15 minute digestion at room temperature The DNase I is then inactivated by heating with the Stop Solution Heating also denatures hairpins in the RNA so the RNA can be used directly in reverse transcription No current RNA isolation procedure removes 100 of the DNA Many commercial DNase I formulations are contaminated with residual RNases This RNase contamination can destroy or degrade valuable RNA samples prior to reverse transcription Laboratory comparisons have shown that Sigma s Amplification Grade DNase I demonstrates lower RNase activity than that from several leading molecular biology product suppliers
    Catalog Number:
    AMPD1
    Price:
    None
    Applications:
    Amplification grade DNase I has been used for the digestion of DNA during isolation and purification of RNA. The purified RNA can be used for the synthesis of cDNA using RNA reverse transcriptase.
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    Structured Review

    Millipore dnasei
    DNase I
    Deoxyribonuclease I DNase I is an endonuclease isolated from bovine pancreas that digests double and single stranded DNA into oligo and mononucleotides Amplification Grade DNase I has been purified to remove RNase activity and is suitable for eliminating DNA from RNA preparations prior to sensitive applications such as RT PCR Reverse Transcriptase Polymerase Chain Reaction DNase I digests double and single stranded DNA into oligo and mononucleotides Using the Reaction Buffer provided DNA is removed from RNA preparations in a 15 minute digestion at room temperature The DNase I is then inactivated by heating with the Stop Solution Heating also denatures hairpins in the RNA so the RNA can be used directly in reverse transcription No current RNA isolation procedure removes 100 of the DNA Many commercial DNase I formulations are contaminated with residual RNases This RNase contamination can destroy or degrade valuable RNA samples prior to reverse transcription Laboratory comparisons have shown that Sigma s Amplification Grade DNase I demonstrates lower RNase activity than that from several leading molecular biology product suppliers
    https://www.bioz.com/result/dnasei/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dnasei - by Bioz Stars, 2021-04
    99/100 stars

    Images

    1) Product Images from "DNase-Sensitive and -Resistant Modes of Biofilm Formation by Listeria monocytogenes"

    Article Title: DNase-Sensitive and -Resistant Modes of Biofilm Formation by Listeria monocytogenes

    Journal: Frontiers in Microbiology

    doi: 10.3389/fmicb.2015.01428

    Biofilm formation of Lm EGD-e grown in 0.1BHI prepared with either dH 2 O, PBS, phosphate buffer (PB), or saline (S) grown at 25°C (A) or 37°C (B) in the presence (gray bars) or absence (black bars) of DNaseI. Values are absorbance at 562 nm and are mean ± standard deviation of three independent experiments. Data was analyzed using Student’s t -test and p -values of statistically significant differences are indicated (all other comparisons: not significant, i.e., p > 0.05).
    Figure Legend Snippet: Biofilm formation of Lm EGD-e grown in 0.1BHI prepared with either dH 2 O, PBS, phosphate buffer (PB), or saline (S) grown at 25°C (A) or 37°C (B) in the presence (gray bars) or absence (black bars) of DNaseI. Values are absorbance at 562 nm and are mean ± standard deviation of three independent experiments. Data was analyzed using Student’s t -test and p -values of statistically significant differences are indicated (all other comparisons: not significant, i.e., p > 0.05).

    Techniques Used: Standard Deviation

    2) Product Images from "A poly(ethylene) glycolylated peptide for ocular delivery compacts DNA into nanoparticles for gene delivery to post-mitotic tissues in vivo"

    Article Title: A poly(ethylene) glycolylated peptide for ocular delivery compacts DNA into nanoparticles for gene delivery to post-mitotic tissues in vivo

    Journal: The journal of gene medicine

    doi: 10.1002/jgm.1415

    PEG-POD compacted DNA nanoparticles have reduced aggregation and increased protection against DNaseI. (a) Rhodamine-labeled DNA was complexed with c-POD or PEG-POD and added to HER cells in culture and observed after 24 h. c-POD/DNA complexes form large aggregates in cell culture while PEG-POD/Rhodamine labeled DNA nanoparticles showed a diffuse punctate pattern across cells. Scale bar = 50 µm. (b) In the absence of pronase, plasmid migration was inhibited by the compaction of the PEG-POD~Luc nanoparticles. Nanoparticle DNA was released following a 10-min pronase incubation. Treatment with a low (0.25 U) or high (2.5 U) dose of DNaseI led to partial and complete digestion of pCAGLuc, respectively. However, PEG-POD nanoparticles remained largely intact under both conditions
    Figure Legend Snippet: PEG-POD compacted DNA nanoparticles have reduced aggregation and increased protection against DNaseI. (a) Rhodamine-labeled DNA was complexed with c-POD or PEG-POD and added to HER cells in culture and observed after 24 h. c-POD/DNA complexes form large aggregates in cell culture while PEG-POD/Rhodamine labeled DNA nanoparticles showed a diffuse punctate pattern across cells. Scale bar = 50 µm. (b) In the absence of pronase, plasmid migration was inhibited by the compaction of the PEG-POD~Luc nanoparticles. Nanoparticle DNA was released following a 10-min pronase incubation. Treatment with a low (0.25 U) or high (2.5 U) dose of DNaseI led to partial and complete digestion of pCAGLuc, respectively. However, PEG-POD nanoparticles remained largely intact under both conditions

    Techniques Used: Labeling, Cell Culture, Plasmid Preparation, Migration, Incubation

    Related Articles

    Mouse Assay:

    Article Title: Neutrophil extracellular traps promote lipopolysaccharide-induced airway inflammation and mucus hypersecretion in mice
    Article Snippet: Animal exposure to LPS and DNase I administration LPS (Escherichia coli 0111:B4; Sigma-Aldrich, St. Louis, MO) was diluted in saline at a dose of 2 mg/50μL and injected into trachea with a microsyringe when mice were under anesthesia; sham-treated mice were given normal saline (NS) alone, described previously [ ]. .. To investigate the role of DNase I on airway inflammation and mucus hypersecretion, mice received aerosolized DNase I (Sigma-Aldrich) 120 U diluted in 5mL NS at 4 and 12 hours after LPS injection through an atomization inhaler. .. Mice were killed 24 hours after LPS injection.

    Injection:

    Article Title: Neutrophil extracellular traps promote lipopolysaccharide-induced airway inflammation and mucus hypersecretion in mice
    Article Snippet: Animal exposure to LPS and DNase I administration LPS (Escherichia coli 0111:B4; Sigma-Aldrich, St. Louis, MO) was diluted in saline at a dose of 2 mg/50μL and injected into trachea with a microsyringe when mice were under anesthesia; sham-treated mice were given normal saline (NS) alone, described previously [ ]. .. To investigate the role of DNase I on airway inflammation and mucus hypersecretion, mice received aerosolized DNase I (Sigma-Aldrich) 120 U diluted in 5mL NS at 4 and 12 hours after LPS injection through an atomization inhaler. .. Mice were killed 24 hours after LPS injection.

    Nucleic Acid Electrophoresis:

    Article Title: A viral genome packaging ring-ATPase is a flexibly coordinated pentamer
    Article Snippet: The purified gp17 protein (~1.5 μM) was incubated with empty capsids purified as above (~2 × 1010 particles) and DNA [300 ng of 50- to 766-bp ladder DNA (New England Biolabs, Ipswich, MA) or linearized 2.8-kb or 6-kb plasmid DNA], and packaging buffer containing 30 mM Tris–HCl (pH 7.5), 100 mM NaCl, 3 mM MgCl2, and 1 mM ATP for 5 min of short time incubation, or for 30 min of long time incubation at 37°C. .. Unpackaged DNA was degraded by adding DNase I (Sigma-Aldrich) by incubating this mixture for 30 min at 37°C, and the encapsidated DNase-I-resistant DNA was released by treatment with proteinase K. The retrieved encapsidated DNA was then analyzed by polyacrylamide (4–20% gradient) or agarose (0.8%) gel electrophoresis. ..

    Incubation:

    Article Title: Obesity Risk Gene TMEM18 Encodes a Sequence-Specific DNA-Binding Protein
    Article Snippet: TMEM18 was detected by Western blot with Anti-Flag antibody (F3165, Sigma). .. Dnase I treatment of the matrix was done as follows: the matrix was washed three times with 10 mM Tris pH 7.5, 0.2 M NaCl and incubated with 10 mg/ml of Dnase I (Sigma) in 10 mM Hepes pH 7.9, 10 mM KCl, 1.5 mM MgCl2 for 15 minutes at room temperature (RT). ..

    Article Title: Ablation of Ggnbp2 impairs meiotic DNA double‐strand break repair during spermatogenesis in mice, et al. Ablation of Ggnbp2 impairs meiotic DNA double‐strand break repair during spermatogenesis in mice
    Article Snippet: All RT‐PCR primers, as listed in Table , were designed according to the sequences obtained from GenBank and synthesized by Operon Technologies (Alameda, CA, USA). .. Dispersed testicular germ cells were prepared by incubation of the seminiferous tubules in PBS supplemented with 0.5% bovine serum albumin, 2 mg/mL collagenase, 0.1 μg/mL DNase I and 0.5% trypsin (Sigma) for 10 minutes at 32°C. ..

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    Millipore dnasei
    CmDnm2 Associates with Chloroplasts Only during the Division Phase. Immunoblot analyses using anti-CmDnm2 antibodies. Twenty micrograms of protein in each sample was separated in each lane, except for in (C) , in which samples were obtained from isolated chloroplasts containing 100 μg of protein. (A) Total protein from synchronized M-phase cells was blotted with preimmune antisera or anti-CmDnm2 antibodies. (B) and (C) Dividing chloroplasts were isolated from M-phase synchronous culture (B) and fractionated further into the pellet (P) and supernatant (S) by osmotic bursting or treatment with 0.5% <t>Nonidet</t> P-40 and 0.1 mg/mL <t>DNaseI</t> and then centrifugation (C) . (D) Aliquots of the synchronous culture were collected at the indicated times, and total proteins were separated. 5-Flurodeoxyuridine (FdU) was added to the culture at a concentration of 10 μg/mL at 2 h before the onset of the second dark period. The cell cycle was arrested at S-phase by 5-flurodeoxyuridine, whereas chloroplast division occurred continuously, producing four or eight chloroplasts per cell.
    Dnasei, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnasei/product/Millipore
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dnasei - by Bioz Stars, 2021-04
    95/100 stars
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    CmDnm2 Associates with Chloroplasts Only during the Division Phase. Immunoblot analyses using anti-CmDnm2 antibodies. Twenty micrograms of protein in each sample was separated in each lane, except for in (C) , in which samples were obtained from isolated chloroplasts containing 100 μg of protein. (A) Total protein from synchronized M-phase cells was blotted with preimmune antisera or anti-CmDnm2 antibodies. (B) and (C) Dividing chloroplasts were isolated from M-phase synchronous culture (B) and fractionated further into the pellet (P) and supernatant (S) by osmotic bursting or treatment with 0.5% Nonidet P-40 and 0.1 mg/mL DNaseI and then centrifugation (C) . (D) Aliquots of the synchronous culture were collected at the indicated times, and total proteins were separated. 5-Flurodeoxyuridine (FdU) was added to the culture at a concentration of 10 μg/mL at 2 h before the onset of the second dark period. The cell cycle was arrested at S-phase by 5-flurodeoxyuridine, whereas chloroplast division occurred continuously, producing four or eight chloroplasts per cell.

    Journal: The Plant Cell

    Article Title: A Plant-Specific Dynamin-Related Protein Forms a Ring at the Chloroplast Division Site

    doi: 10.1105/tpc.009373

    Figure Lengend Snippet: CmDnm2 Associates with Chloroplasts Only during the Division Phase. Immunoblot analyses using anti-CmDnm2 antibodies. Twenty micrograms of protein in each sample was separated in each lane, except for in (C) , in which samples were obtained from isolated chloroplasts containing 100 μg of protein. (A) Total protein from synchronized M-phase cells was blotted with preimmune antisera or anti-CmDnm2 antibodies. (B) and (C) Dividing chloroplasts were isolated from M-phase synchronous culture (B) and fractionated further into the pellet (P) and supernatant (S) by osmotic bursting or treatment with 0.5% Nonidet P-40 and 0.1 mg/mL DNaseI and then centrifugation (C) . (D) Aliquots of the synchronous culture were collected at the indicated times, and total proteins were separated. 5-Flurodeoxyuridine (FdU) was added to the culture at a concentration of 10 μg/mL at 2 h before the onset of the second dark period. The cell cycle was arrested at S-phase by 5-flurodeoxyuridine, whereas chloroplast division occurred continuously, producing four or eight chloroplasts per cell.

    Article Snippet: Isolated dividing chloroplasts were lysed at a concentration of 1 mg total protein/mL in Suc-free isolation medium with or without 0.5% Nonidet P-40 and 0.1 mg/mL DNaseI (D4527; Sigma) for 1 h on ice.

    Techniques: Isolation, Centrifugation, Concentration Assay