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  • 99
    New England Biolabs and 10 u bsai
    And 10 U Bsai, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/and 10 u bsai/product/New England Biolabs
    Average 99 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    and 10 u bsai - by Bioz Stars, 2020-09
    99/100 stars
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    98
    Thermo Fisher eco31i
    Construction of MIDGE vectors . (A) POMC exon 2-3 cDNA, encoding the signal peptide, adrenocorticotropic hormone (ACTH), melanocyte-stimulating hormone (MSH) and β-endorphin (END), was spliced into the pMOK plasmid between the SacI and KpnI restriction sites. The pMOK plasmid contains a kanamycin resistance gene, a cytomegalovirus promoter (PCMV), a chimeric intron and simian virus (SV) 40 polyadenylation (pA) site. The POMC-MIDGE-NLS was derived from the pMOK-POMC plasmid by cutting it with <t>Eco31I,</t> ligation with hairpin ODNs at both ends, and coupling of nuclear localization sequence (NLS) to one of the hairpin ODN. The other vectors were prepared analogously by modifying POMC gene as follows: (B) END sequence was removed to obtain control MIDGE-NLS; (C) ACTH and MSH fragments were removed while END sequence was preserved in its original place to obtain 1xEND-MIDGE-NLS encoding 1 copy of END; (D) ACTH fragment was removed, original END sequence was preserved and MSH fragment was replaced with an additional sequence of END to obtain 2xEND-MIDGE-NLS encoding 2 copies of END; (E) original END sequence was preserved and the ACTH and MSH fragments were replaced with additional END sequences to obtain 3xEND-MIDGE-NLS encoding 3 copies of END.
    Eco31i, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 180 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/eco31i/product/Thermo Fisher
    Average 98 stars, based on 180 article reviews
    Price from $9.99 to $1999.99
    eco31i - by Bioz Stars, 2020-09
    98/100 stars
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    99
    Thermo Fisher bsai hf
    Construction of MIDGE vectors . (A) POMC exon 2-3 cDNA, encoding the signal peptide, adrenocorticotropic hormone (ACTH), melanocyte-stimulating hormone (MSH) and β-endorphin (END), was spliced into the pMOK plasmid between the SacI and KpnI restriction sites. The pMOK plasmid contains a kanamycin resistance gene, a cytomegalovirus promoter (PCMV), a chimeric intron and simian virus (SV) 40 polyadenylation (pA) site. The POMC-MIDGE-NLS was derived from the pMOK-POMC plasmid by cutting it with <t>Eco31I,</t> ligation with hairpin ODNs at both ends, and coupling of nuclear localization sequence (NLS) to one of the hairpin ODN. The other vectors were prepared analogously by modifying POMC gene as follows: (B) END sequence was removed to obtain control MIDGE-NLS; (C) ACTH and MSH fragments were removed while END sequence was preserved in its original place to obtain 1xEND-MIDGE-NLS encoding 1 copy of END; (D) ACTH fragment was removed, original END sequence was preserved and MSH fragment was replaced with an additional sequence of END to obtain 2xEND-MIDGE-NLS encoding 2 copies of END; (E) original END sequence was preserved and the ACTH and MSH fragments were replaced with additional END sequences to obtain 3xEND-MIDGE-NLS encoding 3 copies of END.
    Bsai Hf, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bsai hf/product/Thermo Fisher
    Average 99 stars, based on 69 article reviews
    Price from $9.99 to $1999.99
    bsai hf - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    Image Search Results


    Construction of MIDGE vectors . (A) POMC exon 2-3 cDNA, encoding the signal peptide, adrenocorticotropic hormone (ACTH), melanocyte-stimulating hormone (MSH) and β-endorphin (END), was spliced into the pMOK plasmid between the SacI and KpnI restriction sites. The pMOK plasmid contains a kanamycin resistance gene, a cytomegalovirus promoter (PCMV), a chimeric intron and simian virus (SV) 40 polyadenylation (pA) site. The POMC-MIDGE-NLS was derived from the pMOK-POMC plasmid by cutting it with Eco31I, ligation with hairpin ODNs at both ends, and coupling of nuclear localization sequence (NLS) to one of the hairpin ODN. The other vectors were prepared analogously by modifying POMC gene as follows: (B) END sequence was removed to obtain control MIDGE-NLS; (C) ACTH and MSH fragments were removed while END sequence was preserved in its original place to obtain 1xEND-MIDGE-NLS encoding 1 copy of END; (D) ACTH fragment was removed, original END sequence was preserved and MSH fragment was replaced with an additional sequence of END to obtain 2xEND-MIDGE-NLS encoding 2 copies of END; (E) original END sequence was preserved and the ACTH and MSH fragments were replaced with additional END sequences to obtain 3xEND-MIDGE-NLS encoding 3 copies of END.

    Journal: Molecular Pain

    Article Title: Peripheral non-viral MIDGE vector-driven delivery of ?-endorphin in inflammatory pain

    doi: 10.1186/1744-8069-5-72

    Figure Lengend Snippet: Construction of MIDGE vectors . (A) POMC exon 2-3 cDNA, encoding the signal peptide, adrenocorticotropic hormone (ACTH), melanocyte-stimulating hormone (MSH) and β-endorphin (END), was spliced into the pMOK plasmid between the SacI and KpnI restriction sites. The pMOK plasmid contains a kanamycin resistance gene, a cytomegalovirus promoter (PCMV), a chimeric intron and simian virus (SV) 40 polyadenylation (pA) site. The POMC-MIDGE-NLS was derived from the pMOK-POMC plasmid by cutting it with Eco31I, ligation with hairpin ODNs at both ends, and coupling of nuclear localization sequence (NLS) to one of the hairpin ODN. The other vectors were prepared analogously by modifying POMC gene as follows: (B) END sequence was removed to obtain control MIDGE-NLS; (C) ACTH and MSH fragments were removed while END sequence was preserved in its original place to obtain 1xEND-MIDGE-NLS encoding 1 copy of END; (D) ACTH fragment was removed, original END sequence was preserved and MSH fragment was replaced with an additional sequence of END to obtain 2xEND-MIDGE-NLS encoding 2 copies of END; (E) original END sequence was preserved and the ACTH and MSH fragments were replaced with additional END sequences to obtain 3xEND-MIDGE-NLS encoding 3 copies of END.

    Article Snippet: The product was cut with Eco31I and SacI, ligated and cloned into the pMOK-POMC1xEND plasmid after digestion with SacI and BpiI (Fermentas).

    Techniques: Plasmid Preparation, Derivative Assay, Ligation, Sequencing

    Functional characteristics of primary Eco31I mutants. (A.) DNA-binding, (B.) DNA restriction activity (invert image)

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Functional characteristics of primary Eco31I mutants. (A.) DNA-binding, (B.) DNA restriction activity (invert image)

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: Functional Assay, Binding Assay, Activity Assay

    Gel-filtration of Eco31I and its complexes with DNA

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Gel-filtration of Eco31I and its complexes with DNA

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: Filtration

    Reaction courses of Eco31I variants on plasmid DNA substrates (invert images)

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Reaction courses of Eco31I variants on plasmid DNA substrates (invert images)

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: Plasmid Preparation

    Model of the ‘His-Me finger’ structure and the HNH-like active site of Eco31I (residues 271-354)

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Model of the ‘His-Me finger’ structure and the HNH-like active site of Eco31I (residues 271-354)

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques:

    Restriction activity of site-directed Eco31I variants on pBR322 (invert image)

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Restriction activity of site-directed Eco31I variants on pBR322 (invert image)

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: Activity Assay

    Restriction activity of secondary Eco31I mutants on λ DNA and pBR322 (invert images)

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Restriction activity of secondary Eco31I mutants on λ DNA and pBR322 (invert images)

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: Activity Assay

    Run-off sequencing to determine the nicking activity of Eco31I-N334D

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Run-off sequencing to determine the nicking activity of Eco31I-N334D

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: Sequencing, Activity Assay

    Alignment of Eco31I and related REases recognizing a common pentanucleotide GTCTC

    Journal:

    Article Title: Identification of a single HNH active site in Type IIS restriction endonuclease Eco31I

    doi: 10.1016/j.jmb.2007.04.049

    Figure Lengend Snippet: Alignment of Eco31I and related REases recognizing a common pentanucleotide GTCTC

    Article Snippet: The conditions for testing restriction activity of purified Eco31I mutant proteins and determination of their strand specificity were as follows: 20 nM of plasmid DNA and a particular amount of enzyme were incubated in G+ buffer (Fermentas) in total 70 μl volumes at 37°C.

    Techniques: