neb 5 alpha competent e coli high efficiency  (New England Biolabs)


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    New England Biolabs neb 5 alpha competent e coli high efficiency
    Neb 5 Alpha Competent E Coli High Efficiency, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/neb 5 alpha competent e coli high efficiency/product/New England Biolabs
    Average 98 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    neb 5 alpha competent e coli high efficiency - by Bioz Stars, 2022-08
    98/100 stars

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    New England Biolabs t7 express lysy iq competent e coli high efficiency
    Purification of RNase I (6×His) and RNase activity assay. (A) Purification of RNase I (6×His) from Nickel-NTA agarose column. Lane 1, RNase I (6×His) pooled fractions from a nickel column (purified from <t>T7</t> Express cell extract). Arrows indicate the cytoplasmic RNase I precursor (cRNase I) with the signal peptide (predicted MW 30.7 kDa), and the periplasmic RNase I with the signal peptide removed (predicted MW 27.0 kDa). (B) RNase activity on a FAM-labeled SARS-CoV-2 RNA (50 mer). S = substrate; P = cleavage product(s). Positive controls, 50 and 5 U of RNase I f (NEB). RNase I (6×His) enzyme titration (2 μg to 25 ng protein) was used in the activity assay to digest fixed amount of RNA (16 nM) in NEB buffer 3 at 37°C for 1 h. Proteinase K (1.6 U) was added to remove RNase I. The final cleavage products were analyzed by capillary electrophoresis (CE), and peaks were visualized by PeakScan.
    T7 Express Lysy Iq Competent E Coli High Efficiency, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t7 express lysy iq competent e coli high efficiency/product/New England Biolabs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    t7 express lysy iq competent e coli high efficiency - by Bioz Stars, 2022-08
    86/100 stars
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    Purification of RNase I (6×His) and RNase activity assay. (A) Purification of RNase I (6×His) from Nickel-NTA agarose column. Lane 1, RNase I (6×His) pooled fractions from a nickel column (purified from T7 Express cell extract). Arrows indicate the cytoplasmic RNase I precursor (cRNase I) with the signal peptide (predicted MW 30.7 kDa), and the periplasmic RNase I with the signal peptide removed (predicted MW 27.0 kDa). (B) RNase activity on a FAM-labeled SARS-CoV-2 RNA (50 mer). S = substrate; P = cleavage product(s). Positive controls, 50 and 5 U of RNase I f (NEB). RNase I (6×His) enzyme titration (2 μg to 25 ng protein) was used in the activity assay to digest fixed amount of RNA (16 nM) in NEB buffer 3 at 37°C for 1 h. Proteinase K (1.6 U) was added to remove RNase I. The final cleavage products were analyzed by capillary electrophoresis (CE), and peaks were visualized by PeakScan.

    Journal: Frontiers in Microbiology

    Article Title: Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein, E. coli Ribonuclease I and Human RNase A

    doi: 10.3389/fmicb.2021.660149

    Figure Lengend Snippet: Purification of RNase I (6×His) and RNase activity assay. (A) Purification of RNase I (6×His) from Nickel-NTA agarose column. Lane 1, RNase I (6×His) pooled fractions from a nickel column (purified from T7 Express cell extract). Arrows indicate the cytoplasmic RNase I precursor (cRNase I) with the signal peptide (predicted MW 30.7 kDa), and the periplasmic RNase I with the signal peptide removed (predicted MW 27.0 kDa). (B) RNase activity on a FAM-labeled SARS-CoV-2 RNA (50 mer). S = substrate; P = cleavage product(s). Positive controls, 50 and 5 U of RNase I f (NEB). RNase I (6×His) enzyme titration (2 μg to 25 ng protein) was used in the activity assay to digest fixed amount of RNA (16 nM) in NEB buffer 3 at 37°C for 1 h. Proteinase K (1.6 U) was added to remove RNase I. The final cleavage products were analyzed by capillary electrophoresis (CE), and peaks were visualized by PeakScan.

    Article Snippet: The protein expression level was evaluated in four T7 expression strains: T7 Express (C2566, NEB), T7 Express with LysY and lacI q (C3013, NEB), T7 SHuffle (C3026, E. coli K strain, NEB), and Nico (λDE3) with reduced histidine-rich background proteins (NEB).

    Techniques: Purification, Activity Assay, Nickel Column, Labeling, Titration, Electrophoresis

    Expression and purification of E. coli RNase III and RNase activity assay on dsRNA. (A) RNase III expression level in three E. coli T7 strains: T7 Shuffle (C3026, K strain), T7 Express with lacI q and LysY (C3013), and Nico (λDE3). (B) Purified RNase III from nickel-NTA agarose column chromatography and Ni magnetic beads. (C) Ribonuclease activity assay on dsRNA (40 mer duplex and dsRNA ladder).

    Journal: Frontiers in Microbiology

    Article Title: Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein, E. coli Ribonuclease I and Human RNase A

    doi: 10.3389/fmicb.2021.660149

    Figure Lengend Snippet: Expression and purification of E. coli RNase III and RNase activity assay on dsRNA. (A) RNase III expression level in three E. coli T7 strains: T7 Shuffle (C3026, K strain), T7 Express with lacI q and LysY (C3013), and Nico (λDE3). (B) Purified RNase III from nickel-NTA agarose column chromatography and Ni magnetic beads. (C) Ribonuclease activity assay on dsRNA (40 mer duplex and dsRNA ladder).

    Article Snippet: The protein expression level was evaluated in four T7 expression strains: T7 Express (C2566, NEB), T7 Express with LysY and lacI q (C3013, NEB), T7 SHuffle (C3026, E. coli K strain, NEB), and Nico (λDE3) with reduced histidine-rich background proteins (NEB).

    Techniques: Expressing, Purification, Activity Assay, Column Chromatography, Magnetic Beads

    Expression of hRNase A-ACE2NTD150 in T7 Express LysY/ lacI q (C3013). (A) Schematic diagram of the fusion protein. (B) SDS-PAGE analysis of five isolates of hRNase A-ACE2NTD150 (five isolates with MBP signal peptide, five clones without MBP signal peptide). Total cell lysate of pET21b serves as a negative control. (C,D) Western blot analysis of the fusion proteins (soluble fraction/supernatant) by anti-His mAb and anti-ACE2 mAb.

    Journal: Frontiers in Microbiology

    Article Title: Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein, E. coli Ribonuclease I and Human RNase A

    doi: 10.3389/fmicb.2021.660149

    Figure Lengend Snippet: Expression of hRNase A-ACE2NTD150 in T7 Express LysY/ lacI q (C3013). (A) Schematic diagram of the fusion protein. (B) SDS-PAGE analysis of five isolates of hRNase A-ACE2NTD150 (five isolates with MBP signal peptide, five clones without MBP signal peptide). Total cell lysate of pET21b serves as a negative control. (C,D) Western blot analysis of the fusion proteins (soluble fraction/supernatant) by anti-His mAb and anti-ACE2 mAb.

    Article Snippet: The protein expression level was evaluated in four T7 expression strains: T7 Express (C2566, NEB), T7 Express with LysY and lacI q (C3013, NEB), T7 SHuffle (C3026, E. coli K strain, NEB), and Nico (λDE3) with reduced histidine-rich background proteins (NEB).

    Techniques: Expressing, SDS Page, Clone Assay, Negative Control, Western Blot