e coli cell lysates  (New England Biolabs)


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    Structured Review

    New England Biolabs e coli cell lysates
    Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of <t>E.</t> <t>coli</t> 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the <t>E.</t> <t>coli</t> 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.
    E Coli Cell Lysates, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    e coli cell lysates - by Bioz Stars, 2022-07
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    Images

    1) Product Images from "Ribosome inhibition by C9ORF72-ALS/FTD-associated poly-PR and poly-GR proteins revealed by cryo-EM"

    Article Title: Ribosome inhibition by C9ORF72-ALS/FTD-associated poly-PR and poly-GR proteins revealed by cryo-EM

    Journal: Nature Communications

    doi: 10.1038/s41467-022-30418-0

    Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of E. coli 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the E. coli 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.
    Figure Legend Snippet: Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of E. coli 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the E. coli 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.

    Techniques Used: Cryo-EM Sample Prep, Binding Assay, Inhibition

    Inhibition of peptidyl transfer by PR 20 and GR 20 . a Time progress curves of inhibition of puromycin peptide bond formation by different concentrations of PR 20 on E. coli 70S ribosomes ( n = 3 independent experiments). Count per minute (cpm). b Dependence of inhibition of peptide bond formation on the lengths of poly-PR and poly-GR repeats (puromycin assay on E. coli ribosomes; apparent inhibition constants are shown on the y axis; n = 2 independent experiments, error bars are standard error). K i ,app was > 2000 nM (the highest concentration tested) for both PR 4 and GR 4 and is shown as an asterisk. c Time progress curves of inhibition of puromycin peptide bond formation by PR 20 on rabbit 80S ribosomes ( n = 2 independent experiments). Source data are provided as a Source Data file.
    Figure Legend Snippet: Inhibition of peptidyl transfer by PR 20 and GR 20 . a Time progress curves of inhibition of puromycin peptide bond formation by different concentrations of PR 20 on E. coli 70S ribosomes ( n = 3 independent experiments). Count per minute (cpm). b Dependence of inhibition of peptide bond formation on the lengths of poly-PR and poly-GR repeats (puromycin assay on E. coli ribosomes; apparent inhibition constants are shown on the y axis; n = 2 independent experiments, error bars are standard error). K i ,app was > 2000 nM (the highest concentration tested) for both PR 4 and GR 4 and is shown as an asterisk. c Time progress curves of inhibition of puromycin peptide bond formation by PR 20 on rabbit 80S ribosomes ( n = 2 independent experiments). Source data are provided as a Source Data file.

    Techniques Used: Inhibition, Concentration Assay

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    New England Biolabs e coli cell lysates
    Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of <t>E.</t> <t>coli</t> 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the <t>E.</t> <t>coli</t> 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.
    E Coli Cell Lysates, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli cell lysates/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e coli cell lysates - by Bioz Stars, 2022-07
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    New England Biolabs competent e coli cells
    Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of <t>E.</t> <t>coli</t> 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the <t>E.</t> <t>coli</t> 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.
    Competent E Coli Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    competent e coli cells - by Bioz Stars, 2022-07
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    Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of E. coli 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the E. coli 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Ribosome inhibition by C9ORF72-ALS/FTD-associated poly-PR and poly-GR proteins revealed by cryo-EM

    doi: 10.1038/s41467-022-30418-0

    Figure Lengend Snippet: Cryo-EM shows that PR 20 occupies the polypeptide tunnel of the bacterial 70S ribosome. a Overview of the structure of E. coli 70S•PR 20 . b PR 20 binds to the 70S polypeptide exit channel. c PR 20 overlaps with the macrolide antibiotic binding site in the polypeptide tunnel. Erythromycin (Ery; orange) from the E. coli 70S•Ery crystal structure is shown ( PDB:4V7U 87 ). d Preincubation of ribosomes with erythromycin (Ery) relieves the inhibition of peptide bond formation by 2 μM PR 20 , consistent with an overlapping binding site for Ery and PR 20 . n = 2 independent experiments. Source data are provided as a Source Data file.

    Article Snippet: E. coli cell lysates (NEBExpress, NEB) were used to investigate bacterial translation inhibition by GR20 and PR20 .

    Techniques: Cryo-EM Sample Prep, Binding Assay, Inhibition

    Inhibition of peptidyl transfer by PR 20 and GR 20 . a Time progress curves of inhibition of puromycin peptide bond formation by different concentrations of PR 20 on E. coli 70S ribosomes ( n = 3 independent experiments). Count per minute (cpm). b Dependence of inhibition of peptide bond formation on the lengths of poly-PR and poly-GR repeats (puromycin assay on E. coli ribosomes; apparent inhibition constants are shown on the y axis; n = 2 independent experiments, error bars are standard error). K i ,app was > 2000 nM (the highest concentration tested) for both PR 4 and GR 4 and is shown as an asterisk. c Time progress curves of inhibition of puromycin peptide bond formation by PR 20 on rabbit 80S ribosomes ( n = 2 independent experiments). Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Ribosome inhibition by C9ORF72-ALS/FTD-associated poly-PR and poly-GR proteins revealed by cryo-EM

    doi: 10.1038/s41467-022-30418-0

    Figure Lengend Snippet: Inhibition of peptidyl transfer by PR 20 and GR 20 . a Time progress curves of inhibition of puromycin peptide bond formation by different concentrations of PR 20 on E. coli 70S ribosomes ( n = 3 independent experiments). Count per minute (cpm). b Dependence of inhibition of peptide bond formation on the lengths of poly-PR and poly-GR repeats (puromycin assay on E. coli ribosomes; apparent inhibition constants are shown on the y axis; n = 2 independent experiments, error bars are standard error). K i ,app was > 2000 nM (the highest concentration tested) for both PR 4 and GR 4 and is shown as an asterisk. c Time progress curves of inhibition of puromycin peptide bond formation by PR 20 on rabbit 80S ribosomes ( n = 2 independent experiments). Source data are provided as a Source Data file.

    Article Snippet: E. coli cell lysates (NEBExpress, NEB) were used to investigate bacterial translation inhibition by GR20 and PR20 .

    Techniques: Inhibition, Concentration Assay