lysine acetylation Search Results


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  • 94
    NSJ Bioreagents h3k56ac antibody / acetyl histone h3 lysine 56
    H3k56ac Antibody / Acetyl Histone H3 Lysine 56, supplied by NSJ Bioreagents, 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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    95
    Cell Signaling Technology Inc anti acetyllysine antibody bead conjugated ptmscan acetyl lysine motif
    Inactivation of the two known acetylation mechanisms in E. coli eliminates the majority of acetylation. Wild-type (WT) E. coli (strain BW25113) and an isogenic Δ pta yfiQ acs cobB mutant (Gutted) were aerated in TB7 supplemented with 0.4% glucose for 10 h. Whole-cell lysates were analyzed (A) by Coomassie blue-stained SDS-polyacrylamide gel to ensure equivalent loading and (B) by <t>anti-acetyllysine</t> Western blotting.
    Anti Acetyllysine Antibody Bead Conjugated Ptmscan Acetyl Lysine Motif, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Cell Signaling Technology Inc acetyl lysine
    Inactivation of the two known acetylation mechanisms in E. coli eliminates the majority of acetylation. Wild-type (WT) E. coli (strain BW25113) and an isogenic Δ pta yfiQ acs cobB mutant (Gutted) were aerated in TB7 supplemented with 0.4% glucose for 10 h. Whole-cell lysates were analyzed (A) by Coomassie blue-stained SDS-polyacrylamide gel to ensure equivalent loading and (B) by <t>anti-acetyllysine</t> Western blotting.
    Acetyl Lysine, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Cell Signaling Technology Inc anti acetyl lysine antibody
    Inactivation of the two known acetylation mechanisms in E. coli eliminates the majority of acetylation. Wild-type (WT) E. coli (strain BW25113) and an isogenic Δ pta yfiQ acs cobB mutant (Gutted) were aerated in TB7 supplemented with 0.4% glucose for 10 h. Whole-cell lysates were analyzed (A) by Coomassie blue-stained SDS-polyacrylamide gel to ensure equivalent loading and (B) by <t>anti-acetyllysine</t> Western blotting.
    Anti Acetyl Lysine Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti acetyl lysine antibody/product/Cell Signaling Technology Inc
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    95
    Cell Signaling Technology Inc icp0380
    Inactivation of the two known acetylation mechanisms in E. coli eliminates the majority of acetylation. Wild-type (WT) E. coli (strain BW25113) and an isogenic Δ pta yfiQ acs cobB mutant (Gutted) were aerated in TB7 supplemented with 0.4% glucose for 10 h. Whole-cell lysates were analyzed (A) by Coomassie blue-stained SDS-polyacrylamide gel to ensure equivalent loading and (B) by <t>anti-acetyllysine</t> Western blotting.
    Icp0380, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Inactivation of the two known acetylation mechanisms in E. coli eliminates the majority of acetylation. Wild-type (WT) E. coli (strain BW25113) and an isogenic Δ pta yfiQ acs cobB mutant (Gutted) were aerated in TB7 supplemented with 0.4% glucose for 10 h. Whole-cell lysates were analyzed (A) by Coomassie blue-stained SDS-polyacrylamide gel to ensure equivalent loading and (B) by anti-acetyllysine Western blotting.

    Journal: mBio

    Article Title: Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli

    doi: 10.1128/mBio.01905-18

    Figure Lengend Snippet: Inactivation of the two known acetylation mechanisms in E. coli eliminates the majority of acetylation. Wild-type (WT) E. coli (strain BW25113) and an isogenic Δ pta yfiQ acs cobB mutant (Gutted) were aerated in TB7 supplemented with 0.4% glucose for 10 h. Whole-cell lysates were analyzed (A) by Coomassie blue-stained SDS-polyacrylamide gel to ensure equivalent loading and (B) by anti-acetyllysine Western blotting.

    Article Snippet: Acetylated peptides were enriched using 1/4 tube of the anti-acetyllysine antibody-bead-conjugated PTMScan Acetyl-Lysine Motif [Ac-K] kit (Cell Signaling Technologies) for each of the 1-mg protein lysate samples according to the manufacturer’s instructions.

    Techniques: Mutagenesis, Staining, Western Blot

    Overexpression of five GNAT family members results in altered lysine acetylation patterns by anti-acetyllysine Western blotting. The gutted strain (BW25113 Δ pta yfiQ acs cobB ) was transformed with the pCA24n vector control (negative [−] control) or pCA24n containing the indicated genes under an IPTG-inducible promoter . As a positive (+) control, an isogenic strain that retained the WT allele of acs (Δ pta yfiQ cobB ) was transformed with pCA24n containing YfiQ. The resulting strains were aerated in TB7 supplemented with 0.4% glucose, 50 μM IPTG, and 25 μg/ml chloramphenicol for 10 h. Whole-cell lysates were analyzed (right panels) by Coomassie blue-stained SDS-polyacrylamide gel electrophoresis to ensure equivalent loading and (left panels) by anti-acetyllysine Western blotting. Note that the band in RimJ was not reproducible. The positive control contains one additional YfiQ-dependent band around 72 kDa, which corresponds to Acs . YncA and AstA each produce an acetylated band that can be observed in the Coomassie blue-stained gel at the expected molecular weight of these proteins.

    Journal: mBio

    Article Title: Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli

    doi: 10.1128/mBio.01905-18

    Figure Lengend Snippet: Overexpression of five GNAT family members results in altered lysine acetylation patterns by anti-acetyllysine Western blotting. The gutted strain (BW25113 Δ pta yfiQ acs cobB ) was transformed with the pCA24n vector control (negative [−] control) or pCA24n containing the indicated genes under an IPTG-inducible promoter . As a positive (+) control, an isogenic strain that retained the WT allele of acs (Δ pta yfiQ cobB ) was transformed with pCA24n containing YfiQ. The resulting strains were aerated in TB7 supplemented with 0.4% glucose, 50 μM IPTG, and 25 μg/ml chloramphenicol for 10 h. Whole-cell lysates were analyzed (right panels) by Coomassie blue-stained SDS-polyacrylamide gel electrophoresis to ensure equivalent loading and (left panels) by anti-acetyllysine Western blotting. Note that the band in RimJ was not reproducible. The positive control contains one additional YfiQ-dependent band around 72 kDa, which corresponds to Acs . YncA and AstA each produce an acetylated band that can be observed in the Coomassie blue-stained gel at the expected molecular weight of these proteins.

    Article Snippet: Acetylated peptides were enriched using 1/4 tube of the anti-acetyllysine antibody-bead-conjugated PTMScan Acetyl-Lysine Motif [Ac-K] kit (Cell Signaling Technologies) for each of the 1-mg protein lysate samples according to the manufacturer’s instructions.

    Techniques: Over Expression, Western Blot, Transformation Assay, Plasmid Preparation, Negative Control, Positive Control, Staining, Polyacrylamide Gel Electrophoresis, Molecular Weight

    Mutation of conserved catalytic amino acids prevents RimI-, PhnO-, YjaB-, and YiaC-dependent acetylation. The gutted strain (BW25113 Δ pta yfiQ acs cobB ) was transformed with the pCA24n vector control, pCA24n carrying the wild-type allele for each putative KAT, or mutant alleles for each putative KAT with alanine substitutions of the indicated residues. The resulting strains were grown in TB7 supplemented with 0.4% glucose, 100 μM IPTG, and 25 μg/ml chloramphenicol for 8 h. Crude lysates harvested after 4 h were analyzed for expression of the KAT proteins. Whole-cell lysates harvested after 8 h were analyzed for acetylation. Coomassie blue-stained SDS-PAGE gels (A and C) served as loading controls for anti-His (B) and anti-acetyllysine (D) Western blot analysis.

    Journal: mBio

    Article Title: Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli

    doi: 10.1128/mBio.01905-18

    Figure Lengend Snippet: Mutation of conserved catalytic amino acids prevents RimI-, PhnO-, YjaB-, and YiaC-dependent acetylation. The gutted strain (BW25113 Δ pta yfiQ acs cobB ) was transformed with the pCA24n vector control, pCA24n carrying the wild-type allele for each putative KAT, or mutant alleles for each putative KAT with alanine substitutions of the indicated residues. The resulting strains were grown in TB7 supplemented with 0.4% glucose, 100 μM IPTG, and 25 μg/ml chloramphenicol for 8 h. Crude lysates harvested after 4 h were analyzed for expression of the KAT proteins. Whole-cell lysates harvested after 8 h were analyzed for acetylation. Coomassie blue-stained SDS-PAGE gels (A and C) served as loading controls for anti-His (B) and anti-acetyllysine (D) Western blot analysis.

    Article Snippet: Acetylated peptides were enriched using 1/4 tube of the anti-acetyllysine antibody-bead-conjugated PTMScan Acetyl-Lysine Motif [Ac-K] kit (Cell Signaling Technologies) for each of the 1-mg protein lysate samples according to the manufacturer’s instructions.

    Techniques: Mutagenesis, Transformation Assay, Plasmid Preparation, Expressing, Staining, SDS Page, Western Blot