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fluorometer ds 11 fx  (DeNovix)

 
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    DeNovix fluorometer ds 11 fx
    Fluorometer Ds 11 Fx, supplied by DeNovix, used in various techniques. Bioz Stars score: 97/100, based on 1045 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/spectrophotometer+fluorometer/Microvolume+Spectrophotometer+And+Fluorometer+DeNovix+DS-11+FX/pmc13179062-313-8-12
    Average 97 stars, based on 1045 article reviews
    fluorometer ds 11 fx - by Bioz Stars, 2026-08
    97/100 stars

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    a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the <t>absorption</t> at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.
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    a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the <t>absorption</t> at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.
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    rna concentration  (DeNovix)
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    a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the <t>absorption</t> at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.
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    a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the <t>absorption</t> at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.
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    peptide concentration  (DeNovix)
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    DeNovix peptide concentration
    a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the <t>absorption</t> at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.
    Peptide Concentration, supplied by DeNovix, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/spectrophotometer+fluorometer/Microvolume+Spectrophotometer+And+Fluorometer+DeNovix+DS-11+FX/bio_rxiv__64898__2026__04__22__720116-178-0-9
    Average 97 stars, based on 1 article reviews
    peptide concentration - by Bioz Stars, 2026-08
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    Image Search Results


    a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the absorption at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.

    Journal: Nature Communications

    Article Title: Reprogramming of bacterial virulence by lysine acetylation

    doi: 10.1038/s41467-026-72244-8

    Figure Lengend Snippet: a SnCE1 C256A AcK231 is neither deacetylated by human SIRT1 and SIRT2 nor by S. negevensis CobB, i.e., SnCobB. Deacetylation of acetylated wild type SnCE1 and site-specifically acetylated SnCE1 C256A AcK231 was assessed by immunoblotting with anti-acetyl lysine antibody (IB: AcK) and Coomassie Brilliant Blue staining was done as loading control (CBB). The experiment was performed in two independent technical replicates ( n = 2). Source data are provided as Source Data file. b SnCE1 C256A AcK231 elutes as monomer from analytic SEC column. Wild type SnCE1 elutes as monomer, SnCE1 C256A as tetramer. A 280 is the absorption at 280 nm. mAU: milli absorbance units. Fractions were analyzed by SDS-PAGE and gels were stained with Coomassie brilliant blue (CBB), immunoblotting with anti-acetyl-lysine antibody confirms the acetylation (IB: AcK) and staining with anti-SnCE1 antibody was done as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file. c SnCE1 C256A AcK231 is neither deacetylated by human sirtuins (SIRT1-SIRT7) nor by selected human classical HDACs. The acetylation state of SnCE1 was assessed by immunoblotting using an anti-acetyl lysine antibody (IB: AcK). Immunoblotting with anti-SnCE1 antibody served as loading control (IB: SnCE1). The experiment was performed once ( n = 1). Source data are provided as Source Data file.

    Article Snippet: Elution fractions containing pure protein were pooled and concentrated before protein concentration was determined by measuring absorption at 280 nm using a spectrophotometer DS-11 FX (DeNovix, Wilmington USA).

    Techniques: Western Blot, Staining, Control, SDS Page