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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 1081 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ds+11+fx+spectrophotometer/Microvolume+Spectrophotometer+And+Fluorometer+DeNovix+DS-11+FX/pmc13179062-313-8-12
Average 97 stars, based on 1081 article reviews
fluorometer ds 11 fx - by Bioz Stars, 2026-10
97/100 stars

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Concentration Assay:

Article Title: Enhanced Bioactivity of Puerariae Radix‐ Hovenia Seed Extracts Through Lactiplantibacillus plantarum and Lacticaseibacillus paracasei Co‐Fermentation: Impact on Alcoholic Liver Injury and Macrophage Polarization
Article Snippet: Liver tissue was homogenized in TRIzol reagent, and total RNA was extracted using the RNAsimple Total RNA Kit (Tiangen, China). .. RNA concentration was measured using a DS‐11 FX+ spectrophotometer (DeNovix, USA). .. The extracted RNA was then reverse‐transcribed into cDNA using the TransScript One‐Step gDNA Removal and cDNA Synthesis SuperMix (TransGen, China).

Article Title: Regorafenib-Induced Stress Response Alters the Bioenergetic Profile of Osteosarcoma Cells and Modulates Gene Expression Associated with Metabolic regulation-a Potential Mechanism of Osteosarcoma Treatment-Related Adaptation
Article Snippet: Total RNA was extracted using 1 mL of TRI Reagent (Sigma Aldrich/Merck, Poznań, Poland) following the manufacturer’s protocol. .. The isolated RNA was diluted in nuclease-free water (Sigma Aldrich/Merck, Poznań, Poland), and its concentration and purity were assessed spectrophotometrically at 260 and 280 nm using a DS-11 Fx spectrophotometer (Denovix, Wilmington, DE, USA). .. To ensure RNA integrity, DNase I digestion using PrecisionDNAse kit (PrimerDesign, BLIRT S.A., Gdańsk, Poland) was performed prior to reverse transcription; 500 ng of total RNA was used to detect mRNAs, and 375 ng was used to detect noncoding RNAs. cDNA synthesis was carried out with the Tetro cDNA Synthesis Kit (Bioline Reagents Limited, London, UK) or Mir-XTM miRNA First-Strand Synthesis Kit (Takara Clontech Laboratories, Biokom, Poznań, Poland) according to the manufacturer’s instructions in a T100 Thermal Cycler (Bio-Rad, Hercules, CA, USA).

Spectrophotometry:

Article Title: Enhanced Bioactivity of Puerariae Radix‐ Hovenia Seed Extracts Through Lactiplantibacillus plantarum and Lacticaseibacillus paracasei Co‐Fermentation: Impact on Alcoholic Liver Injury and Macrophage Polarization
Article Snippet: Liver tissue was homogenized in TRIzol reagent, and total RNA was extracted using the RNAsimple Total RNA Kit (Tiangen, China). .. RNA concentration was measured using a DS‐11 FX+ spectrophotometer (DeNovix, USA). .. The extracted RNA was then reverse‐transcribed into cDNA using the TransScript One‐Step gDNA Removal and cDNA Synthesis SuperMix (TransGen, China).

Article Title: Efficacy of Selected Commercial Bio‐Products in Disrupting Symbiont Acquisition and Survival of <i>Halyomorpha halys</i> (Hemiptera: Pentatomidae)
Article Snippet: To estimate the quantitative differences of P. carbekii in dead and surviving nymphs, RNA was extracted using NucleoZOL (Macherey- Nagel, Düren, Germany) RNA isolation buffer following the manufacturer's instructions. .. The extracted RNA was quantified using a DS- 11 FX+ spectrophotometer (Denovix Inc., Wilmington, DE, USA) and treated with DNase I (Thermo Fisher Scientific, Waltham, MA, USA) to remove genomic DNA contamination. .. Complementary DNA (cDNA) synthesis was performed using the iScript cDNA Synthesis Kit (Bio- Rad, Hercules, CA, USA).

Article Title: To multicellularity and back again: Description of two new coccoid genera ( Portococcus gen. nov. and Pseudanabaenococcus gen. nov.) in the basal “filamentous” order Pseudanabaenales, Cyanobacteria
Article Snippet: .. Quality of the gDNA of LEGE strains was evaluated in a DS‐11 FX Spectrophotometer (DeNovix, Wilmington, Delaware, United States) and 1% agarose gel electrophoresis, before genome sequencing. .. Genomes were sequenced at MicrobesNG using the Illumina platform with 2 × 250 bp paired‐end libraries.

Article Title: Dynamic Gelatin Hydrogels Crosslinked by Dithiolane‐Norbornene Click Chemistry
Article Snippet: .. RNA was isolated using the NucleoSpin RNA kit (MACHEREY‐NAGEL) and quantified using a DS‐11 FX+ spectrophotometer (DeNovix). cDNA synthesis was performed with the PrimeScript RT reagent kit, and pluripotency gene expression was analyzed using SYBR Premix Ex TaqII. ..

Article Title: To multicellularity and back again: Description of two new coccoid genera (Portococcus gen. nov. and Pseudanabaenococcus gen. nov.) in the basal "filamentous" order Pseudanabaenales, Cyanobacteria.
Article Snippet: .. Quality of the gDNA of LEGE strains was evaluated in a DS- 11 FX Spectrophotometer (DeNovix, Wilmington, Delaware, United States) and 1% agarose gel electrophoresis, before genome sequencing. .. Genomes were sequenced at MicrobesNG using the Illumina platform with 2 × 250 bp paired- end libraries.

Article Title: Aging and longevity in decades‐old genebanked seeds from U.S. endangered plant species: Assessments using survival and RNA integrity assays
Article Snippet: RNA was extracted using the Plant RNeasy kit (Qiagen, Hilden, Germany) and Nucleospin RNA kit with Fruit‐mate (Takara, Düren, Germany). .. RNA yield and purity were assessed using a DS‐11 FX+ Spectrophotometer (DeNovix, Wilmington, Delaware, USA; Tetreault et al., ). ..

Article Title: Regorafenib-Induced Stress Response Alters the Bioenergetic Profile of Osteosarcoma Cells and Modulates Gene Expression Associated with Metabolic regulation-a Potential Mechanism of Osteosarcoma Treatment-Related Adaptation
Article Snippet: Total RNA was extracted using 1 mL of TRI Reagent (Sigma Aldrich/Merck, Poznań, Poland) following the manufacturer’s protocol. .. The isolated RNA was diluted in nuclease-free water (Sigma Aldrich/Merck, Poznań, Poland), and its concentration and purity were assessed spectrophotometrically at 260 and 280 nm using a DS-11 Fx spectrophotometer (Denovix, Wilmington, DE, USA). .. To ensure RNA integrity, DNase I digestion using PrecisionDNAse kit (PrimerDesign, BLIRT S.A., Gdańsk, Poland) was performed prior to reverse transcription; 500 ng of total RNA was used to detect mRNAs, and 375 ng was used to detect noncoding RNAs. cDNA synthesis was carried out with the Tetro cDNA Synthesis Kit (Bioline Reagents Limited, London, UK) or Mir-XTM miRNA First-Strand Synthesis Kit (Takara Clontech Laboratories, Biokom, Poznań, Poland) according to the manufacturer’s instructions in a T100 Thermal Cycler (Bio-Rad, Hercules, CA, USA).

Article Title: Method and device for detection of ampicillin-resistant non-typhoidal
Article Snippet: .. The quality of genomic DNA was examined using DS-11 FX Spectrophotometer (DeNovix, Wilmington, DE). .. Next-Generation Sequencing (NGS) The next-generation sequencing was performed using MiSeq (Illumina, San Diego, CA) according to the manuscript.

Agarose Gel Electrophoresis:

Article Title: To multicellularity and back again: Description of two new coccoid genera ( Portococcus gen. nov. and Pseudanabaenococcus gen. nov.) in the basal “filamentous” order Pseudanabaenales, Cyanobacteria
Article Snippet: .. Quality of the gDNA of LEGE strains was evaluated in a DS‐11 FX Spectrophotometer (DeNovix, Wilmington, Delaware, United States) and 1% agarose gel electrophoresis, before genome sequencing. .. Genomes were sequenced at MicrobesNG using the Illumina platform with 2 × 250 bp paired‐end libraries.

Article Title: To multicellularity and back again: Description of two new coccoid genera (Portococcus gen. nov. and Pseudanabaenococcus gen. nov.) in the basal "filamentous" order Pseudanabaenales, Cyanobacteria.
Article Snippet: .. Quality of the gDNA of LEGE strains was evaluated in a DS- 11 FX Spectrophotometer (DeNovix, Wilmington, Delaware, United States) and 1% agarose gel electrophoresis, before genome sequencing. .. Genomes were sequenced at MicrobesNG using the Illumina platform with 2 × 250 bp paired- end libraries.

Sequencing:

Article Title: To multicellularity and back again: Description of two new coccoid genera ( Portococcus gen. nov. and Pseudanabaenococcus gen. nov.) in the basal “filamentous” order Pseudanabaenales, Cyanobacteria
Article Snippet: .. Quality of the gDNA of LEGE strains was evaluated in a DS‐11 FX Spectrophotometer (DeNovix, Wilmington, Delaware, United States) and 1% agarose gel electrophoresis, before genome sequencing. .. Genomes were sequenced at MicrobesNG using the Illumina platform with 2 × 250 bp paired‐end libraries.

Article Title: To multicellularity and back again: Description of two new coccoid genera (Portococcus gen. nov. and Pseudanabaenococcus gen. nov.) in the basal "filamentous" order Pseudanabaenales, Cyanobacteria.
Article Snippet: .. Quality of the gDNA of LEGE strains was evaluated in a DS- 11 FX Spectrophotometer (DeNovix, Wilmington, Delaware, United States) and 1% agarose gel electrophoresis, before genome sequencing. .. Genomes were sequenced at MicrobesNG using the Illumina platform with 2 × 250 bp paired- end libraries.

Isolation:

Article Title: Dynamic Gelatin Hydrogels Crosslinked by Dithiolane‐Norbornene Click Chemistry
Article Snippet: .. RNA was isolated using the NucleoSpin RNA kit (MACHEREY‐NAGEL) and quantified using a DS‐11 FX+ spectrophotometer (DeNovix). cDNA synthesis was performed with the PrimeScript RT reagent kit, and pluripotency gene expression was analyzed using SYBR Premix Ex TaqII. ..

Article Title: Regorafenib-Induced Stress Response Alters the Bioenergetic Profile of Osteosarcoma Cells and Modulates Gene Expression Associated with Metabolic regulation-a Potential Mechanism of Osteosarcoma Treatment-Related Adaptation
Article Snippet: Total RNA was extracted using 1 mL of TRI Reagent (Sigma Aldrich/Merck, Poznań, Poland) following the manufacturer’s protocol. .. The isolated RNA was diluted in nuclease-free water (Sigma Aldrich/Merck, Poznań, Poland), and its concentration and purity were assessed spectrophotometrically at 260 and 280 nm using a DS-11 Fx spectrophotometer (Denovix, Wilmington, DE, USA). .. To ensure RNA integrity, DNase I digestion using PrecisionDNAse kit (PrimerDesign, BLIRT S.A., Gdańsk, Poland) was performed prior to reverse transcription; 500 ng of total RNA was used to detect mRNAs, and 375 ng was used to detect noncoding RNAs. cDNA synthesis was carried out with the Tetro cDNA Synthesis Kit (Bioline Reagents Limited, London, UK) or Mir-XTM miRNA First-Strand Synthesis Kit (Takara Clontech Laboratories, Biokom, Poznań, Poland) according to the manufacturer’s instructions in a T100 Thermal Cycler (Bio-Rad, Hercules, CA, USA).

cDNA Synthesis:

Article Title: Dynamic Gelatin Hydrogels Crosslinked by Dithiolane‐Norbornene Click Chemistry
Article Snippet: .. RNA was isolated using the NucleoSpin RNA kit (MACHEREY‐NAGEL) and quantified using a DS‐11 FX+ spectrophotometer (DeNovix). cDNA synthesis was performed with the PrimeScript RT reagent kit, and pluripotency gene expression was analyzed using SYBR Premix Ex TaqII. ..

Gene Expression:

Article Title: Dynamic Gelatin Hydrogels Crosslinked by Dithiolane‐Norbornene Click Chemistry
Article Snippet: .. RNA was isolated using the NucleoSpin RNA kit (MACHEREY‐NAGEL) and quantified using a DS‐11 FX+ spectrophotometer (DeNovix). cDNA synthesis was performed with the PrimeScript RT reagent kit, and pluripotency gene expression was analyzed using SYBR Premix Ex TaqII. ..



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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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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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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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DeNovix denovix ds 11 fx spectrophotometer fluorometer
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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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