3 × sequencing gel loading dye Search Results


3 × sequencing gel loading dye  (Fisher Scientific)
90
Fisher Scientific 3 × sequencing gel loading dye
3 × Sequencing Gel Loading Dye, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/3 × sequencing gel loading dye/product/Fisher Scientific
Average 90 stars, based on 1 article reviews
3 × sequencing gel loading dye - by Bioz Stars, 2026-03
90/100 stars
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sequencing gel loading dye  (Fisher Scientific)
90
Fisher Scientific sequencing gel loading dye
Identification of DNA-PK phosphorylation sites in PNKP. ( A ) Purified His-tagged PNKP (0.5 µg) was incubated with or without DNA-PK (400 ng), calf thymus DNA (10 µg/ml) or 10 µM wortmannin, as indicated by the + or − symbols. The reaction was carried out at 30°C for 30 min and stopped by boiling in SDS sample buffer. Proteins were separated by electrophoresis on a 10% SDS polyacrylamide gel stained with Coomassie blue, and dried for autoradiography. ( B ) Purified PNKP, phosphorylated by DNA-PK, was separated by electrophoresis on an SDS polyacrylamide gel and then digested with trypsin as described in ‘Materials and methods’ section. The resulting 32 P-labeled peptides were chromatographed on a Vydac 218TP54 C 18 column (Separation Group, Hesperia, CA, USA) equilibrated in 0.1% (v/v) trifluoroacetic acid in water. The column was developed with a linear acetonitrile gradient (dashed diagonal line, right hand Y -axis) at 0.8 ml/min, and fractions of 0.4 ml were collected: >80% of the radioactivity applied to the column was recovered in the fractions. ( C ) An aliquot of the major 32 P-labeled peptide derived from phosphorylated PNKP ( B) was covalently coupled to a Sequelon acrylamide membrane and analyzed on an Applied Biosystems 476A sequenator. 32 P radioactivity was measured after each cycle of Edman degradation. In combination with MALDI-TOF MS, database searching against predicted PNKP tryptic peptides and phosphoamino acid analysis (data not shown) enabled the identification of the site of phosphorylation in the peptide. The putative amino acid sequence of this peptide, deduced from a combination of phosphoamino acid analysis, MS and solid-phase <t>sequencing,</t> is indicated at the bottom of the graph.
Sequencing Gel Loading Dye, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sequencing gel loading dye/product/Fisher Scientific
Average 90 stars, based on 1 article reviews
sequencing gel loading dye - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
sequencing gel loading dye  (Amresco)
90
Amresco sequencing gel loading dye
Identification of DNA-PK phosphorylation sites in PNKP. ( A ) Purified His-tagged PNKP (0.5 µg) was incubated with or without DNA-PK (400 ng), calf thymus DNA (10 µg/ml) or 10 µM wortmannin, as indicated by the + or − symbols. The reaction was carried out at 30°C for 30 min and stopped by boiling in SDS sample buffer. Proteins were separated by electrophoresis on a 10% SDS polyacrylamide gel stained with Coomassie blue, and dried for autoradiography. ( B ) Purified PNKP, phosphorylated by DNA-PK, was separated by electrophoresis on an SDS polyacrylamide gel and then digested with trypsin as described in ‘Materials and methods’ section. The resulting 32 P-labeled peptides were chromatographed on a Vydac 218TP54 C 18 column (Separation Group, Hesperia, CA, USA) equilibrated in 0.1% (v/v) trifluoroacetic acid in water. The column was developed with a linear acetonitrile gradient (dashed diagonal line, right hand Y -axis) at 0.8 ml/min, and fractions of 0.4 ml were collected: >80% of the radioactivity applied to the column was recovered in the fractions. ( C ) An aliquot of the major 32 P-labeled peptide derived from phosphorylated PNKP ( B) was covalently coupled to a Sequelon acrylamide membrane and analyzed on an Applied Biosystems 476A sequenator. 32 P radioactivity was measured after each cycle of Edman degradation. In combination with MALDI-TOF MS, database searching against predicted PNKP tryptic peptides and phosphoamino acid analysis (data not shown) enabled the identification of the site of phosphorylation in the peptide. The putative amino acid sequence of this peptide, deduced from a combination of phosphoamino acid analysis, MS and solid-phase <t>sequencing,</t> is indicated at the bottom of the graph.
Sequencing Gel Loading Dye, supplied by Amresco, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sequencing gel loading dye/product/Amresco
Average 90 stars, based on 1 article reviews
sequencing gel loading dye - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
sequencing gel loading dye  (Amersham Life Sciences Inc)
90
Amersham Life Sciences Inc sequencing gel loading dye
Identification of DNA-PK phosphorylation sites in PNKP. ( A ) Purified His-tagged PNKP (0.5 µg) was incubated with or without DNA-PK (400 ng), calf thymus DNA (10 µg/ml) or 10 µM wortmannin, as indicated by the + or − symbols. The reaction was carried out at 30°C for 30 min and stopped by boiling in SDS sample buffer. Proteins were separated by electrophoresis on a 10% SDS polyacrylamide gel stained with Coomassie blue, and dried for autoradiography. ( B ) Purified PNKP, phosphorylated by DNA-PK, was separated by electrophoresis on an SDS polyacrylamide gel and then digested with trypsin as described in ‘Materials and methods’ section. The resulting 32 P-labeled peptides were chromatographed on a Vydac 218TP54 C 18 column (Separation Group, Hesperia, CA, USA) equilibrated in 0.1% (v/v) trifluoroacetic acid in water. The column was developed with a linear acetonitrile gradient (dashed diagonal line, right hand Y -axis) at 0.8 ml/min, and fractions of 0.4 ml were collected: >80% of the radioactivity applied to the column was recovered in the fractions. ( C ) An aliquot of the major 32 P-labeled peptide derived from phosphorylated PNKP ( B) was covalently coupled to a Sequelon acrylamide membrane and analyzed on an Applied Biosystems 476A sequenator. 32 P radioactivity was measured after each cycle of Edman degradation. In combination with MALDI-TOF MS, database searching against predicted PNKP tryptic peptides and phosphoamino acid analysis (data not shown) enabled the identification of the site of phosphorylation in the peptide. The putative amino acid sequence of this peptide, deduced from a combination of phosphoamino acid analysis, MS and solid-phase <t>sequencing,</t> is indicated at the bottom of the graph.
Sequencing Gel Loading Dye, supplied by Amersham Life Sciences Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sequencing gel loading dye/product/Amersham Life Sciences Inc
Average 90 stars, based on 1 article reviews
sequencing gel loading dye - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
3x sequencing gel loading dye  (Fisher Scientific)
90
Fisher Scientific 3x sequencing gel loading dye
Identification of DNA-PK phosphorylation sites in PNKP. ( A ) Purified His-tagged PNKP (0.5 µg) was incubated with or without DNA-PK (400 ng), calf thymus DNA (10 µg/ml) or 10 µM wortmannin, as indicated by the + or − symbols. The reaction was carried out at 30°C for 30 min and stopped by boiling in SDS sample buffer. Proteins were separated by electrophoresis on a 10% SDS polyacrylamide gel stained with Coomassie blue, and dried for autoradiography. ( B ) Purified PNKP, phosphorylated by DNA-PK, was separated by electrophoresis on an SDS polyacrylamide gel and then digested with trypsin as described in ‘Materials and methods’ section. The resulting 32 P-labeled peptides were chromatographed on a Vydac 218TP54 C 18 column (Separation Group, Hesperia, CA, USA) equilibrated in 0.1% (v/v) trifluoroacetic acid in water. The column was developed with a linear acetonitrile gradient (dashed diagonal line, right hand Y -axis) at 0.8 ml/min, and fractions of 0.4 ml were collected: >80% of the radioactivity applied to the column was recovered in the fractions. ( C ) An aliquot of the major 32 P-labeled peptide derived from phosphorylated PNKP ( B) was covalently coupled to a Sequelon acrylamide membrane and analyzed on an Applied Biosystems 476A sequenator. 32 P radioactivity was measured after each cycle of Edman degradation. In combination with MALDI-TOF MS, database searching against predicted PNKP tryptic peptides and phosphoamino acid analysis (data not shown) enabled the identification of the site of phosphorylation in the peptide. The putative amino acid sequence of this peptide, deduced from a combination of phosphoamino acid analysis, MS and solid-phase <t>sequencing,</t> is indicated at the bottom of the graph.
3x Sequencing Gel Loading Dye, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/3x sequencing gel loading dye/product/Fisher Scientific
Average 90 stars, based on 1 article reviews
3x sequencing gel loading dye - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


Identification of DNA-PK phosphorylation sites in PNKP. ( A ) Purified His-tagged PNKP (0.5 µg) was incubated with or without DNA-PK (400 ng), calf thymus DNA (10 µg/ml) or 10 µM wortmannin, as indicated by the + or − symbols. The reaction was carried out at 30°C for 30 min and stopped by boiling in SDS sample buffer. Proteins were separated by electrophoresis on a 10% SDS polyacrylamide gel stained with Coomassie blue, and dried for autoradiography. ( B ) Purified PNKP, phosphorylated by DNA-PK, was separated by electrophoresis on an SDS polyacrylamide gel and then digested with trypsin as described in ‘Materials and methods’ section. The resulting 32 P-labeled peptides were chromatographed on a Vydac 218TP54 C 18 column (Separation Group, Hesperia, CA, USA) equilibrated in 0.1% (v/v) trifluoroacetic acid in water. The column was developed with a linear acetonitrile gradient (dashed diagonal line, right hand Y -axis) at 0.8 ml/min, and fractions of 0.4 ml were collected: >80% of the radioactivity applied to the column was recovered in the fractions. ( C ) An aliquot of the major 32 P-labeled peptide derived from phosphorylated PNKP ( B) was covalently coupled to a Sequelon acrylamide membrane and analyzed on an Applied Biosystems 476A sequenator. 32 P radioactivity was measured after each cycle of Edman degradation. In combination with MALDI-TOF MS, database searching against predicted PNKP tryptic peptides and phosphoamino acid analysis (data not shown) enabled the identification of the site of phosphorylation in the peptide. The putative amino acid sequence of this peptide, deduced from a combination of phosphoamino acid analysis, MS and solid-phase sequencing, is indicated at the bottom of the graph.

Journal: Nucleic Acids Research

Article Title: Phosphorylation of polynucleotide kinase/ phosphatase by DNA-dependent protein kinase and ataxia-telangiectasia mutated regulates its association with sites of DNA damage

doi: 10.1093/nar/gkr647

Figure Lengend Snippet: Identification of DNA-PK phosphorylation sites in PNKP. ( A ) Purified His-tagged PNKP (0.5 µg) was incubated with or without DNA-PK (400 ng), calf thymus DNA (10 µg/ml) or 10 µM wortmannin, as indicated by the + or − symbols. The reaction was carried out at 30°C for 30 min and stopped by boiling in SDS sample buffer. Proteins were separated by electrophoresis on a 10% SDS polyacrylamide gel stained with Coomassie blue, and dried for autoradiography. ( B ) Purified PNKP, phosphorylated by DNA-PK, was separated by electrophoresis on an SDS polyacrylamide gel and then digested with trypsin as described in ‘Materials and methods’ section. The resulting 32 P-labeled peptides were chromatographed on a Vydac 218TP54 C 18 column (Separation Group, Hesperia, CA, USA) equilibrated in 0.1% (v/v) trifluoroacetic acid in water. The column was developed with a linear acetonitrile gradient (dashed diagonal line, right hand Y -axis) at 0.8 ml/min, and fractions of 0.4 ml were collected: >80% of the radioactivity applied to the column was recovered in the fractions. ( C ) An aliquot of the major 32 P-labeled peptide derived from phosphorylated PNKP ( B) was covalently coupled to a Sequelon acrylamide membrane and analyzed on an Applied Biosystems 476A sequenator. 32 P radioactivity was measured after each cycle of Edman degradation. In combination with MALDI-TOF MS, database searching against predicted PNKP tryptic peptides and phosphoamino acid analysis (data not shown) enabled the identification of the site of phosphorylation in the peptide. The putative amino acid sequence of this peptide, deduced from a combination of phosphoamino acid analysis, MS and solid-phase sequencing, is indicated at the bottom of the graph.

Article Snippet: Aliquots (4 μl) were taken at 0, 0.5, 1, 2 and 5 min intervals, mixed with 2 μl sequencing gel loading dye (Fisher Scientific), boiled and analyzed as above.

Techniques: Phospho-proteomics, Purification, Incubation, Electrophoresis, Staining, Autoradiography, Labeling, Radioactivity, Derivative Assay, Membrane, Phosphoamino Acid Analysis, Sequencing