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sybr gold solution  (Thermo Fisher)


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    Structured Review

    Thermo Fisher sybr gold solution
    Sybr Gold Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sybr+gold+solution/TRIS-buffered+saline+(TBS/pmc12686545-271-16-19
    Average 99 stars, based on 1 article reviews
    sybr gold solution - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Membrane:

    Article Title: Age deceleration and reversal gene patterns in dauer diapause
    Article Snippet: The membrane was washed three times with TBS-T and revealed in a dark room using PierceTM ECL Plus Western Blotting Substrate (Thermo Fisher Scientific) and CL-XPosureTM Film (13×18 cm, Thermo Fisher Scientific). .. To assess total DNA levels, the membrane was washed five times with TBS-T and incubated with SYBR Gold solution (Thermo Fisher Scientific, 1:10000 in TBS-T) overnight at 4°C. .. Membrane was revealed using a ChemiDoc Imaging System (Bio-Rad) and the Bio-Rad ImageLab 5.0 software.

    Article Title: Age Deceleration and Reversal Gene Patterns in Dauer Diapause
    Article Snippet: The membrane was washed three times with TBS‐T and revealed in a dark room using Pierce ECL Plus Western Blotting Substrate (Thermo Fisher Scientific) and CL‐XPosure Film (13 × 18 cm, Thermo Fisher Scientific). .. To assess total DNA levels, the membrane was washed five times with TBS‐T and incubated with SYBR Gold solution (Thermo Fisher Scientific, 1:10000 in TBS‐T) overnight at 4°C. .. The membrane was revealed using a ChemiDoc Imaging System (Bio‐Rad) and the Bio‐Rad ImageLab 5.0 software.

    Incubation:

    Article Title: Age deceleration and reversal gene patterns in dauer diapause
    Article Snippet: The membrane was washed three times with TBS-T and revealed in a dark room using PierceTM ECL Plus Western Blotting Substrate (Thermo Fisher Scientific) and CL-XPosureTM Film (13×18 cm, Thermo Fisher Scientific). .. To assess total DNA levels, the membrane was washed five times with TBS-T and incubated with SYBR Gold solution (Thermo Fisher Scientific, 1:10000 in TBS-T) overnight at 4°C. .. Membrane was revealed using a ChemiDoc Imaging System (Bio-Rad) and the Bio-Rad ImageLab 5.0 software.

    Article Title: Age Deceleration and Reversal Gene Patterns in Dauer Diapause
    Article Snippet: The membrane was washed three times with TBS‐T and revealed in a dark room using Pierce ECL Plus Western Blotting Substrate (Thermo Fisher Scientific) and CL‐XPosure Film (13 × 18 cm, Thermo Fisher Scientific). .. To assess total DNA levels, the membrane was washed five times with TBS‐T and incubated with SYBR Gold solution (Thermo Fisher Scientific, 1:10000 in TBS‐T) overnight at 4°C. .. The membrane was revealed using a ChemiDoc Imaging System (Bio‐Rad) and the Bio‐Rad ImageLab 5.0 software.

    Staining:

    Article Title: Evolving Escherichia coli to use a tRNA with a non-canonical fold as an adaptor of the genetic code.
    Article Snippet: A low range ssRNA ladder (New England Biolabs) was used as a size marker, prepared according to the manufacturer’s protocol. .. The gels were stained for 25 min with 50 ml of SYBR gold solution (Thermo Fisher Scientific) according to the manufacturer’s guidelines. ..

    Article Title: Evolving Escherichia coli to use a tRNA with a non-canonical fold as an adaptor of the genetic code
    Article Snippet: A low range ssRNA ladder (New England Biolabs) was used as a size marker, prepared according to the manufacturer’s protocol. .. The gels were stained for 25 min with 50 ml of SYBR gold solution (Thermo Fisher Scientific) according to the manufacturer’s guidelines. ..

    Article Title: Mitochondrial small RNA alterations associated with increased lysosome activity in an Alzheimer’s Disease Mouse Model uncovered by PANDORA-seq
    Article Snippet: .. After staining with SYBR Gold solution (Invitrogen; S11494), gels that contained small RNAs of 15–50 nucleotides were excised based on small RNA ladders (Abnova TM R0007). ..

    Article Title: Substituted Triazole-3,5-Diamine Compounds as Novel Human Topoisomerase III Beta Inhibitors.
    Article Snippet: After mixing by gentle vortex, the reaction mixtures were spun down and incubated at 37 ◦C for 1 h. The relaxation reactions were terminated by the addition of 1 μL of 10% SDS and 2 μL of 800 units/mL of proteinase K (New England Biolabs) and incubated at 45 ◦C for 30 min. .. Following the addition of 5 μL of stop solution (50 mM of EDTA, 50% glycerol, and 0.5% v/v bromophenol blue), the reaction products were analyzed in a 1% agarose gel with TAE (40 mM of Tris-acetate, pH 8.0, 2 mM of EDTA) buffer containing 5 μg/mL of chloroquine at 25 V (1 V/cm) for 18 h. Gels were washed with TAE buffer for 1 h and 50 mM of NaCl for 1 h to remove the chloroquine, and finally with deionized water for 30 min. Gels were stained for 2 h with 1 μg/mL of SYBR Gold solution (Thermo Fischer Scientific, Waltham, MA, USA). ..

    Agarose Gel Electrophoresis:

    Article Title: Substituted Triazole-3,5-Diamine Compounds as Novel Human Topoisomerase III Beta Inhibitors.
    Article Snippet: After mixing by gentle vortex, the reaction mixtures were spun down and incubated at 37 ◦C for 1 h. The relaxation reactions were terminated by the addition of 1 μL of 10% SDS and 2 μL of 800 units/mL of proteinase K (New England Biolabs) and incubated at 45 ◦C for 30 min. .. Following the addition of 5 μL of stop solution (50 mM of EDTA, 50% glycerol, and 0.5% v/v bromophenol blue), the reaction products were analyzed in a 1% agarose gel with TAE (40 mM of Tris-acetate, pH 8.0, 2 mM of EDTA) buffer containing 5 μg/mL of chloroquine at 25 V (1 V/cm) for 18 h. Gels were washed with TAE buffer for 1 h and 50 mM of NaCl for 1 h to remove the chloroquine, and finally with deionized water for 30 min. Gels were stained for 2 h with 1 μg/mL of SYBR Gold solution (Thermo Fischer Scientific, Waltham, MA, USA). ..



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    a, the 5’ end of the mRNA reporters, which lacked a start codon, was transcribed and capped in vitro . The integrity of the RNA was verified by polyacrylamide gel electrophoresis (PAGE) and <t>SYBR</t> gold staining. b, successful capping of the in vitro transcribed 5’ ends was verified by dot blot using anti-m 7 G antibodies. Methylene blue staining was used as a loading control. c, the 3’ end of the mRNA reporters, containing the ORF and the 3’UTR but lacking a start codon, was transcribed and polyadenylated in vitro . The integrity of the RNA and the efficiency of polyadenylation were verified using PAGE and SYBR gold staining. d, the ligation efficiency of NanoLuc mRNA reporters was verified using PAGE and SYBR gold staining. Ligated mRNA shows a shift in molecular weight compared to unligated mRNA. e, relative light units were measured in lysates from HEK293T cells co-transfected with increasing amounts of unligated RNA pieces and constant amounts (20 ng) of full-length NanoLuc mRNA. Mean ± SEM, n = 3. The line plot shows stable NanoLuc activity across different amounts of unligated RNA. f, Integrity of the synthetic 5’ phosphorylated RNA oligos containing unmodified or 2’O-methylation in different positions around the start codon. g, the efficiency of ligation was verified by RT-qPCR. Two sets of primers were used (Supplementary Table 1). The first set specifically recognizes the ligated mRNA, while the second set binds NanoLuc ORF to obtain total levels of mRNA. The efficiency of ligation was calculated as: (ligated mRNA)/(total RNA)*100. h, NanoLuc activity normalized by transfected mRNAs, which was obtained using RT-qPCR from the RNA transfected into HEK293T cells. Mean ± SEM, n = 3. i, relative light units were measured in lysates from HeLa cells transfected with ligated NanoLuc mRNAs carrying 2’O-methylation in different positions around the start codon. Unmethylated (blue) and unligated mRNAs were used as controls. Mean ± SEM, n = 4. p = One-way ANOVA with Tukey’s post hoc analysis. j, denaturing agarose gel electrophoresis indicating the ligation efficiencies for the GFP mRNA reporters. These RNA pieces are larger than the ones used for NanoLuc reporters and do not resolve well in PAGE gels. Thus, agarose gels are better suited for their separation. k, schematic indicating the relative lengths of 5’UTRs in the NanoLuc and GFP mRNA reporters.
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    a, the 5’ end of the mRNA reporters, which lacked a start codon, was transcribed and capped in vitro . The integrity of the RNA was verified by polyacrylamide gel electrophoresis (PAGE) and SYBR gold staining. b, successful capping of the in vitro transcribed 5’ ends was verified by dot blot using anti-m 7 G antibodies. Methylene blue staining was used as a loading control. c, the 3’ end of the mRNA reporters, containing the ORF and the 3’UTR but lacking a start codon, was transcribed and polyadenylated in vitro . The integrity of the RNA and the efficiency of polyadenylation were verified using PAGE and SYBR gold staining. d, the ligation efficiency of NanoLuc mRNA reporters was verified using PAGE and SYBR gold staining. Ligated mRNA shows a shift in molecular weight compared to unligated mRNA. e, relative light units were measured in lysates from HEK293T cells co-transfected with increasing amounts of unligated RNA pieces and constant amounts (20 ng) of full-length NanoLuc mRNA. Mean ± SEM, n = 3. The line plot shows stable NanoLuc activity across different amounts of unligated RNA. f, Integrity of the synthetic 5’ phosphorylated RNA oligos containing unmodified or 2’O-methylation in different positions around the start codon. g, the efficiency of ligation was verified by RT-qPCR. Two sets of primers were used (Supplementary Table 1). The first set specifically recognizes the ligated mRNA, while the second set binds NanoLuc ORF to obtain total levels of mRNA. The efficiency of ligation was calculated as: (ligated mRNA)/(total RNA)*100. h, NanoLuc activity normalized by transfected mRNAs, which was obtained using RT-qPCR from the RNA transfected into HEK293T cells. Mean ± SEM, n = 3. i, relative light units were measured in lysates from HeLa cells transfected with ligated NanoLuc mRNAs carrying 2’O-methylation in different positions around the start codon. Unmethylated (blue) and unligated mRNAs were used as controls. Mean ± SEM, n = 4. p = One-way ANOVA with Tukey’s post hoc analysis. j, denaturing agarose gel electrophoresis indicating the ligation efficiencies for the GFP mRNA reporters. These RNA pieces are larger than the ones used for NanoLuc reporters and do not resolve well in PAGE gels. Thus, agarose gels are better suited for their separation. k, schematic indicating the relative lengths of 5’UTRs in the NanoLuc and GFP mRNA reporters.

    Journal: bioRxiv

    Article Title: Targeted Inhibition of Translation Initiation via 2’O-Methylation of Start Codons

    doi: 10.1101/2025.06.14.659565

    Figure Lengend Snippet: a, the 5’ end of the mRNA reporters, which lacked a start codon, was transcribed and capped in vitro . The integrity of the RNA was verified by polyacrylamide gel electrophoresis (PAGE) and SYBR gold staining. b, successful capping of the in vitro transcribed 5’ ends was verified by dot blot using anti-m 7 G antibodies. Methylene blue staining was used as a loading control. c, the 3’ end of the mRNA reporters, containing the ORF and the 3’UTR but lacking a start codon, was transcribed and polyadenylated in vitro . The integrity of the RNA and the efficiency of polyadenylation were verified using PAGE and SYBR gold staining. d, the ligation efficiency of NanoLuc mRNA reporters was verified using PAGE and SYBR gold staining. Ligated mRNA shows a shift in molecular weight compared to unligated mRNA. e, relative light units were measured in lysates from HEK293T cells co-transfected with increasing amounts of unligated RNA pieces and constant amounts (20 ng) of full-length NanoLuc mRNA. Mean ± SEM, n = 3. The line plot shows stable NanoLuc activity across different amounts of unligated RNA. f, Integrity of the synthetic 5’ phosphorylated RNA oligos containing unmodified or 2’O-methylation in different positions around the start codon. g, the efficiency of ligation was verified by RT-qPCR. Two sets of primers were used (Supplementary Table 1). The first set specifically recognizes the ligated mRNA, while the second set binds NanoLuc ORF to obtain total levels of mRNA. The efficiency of ligation was calculated as: (ligated mRNA)/(total RNA)*100. h, NanoLuc activity normalized by transfected mRNAs, which was obtained using RT-qPCR from the RNA transfected into HEK293T cells. Mean ± SEM, n = 3. i, relative light units were measured in lysates from HeLa cells transfected with ligated NanoLuc mRNAs carrying 2’O-methylation in different positions around the start codon. Unmethylated (blue) and unligated mRNAs were used as controls. Mean ± SEM, n = 4. p = One-way ANOVA with Tukey’s post hoc analysis. j, denaturing agarose gel electrophoresis indicating the ligation efficiencies for the GFP mRNA reporters. These RNA pieces are larger than the ones used for NanoLuc reporters and do not resolve well in PAGE gels. Thus, agarose gels are better suited for their separation. k, schematic indicating the relative lengths of 5’UTRs in the NanoLuc and GFP mRNA reporters.

    Article Snippet: Electrophoresis was run in a 0.5X TBE running buffer and stained with a 1X SYBR gold solution (ThermoFisher, Cat. #: S11494).

    Techniques: In Vitro, Polyacrylamide Gel Electrophoresis, Staining, Dot Blot, Control, Ligation, Molecular Weight, Transfection, Activity Assay, Methylation, Quantitative RT-PCR, Agarose Gel Electrophoresis

    a-b, the 5’UTR sequence of all canonical protein-coding transcripts was downloaded from Biomart and analyzed to estimate the percentage of transcripts with one or more upstream AUGs (a) and the percentage of transcripts with one or more upstream near-cognate codon (b). This analysis indicated that 99% of human transcripts contain at least one near-cognate codon in their 5’UTRs, whereas 50% of human transcripts contain at least one AUG in their 5’UTR sequences. c, distribution of upstream near-cognate or AUG codons per transcript. CUG is the most prevalent near-cognate codon in human transcripts. d, while virtually all human transcripts contain cryptic initiation sites in their 5’UTRs, not all are used at a given moment or physiological condition. To determine the upstream near-cognate or AUG codons used for initiation, we previously performed HR-Ribo-seq in HeLa cells. In this method, the inhibitor Harringtonine (HR) stalls the initiator ribosome while letting the elongator ribosomes slide off of mRNAs. Subsequent RNAse footprinting and isolation of ribosome-protected fragments (RPFs) allow the identification of initiation sites transcriptome-wide. e, HR-Ribo-seq indicates that ∼70% of transcripts initiate translation from at least one upstream site in wildtype HeLa cells. f, the integrity of ligated NanoLuc mRNAs carrying near-cognate codons was verified using PAGE and SYBR gold staining. g, relative light units were measured in lysates from HeLa cells transfected with unmodified, C m UG, or G m UG-modified NanoLuc mRNAs. Mean ± SEM, n = 4. p = two-tailed Student’s t-test .

    Journal: bioRxiv

    Article Title: Targeted Inhibition of Translation Initiation via 2’O-Methylation of Start Codons

    doi: 10.1101/2025.06.14.659565

    Figure Lengend Snippet: a-b, the 5’UTR sequence of all canonical protein-coding transcripts was downloaded from Biomart and analyzed to estimate the percentage of transcripts with one or more upstream AUGs (a) and the percentage of transcripts with one or more upstream near-cognate codon (b). This analysis indicated that 99% of human transcripts contain at least one near-cognate codon in their 5’UTRs, whereas 50% of human transcripts contain at least one AUG in their 5’UTR sequences. c, distribution of upstream near-cognate or AUG codons per transcript. CUG is the most prevalent near-cognate codon in human transcripts. d, while virtually all human transcripts contain cryptic initiation sites in their 5’UTRs, not all are used at a given moment or physiological condition. To determine the upstream near-cognate or AUG codons used for initiation, we previously performed HR-Ribo-seq in HeLa cells. In this method, the inhibitor Harringtonine (HR) stalls the initiator ribosome while letting the elongator ribosomes slide off of mRNAs. Subsequent RNAse footprinting and isolation of ribosome-protected fragments (RPFs) allow the identification of initiation sites transcriptome-wide. e, HR-Ribo-seq indicates that ∼70% of transcripts initiate translation from at least one upstream site in wildtype HeLa cells. f, the integrity of ligated NanoLuc mRNAs carrying near-cognate codons was verified using PAGE and SYBR gold staining. g, relative light units were measured in lysates from HeLa cells transfected with unmodified, C m UG, or G m UG-modified NanoLuc mRNAs. Mean ± SEM, n = 4. p = two-tailed Student’s t-test .

    Article Snippet: Electrophoresis was run in a 0.5X TBE running buffer and stained with a 1X SYBR gold solution (ThermoFisher, Cat. #: S11494).

    Techniques: Sequencing, Footprinting, Isolation, Staining, Transfection, Modification, Two Tailed Test