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lysis buffer  (Bio-Rad)


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    Structured Review

    Bio-Rad lysis buffer
    Lysis Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 183 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/buffer+preparation/iScript+RT-qPCR+Sample+Preparation+Reagent/pmc13061224-241-13-20
    Average 94 stars, based on 183 article reviews
    lysis buffer - by Bioz Stars, 2026-09
    94/100 stars

    Images

    Related Articles

    Acrylamide Gel Assay:

    Article Title: AXL-Driven Stemness and Hedgehog Signaling in HER2-Positive Breast Cancer with Acquired Trastuzumab Resistance: Synergistic Potential of AXL and HER2 Co-Targeting.
    Article Snippet: .. Protein samples were loaded onto a 7.5% acrylamide gel in running buffer containing 10% SDS, with Precision Plus ProteinTM Dual Color Standards (Bio-Rad, Hercules, CA, USA) used as a molecular weight marker. ..

    Molecular Weight:

    Article Title: AXL-Driven Stemness and Hedgehog Signaling in HER2-Positive Breast Cancer with Acquired Trastuzumab Resistance: Synergistic Potential of AXL and HER2 Co-Targeting.
    Article Snippet: .. Protein samples were loaded onto a 7.5% acrylamide gel in running buffer containing 10% SDS, with Precision Plus ProteinTM Dual Color Standards (Bio-Rad, Hercules, CA, USA) used as a molecular weight marker. ..

    Marker:

    Article Title: AXL-Driven Stemness and Hedgehog Signaling in HER2-Positive Breast Cancer with Acquired Trastuzumab Resistance: Synergistic Potential of AXL and HER2 Co-Targeting.
    Article Snippet: .. Protein samples were loaded onto a 7.5% acrylamide gel in running buffer containing 10% SDS, with Precision Plus ProteinTM Dual Color Standards (Bio-Rad, Hercules, CA, USA) used as a molecular weight marker. ..

    other:

    Article Title: Th17 cells require the DNA repair sensor xeroderma pigmentosum complementation Group C to control oxidative DNA damage in a murine model.
    Article Snippet: Sample preparation was performed with 2x Laemmli sample buffer (Bio-rad), and heated for 10min at 95 °C for protein denaturation.

    Article Title: Th17 cells require the DNA repair sensor xeroderma pigmentosum complementation Group C to control oxidative DNA damage in a murine model
    Article Snippet: Sample preparation was performed with 2x Laemmli sample buffer (Bio-rad), and heated for 10 min at 95 °C for protein denaturation.

    Polymerase Chain Reaction:

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line.
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Lysis:

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line.
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Quantitative RT-PCR:

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line.
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Sample Prep:

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line.
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Transferring:

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line.
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Gentle:

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Article Title: Single-cell analysis of inhibitory efferent neurons of the zebrafish lateral line.
    Article Snippet: .. The collected cell was expelled into an RNase-free PCR tube containing 5 μl lysis buffer (iScript RT-qPCR Sample Preparation Reagent, Bio-Rad) by breaking the pipette tip in the tube and applying gentle positive pressure. ..

    Nucleic Acid Electrophoresis:

    Article Title: Fc-free single-chain antibody mRNA therapy for airway infection of multidrug-resistant Pseudomonas aeruginosa
    Article Snippet: The supernatant (100 μL, equivalent to an extract from 6.7 mg of tissue) from the liver homogenate (15 mL T-PER/g liver) of the mice was incubated with nickel‒nitrilotriacetic acid agarose (100 μL of 50% slurry, Cat. No. 30210; Qiagen) for 1 h at room temperature with constant shaking. .. After two washes with washing buffer, the bound protein components were eluted with elution buffer, mixed under either non-reducing (2× Laemmli sample buffer, Cat. No. 1610737; Bio-Rad Laboratories, Inc., Hercules, CA, USA) or reducing conditions (2× Laemmli sample buffer containing 50 mM dithiothreitol, Invitrogen NuPAGE 10× Sample Reducing Agent, Cat. No. NP0009; Thermo Fisher Scientific) at 85 °C for 5 min. Then, 10 μL of sample solution (equivalent to an extract from 0.67 mg of the liver) was loaded for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Miniprotean 4–15% TGX gel, Cat. No. 4561081; Bio-Rad Laboratories, Inc.), and transferred to a poly vinylidene di-fluoride or nitrocellulose membrane (Cat. No. IB34002 and Cat. No. IB33002; Thermo Fisher Scientific) via a dry blot module (Invitrogen iBlotTM 3, Cat. No. IB31001; Thermo Fisher Scientific). .. After blotting on a membrane, the membrane was incubated with 8% acetic acid for 15 min, 3% H2O2 in PBS/0.01%Tween-20 for 15 min, blocked with 4% skim milk in PBS/0.01%T for 1 h, and then incubated with a horseradish peroxidase (HRP)-conjugated anti-cMyc antibody (anti-Myc-tag mAb-HRP-DirecT, mouse IgG2bk, Cat. No. M192-7; MBL, Tokyo, Japan) at 1:10,000 dilution in 4% skim milk in PBS/0.01%Tween-20 overnight at 4 °C.

    Membrane:

    Article Title: Fc-free single-chain antibody mRNA therapy for airway infection of multidrug-resistant Pseudomonas aeruginosa
    Article Snippet: The supernatant (100 μL, equivalent to an extract from 6.7 mg of tissue) from the liver homogenate (15 mL T-PER/g liver) of the mice was incubated with nickel‒nitrilotriacetic acid agarose (100 μL of 50% slurry, Cat. No. 30210; Qiagen) for 1 h at room temperature with constant shaking. .. After two washes with washing buffer, the bound protein components were eluted with elution buffer, mixed under either non-reducing (2× Laemmli sample buffer, Cat. No. 1610737; Bio-Rad Laboratories, Inc., Hercules, CA, USA) or reducing conditions (2× Laemmli sample buffer containing 50 mM dithiothreitol, Invitrogen NuPAGE 10× Sample Reducing Agent, Cat. No. NP0009; Thermo Fisher Scientific) at 85 °C for 5 min. Then, 10 μL of sample solution (equivalent to an extract from 0.67 mg of the liver) was loaded for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Miniprotean 4–15% TGX gel, Cat. No. 4561081; Bio-Rad Laboratories, Inc.), and transferred to a poly vinylidene di-fluoride or nitrocellulose membrane (Cat. No. IB34002 and Cat. No. IB33002; Thermo Fisher Scientific) via a dry blot module (Invitrogen iBlotTM 3, Cat. No. IB31001; Thermo Fisher Scientific). .. After blotting on a membrane, the membrane was incubated with 8% acetic acid for 15 min, 3% H2O2 in PBS/0.01%Tween-20 for 15 min, blocked with 4% skim milk in PBS/0.01%T for 1 h, and then incubated with a horseradish peroxidase (HRP)-conjugated anti-cMyc antibody (anti-Myc-tag mAb-HRP-DirecT, mouse IgG2bk, Cat. No. M192-7; MBL, Tokyo, Japan) at 1:10,000 dilution in 4% skim milk in PBS/0.01%Tween-20 overnight at 4 °C.



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    Stable mobilization of CEBPs and PPARG upon transient TAK-981 treatment in pre-adipocytes. ( A <t>)</t> <t>ATAC-seq</t> experimental layout in hTERT A41hWAT-SVF pre-adipocytes. Time series analysis and hierarchical clustering of significant variations in chromatin accessibility at day 0 (D0), 12 h (12h), and day (D7) after TAK-981 treatment. ( C ) GOBP analysis of ATAC-seq clusters 2 and 6 revealed in panel (B). See and for an analysis of all clusters. ( D – F ) Volcano plots displaying the results of ATAC-seq inferred differential TF activity analyses performed at D0, 12h, and D7 after TAK-981 or DMSO treatment. Colored dots indicate significant differentially mobilized TFs (TAK-981 versus DMSO). Differential binding score >0.05 and pAdj <0.001. ( G ) Time series analysis inferred TF activity over time (TAK-981 versus DMSO) at D0, 12h, and D7 after TAK-981 treatment. ( H ) Western blot analysis of CEBPB SUMOylation in DMSO and TAK-981-treated cells. ( I ) Western blot analysis of CEBPB and PPARG in DMSO, rosiglitazone, TAK-981-treated cells and cotreated hTERT A41hWAT-SVF pre-adipocytes. ( J ) Western blot analysis of PPARG in DMSO, rosiglitazone, TAK-981-treated cells and cotreated hASCs.
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    Image Search Results


    Stable mobilization of CEBPs and PPARG upon transient TAK-981 treatment in pre-adipocytes. ( A ) ATAC-seq experimental layout in hTERT A41hWAT-SVF pre-adipocytes. Time series analysis and hierarchical clustering of significant variations in chromatin accessibility at day 0 (D0), 12 h (12h), and day (D7) after TAK-981 treatment. ( C ) GOBP analysis of ATAC-seq clusters 2 and 6 revealed in panel (B). See and for an analysis of all clusters. ( D – F ) Volcano plots displaying the results of ATAC-seq inferred differential TF activity analyses performed at D0, 12h, and D7 after TAK-981 or DMSO treatment. Colored dots indicate significant differentially mobilized TFs (TAK-981 versus DMSO). Differential binding score >0.05 and pAdj <0.001. ( G ) Time series analysis inferred TF activity over time (TAK-981 versus DMSO) at D0, 12h, and D7 after TAK-981 treatment. ( H ) Western blot analysis of CEBPB SUMOylation in DMSO and TAK-981-treated cells. ( I ) Western blot analysis of CEBPB and PPARG in DMSO, rosiglitazone, TAK-981-treated cells and cotreated hTERT A41hWAT-SVF pre-adipocytes. ( J ) Western blot analysis of PPARG in DMSO, rosiglitazone, TAK-981-treated cells and cotreated hASCs.

    Journal: Nucleic Acids Research

    Article Title: Transient SUMOylation inhibition in human pre-adipocytes stably imprints a transcriptional beiging fate

    doi: 10.1093/nar/gkag232

    Figure Lengend Snippet: Stable mobilization of CEBPs and PPARG upon transient TAK-981 treatment in pre-adipocytes. ( A ) ATAC-seq experimental layout in hTERT A41hWAT-SVF pre-adipocytes. Time series analysis and hierarchical clustering of significant variations in chromatin accessibility at day 0 (D0), 12 h (12h), and day (D7) after TAK-981 treatment. ( C ) GOBP analysis of ATAC-seq clusters 2 and 6 revealed in panel (B). See and for an analysis of all clusters. ( D – F ) Volcano plots displaying the results of ATAC-seq inferred differential TF activity analyses performed at D0, 12h, and D7 after TAK-981 or DMSO treatment. Colored dots indicate significant differentially mobilized TFs (TAK-981 versus DMSO). Differential binding score >0.05 and pAdj <0.001. ( G ) Time series analysis inferred TF activity over time (TAK-981 versus DMSO) at D0, 12h, and D7 after TAK-981 treatment. ( H ) Western blot analysis of CEBPB SUMOylation in DMSO and TAK-981-treated cells. ( I ) Western blot analysis of CEBPB and PPARG in DMSO, rosiglitazone, TAK-981-treated cells and cotreated hTERT A41hWAT-SVF pre-adipocytes. ( J ) Western blot analysis of PPARG in DMSO, rosiglitazone, TAK-981-treated cells and cotreated hASCs.

    Article Snippet: Samples for assay for transposase-accessible chromatin sequencing (ATAC-seq) were prepared based on previously published protocols with the Illumina ATAC-seq library preparation kit (20034197) [ – ].

    Techniques: Activity Assay, Binding Assay, Western Blot

    Cryo-EM structure of raiA motif RNA from Nocardioides sp. Iso805N ( Ns-raiA ) at 3.0 Å resolution. ( A ) Cryo-EM density map of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Pyramid diagrams indicate the orientation of Ns-raiA structure. ( B ) Overlaid cryo-EM densities and models of P1c, P3a, PK1, P5, P6, and P8.

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Cryo-EM structure of raiA motif RNA from Nocardioides sp. Iso805N ( Ns-raiA ) at 3.0 Å resolution. ( A ) Cryo-EM density map of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Pyramid diagrams indicate the orientation of Ns-raiA structure. ( B ) Overlaid cryo-EM densities and models of P1c, P3a, PK1, P5, P6, and P8.

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Cryo-EM Sample Prep

    Tertiary and secondary structures of Ns-raiA . ( A ) Atomic model of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Nucleotides in the conserved UU AGAC GUAA linker connecting PK1 and P6 not resolved in the cryo-EM map are shown as a dotted line. Secondary structures of Ns-raiA are shown in the canonical layout ( B ) as proposed in or in a layout that more closely reflects the tertiary structure ( C ). The nucleotides are colored as in the structure in panel (A). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are indicated with Leontis–Westhof nomenclature symbols (inset) .

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Tertiary and secondary structures of Ns-raiA . ( A ) Atomic model of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Nucleotides in the conserved UU AGAC GUAA linker connecting PK1 and P6 not resolved in the cryo-EM map are shown as a dotted line. Secondary structures of Ns-raiA are shown in the canonical layout ( B ) as proposed in or in a layout that more closely reflects the tertiary structure ( C ). The nucleotides are colored as in the structure in panel (A). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are indicated with Leontis–Westhof nomenclature symbols (inset) .

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Cryo-EM Sample Prep

    Structural comparison of raiA motif RNAs from Nocardioides sp. Iso805N ( Ns-raiA ) , Clostridium acetobutylicum ( Ca-raiA ), and Mogibacterium pumilum ( Mp-raiA ). Cryo-EM density map (left) and atomic model (right) of Ns-raiA ( A ), Ca-raiA ( B ), and Mp-raiA ( C ). The absence of P2 and distal P7 in Ca-raiA and Mp-raiA , and the absence of P8 in Mp-raiA are indicated by dashed lines. Sequence and secondary structure of Ca-raiA ( D ), and Mp-raiA ( E ). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are labeled as indicated. Insets show the schematics of J1 regions. Zoom-in views of the P1c-P2-P3a junction in Ns-raiA ( F ), and the P1c-P3a junctions in Ca-raiA ( G ) and Mp-raiA ( H ), highlighting the GAA(A) tetraloop fold, shown in the same orientation. Zoom-in views of the interface of P8 and PK1 stems in Ns-raiA ( I ) and Ca-raiA ( J ), and the PK1 stem in Mp-raiA ( K ), shown in the same orientation.

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Structural comparison of raiA motif RNAs from Nocardioides sp. Iso805N ( Ns-raiA ) , Clostridium acetobutylicum ( Ca-raiA ), and Mogibacterium pumilum ( Mp-raiA ). Cryo-EM density map (left) and atomic model (right) of Ns-raiA ( A ), Ca-raiA ( B ), and Mp-raiA ( C ). The absence of P2 and distal P7 in Ca-raiA and Mp-raiA , and the absence of P8 in Mp-raiA are indicated by dashed lines. Sequence and secondary structure of Ca-raiA ( D ), and Mp-raiA ( E ). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are labeled as indicated. Insets show the schematics of J1 regions. Zoom-in views of the P1c-P2-P3a junction in Ns-raiA ( F ), and the P1c-P3a junctions in Ca-raiA ( G ) and Mp-raiA ( H ), highlighting the GAA(A) tetraloop fold, shown in the same orientation. Zoom-in views of the interface of P8 and PK1 stems in Ns-raiA ( I ) and Ca-raiA ( J ), and the PK1 stem in Mp-raiA ( K ), shown in the same orientation.

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Comparison, Cryo-EM Sample Prep, Sequencing, Labeling

    Structural details of P1 and its interactions with the core. ( A ) Overall view of P1 (shown as colored ribbon for backbone and filled bases and sugars) and its position relative to the core (colored ribbon) in the structure of Ns-raiA . Other stems are shown as white ribbons. ( B ) Close-up view of the interface between P1 and the core, in dashed box region in panel (A). The two insert panels highlight the long-range A81-G240-G10 stacking and the G10-G14-C242 base triple, respectively. ( C ) Secondary structure representation of the region shown in panel (B). Long-range stacking interactions are indicated by gray dashed lines, while base triple interactions are marked with green lines. ( D ) Representative 2D class averages of To-raiA (left) and enlargement with structure features labeled (right). ( E ) Cryo-EM density map and ribbon model of To-raiA . ( F ) Sequence conservation of raiA motif RNA mapped onto the Ns-raiA structure. View on left highlights conservation of P1 and on right conservation of the core. Conservation scores were calculated using the ConSurf server .

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Structural details of P1 and its interactions with the core. ( A ) Overall view of P1 (shown as colored ribbon for backbone and filled bases and sugars) and its position relative to the core (colored ribbon) in the structure of Ns-raiA . Other stems are shown as white ribbons. ( B ) Close-up view of the interface between P1 and the core, in dashed box region in panel (A). The two insert panels highlight the long-range A81-G240-G10 stacking and the G10-G14-C242 base triple, respectively. ( C ) Secondary structure representation of the region shown in panel (B). Long-range stacking interactions are indicated by gray dashed lines, while base triple interactions are marked with green lines. ( D ) Representative 2D class averages of To-raiA (left) and enlargement with structure features labeled (right). ( E ) Cryo-EM density map and ribbon model of To-raiA . ( F ) Sequence conservation of raiA motif RNA mapped onto the Ns-raiA structure. View on left highlights conservation of P1 and on right conservation of the core. Conservation scores were calculated using the ConSurf server .

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Labeling, Cryo-EM Sample Prep, Sequencing