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10x protein extraction reagent 0.5x bugbuster  (Merck KGaA)

 
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    Merck KGaA 10x protein extraction reagent 0.5x bugbuster
    10x Protein Extraction Reagent 0.5x Bugbuster, supplied by Merck KGaA, 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/10x protein extraction reagent 0.5x bugbuster/product/Merck KGaA
    Average 90 stars, based on 1 article reviews
    10x protein extraction reagent 0.5x bugbuster - by Bioz Stars, 2026-06
    90/100 stars

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    SDS-PAGE of the supernatant (soluble fractions) and pellets (insoluble fractions) of samples of E. coli BL21(DE3) cell cultivation to produce PdT (53 kDa) or His–TEV–PdT (54.4 kDa) under C1 (temperature reduction 4 h after the beginning of the exponential growth phase). Culture samples were lysed with <t>BugBuster,</t> and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.
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    SDS-PAGE of the supernatant (soluble fractions) and pellets (insoluble fractions) of samples of E. coli BL21(DE3) cell cultivation to produce PdT (53 kDa) or His–TEV–PdT (54.4 kDa) under C1 (temperature reduction 4 h after the beginning of the exponential growth phase). Culture samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Influence of the mRNA initial region on protein production: a case study using recombinant detoxified pneumolysin as a model

    doi: 10.3389/fbioe.2023.1304965

    Figure Lengend Snippet: SDS-PAGE of the supernatant (soluble fractions) and pellets (insoluble fractions) of samples of E. coli BL21(DE3) cell cultivation to produce PdT (53 kDa) or His–TEV–PdT (54.4 kDa) under C1 (temperature reduction 4 h after the beginning of the exponential growth phase). Culture samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.

    Article Snippet: The disruption buffer was composed of BugBuster 10X (EMD Millipore, Billerica, Massachusetts, United States), 20 mM bis-tris (Sigma-Aldrich, St. Louis, Missouri, United States), Benzonase nuclease (EMD Millipore, Burlington, Massachusetts, United States), an EDTA-free protease inhibitor cocktail (Roche Diagnostics GmbH, Mannheim, Germany), and lysozymes (Sigma, St. Louis, Missouri, United States), as recommended by the BugBuster user guide.

    Techniques: SDS Page, Electrophoresis, Marker

    SDS-PAGE of the supernatant (soluble fractions) and pellets (insoluble fractions) of samples of E. coli BL21(DE3) cell cultivation to produce PdT (53 kDa) or His–TEV–PdT (54.4 kDa) under C2 (temperature reduction when glucose was exhausted). Culture samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Influence of the mRNA initial region on protein production: a case study using recombinant detoxified pneumolysin as a model

    doi: 10.3389/fbioe.2023.1304965

    Figure Lengend Snippet: SDS-PAGE of the supernatant (soluble fractions) and pellets (insoluble fractions) of samples of E. coli BL21(DE3) cell cultivation to produce PdT (53 kDa) or His–TEV–PdT (54.4 kDa) under C2 (temperature reduction when glucose was exhausted). Culture samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.

    Article Snippet: The disruption buffer was composed of BugBuster 10X (EMD Millipore, Billerica, Massachusetts, United States), 20 mM bis-tris (Sigma-Aldrich, St. Louis, Missouri, United States), Benzonase nuclease (EMD Millipore, Burlington, Massachusetts, United States), an EDTA-free protease inhibitor cocktail (Roche Diagnostics GmbH, Mannheim, Germany), and lysozymes (Sigma, St. Louis, Missouri, United States), as recommended by the BugBuster user guide.

    Techniques: SDS Page, Electrophoresis, Marker

    Left panel: SDS-PAGE to compare PdT and His–TEV–PdT production in the final wet biomass processed in parallel. Under cultivation C1, the temperature was reduced from 37°C to 25°C 4 h after the beginning of the exponential growth phase, and under C2, the temperature was reduced when glucose was exhausted. Culture samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker. Right panel: Estimated concentration of PdT and His–TEV–PdT in grams per liter of culture, calculated using Eq. .

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Influence of the mRNA initial region on protein production: a case study using recombinant detoxified pneumolysin as a model

    doi: 10.3389/fbioe.2023.1304965

    Figure Lengend Snippet: Left panel: SDS-PAGE to compare PdT and His–TEV–PdT production in the final wet biomass processed in parallel. Under cultivation C1, the temperature was reduced from 37°C to 25°C 4 h after the beginning of the exponential growth phase, and under C2, the temperature was reduced when glucose was exhausted. Culture samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker. Right panel: Estimated concentration of PdT and His–TEV–PdT in grams per liter of culture, calculated using Eq. .

    Article Snippet: The disruption buffer was composed of BugBuster 10X (EMD Millipore, Billerica, Massachusetts, United States), 20 mM bis-tris (Sigma-Aldrich, St. Louis, Missouri, United States), Benzonase nuclease (EMD Millipore, Burlington, Massachusetts, United States), an EDTA-free protease inhibitor cocktail (Roche Diagnostics GmbH, Mannheim, Germany), and lysozymes (Sigma, St. Louis, Missouri, United States), as recommended by the BugBuster user guide.

    Techniques: SDS Page, Electrophoresis, Marker, Concentration Assay

    Left panel: −30:30 region of the mRNA MFE secondary structure predicted by RNAfold for the translation of the pdt gene version 2. The numbers indicate the ribonucleotide position from the beginning of the sequence used as input. Start codons are located from 31 to 33, considering the figure numbers. The colors represent the different structures observed. Green—stems, yellow—interior loops, blue—hairpin loops, and orange—5′ and 3′ unpaired regions. Right panel: SDS-PAGE of the supernatant (soluble fraction—SF) and pellet (insoluble fraction—IF) of the final wet biomass of E. coli BL21 (DE3) cultivation to produce PdT (53 kDa) from gene version 2. Samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Influence of the mRNA initial region on protein production: a case study using recombinant detoxified pneumolysin as a model

    doi: 10.3389/fbioe.2023.1304965

    Figure Lengend Snippet: Left panel: −30:30 region of the mRNA MFE secondary structure predicted by RNAfold for the translation of the pdt gene version 2. The numbers indicate the ribonucleotide position from the beginning of the sequence used as input. Start codons are located from 31 to 33, considering the figure numbers. The colors represent the different structures observed. Green—stems, yellow—interior loops, blue—hairpin loops, and orange—5′ and 3′ unpaired regions. Right panel: SDS-PAGE of the supernatant (soluble fraction—SF) and pellet (insoluble fraction—IF) of the final wet biomass of E. coli BL21 (DE3) cultivation to produce PdT (53 kDa) from gene version 2. Samples were lysed with BugBuster, and a protein amount corresponding to OD 600 of 5.0 was applied per lane. Electrophoresis with 12% gels was conducted under reducing conditions. MM: molecular marker.

    Article Snippet: The disruption buffer was composed of BugBuster 10X (EMD Millipore, Billerica, Massachusetts, United States), 20 mM bis-tris (Sigma-Aldrich, St. Louis, Missouri, United States), Benzonase nuclease (EMD Millipore, Burlington, Massachusetts, United States), an EDTA-free protease inhibitor cocktail (Roche Diagnostics GmbH, Mannheim, Germany), and lysozymes (Sigma, St. Louis, Missouri, United States), as recommended by the BugBuster user guide.

    Techniques: Sequencing, SDS Page, Electrophoresis, Marker