bl21 de3 Millipore Search Results


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  • 99
    Millipore e coli bl 21
    Expression analysis of recombinant ADAMTS1 in E. coli <t>BL21</t> (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.
    E Coli Bl 21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1404 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Millipore bl21 de3 millipore sigma
    Expression analysis of recombinant ADAMTS1 in E. coli <t>BL21</t> (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.
    Bl21 De3 Millipore Sigma, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore bl 21 de 3
    Expression analysis of recombinant ADAMTS1 in E. coli <t>BL21</t> (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.
    Bl 21 De 3, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 122 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore competent cells
    Expression analysis of recombinant ADAMTS1 in E. coli <t>BL21</t> (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.
    Competent Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore bl21 de3 plyss
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Bl21 De3 Plyss, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 554 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore competent bl21 de3
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Competent Bl21 De3, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore escherichiacoli bl21
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Escherichiacoli Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore bl21 de3 ril
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Bl21 De3 Ril, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Merck KGaA bl21
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Bl21, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 94/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore bl21 de3 r3 rosetta
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Bl21 De3 R3 Rosetta, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore rosetta bl21
    Expression of UspF protein by an IPTG‐inducible E. coli <t>BL21</t> (DE3) <t>pLyS</t> strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.
    Rosetta Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore bl21 de3 rosetta
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Bl21 De3 Rosetta, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore bl21 de3 trxb
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Bl21 De3 Trxb, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore bacterial bl21 de3
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Bacterial Bl21 De3, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore protein purification
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Protein Purification, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Merck KGaA coli bl21
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Coli Bl21, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 89/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore bl21 de3 star
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Bl21 De3 Star, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore rosetta2
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Rosetta2, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1222 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore bl21 de3 t1r bacteria
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Bl21 De3 T1r Bacteria, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bl21 de3 gold cells
    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, <t>BL21</t> Gold, BL21 Codon (+) and BL21 <t>Rosetta</t> in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.
    Bl21 De3 Gold Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bl21 de3 plyss rosetta
    Purification of SXT-Exo and lambda-Exo, and determination of their multimericity by size exclusion chromatography . Panel A : Size exclusion chromatogram of purified SXT-Exo protein expressed from plasmid pEA1-1. Panel B : Size exclusion chromatogram of purified lambda-Exo protein expressed from plasmid pEE4. Panel C : 12% polyacrylamide gel (SDS-PAGE) analysis of the SXT-Exo purification procedure and purified SXT-Bet, SXT-Ssb, lambda-Bet and lambda-Exo proteins; lane 1: Benchmark protein ladder (Invitrogen); lane 2: pEA1-1/ E. coli <t>BL21</t> (DE3) <t>pLysS</t> <t>Rosetta</t> whole cell extract immediately prior to induction; lane 3: whole cell extract 6 hours after induction with IPTG; lane 4: supernatant from cell extract 6 hours post induction; lane 5: purified SXT-Exo; lane 6: purified SXT-Bet expressed from pX28-1; lane 7: purified SXT-Ssb expressed from pSB2; lane 8: purified lambda-Bet expressed from p1DB; lane 9: purified lambda-Exo expressed from pEE4.
    Bl21 De3 Plyss Rosetta, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Millipore strain bl21∷de3
    Purification of SXT-Exo and lambda-Exo, and determination of their multimericity by size exclusion chromatography . Panel A : Size exclusion chromatogram of purified SXT-Exo protein expressed from plasmid pEA1-1. Panel B : Size exclusion chromatogram of purified lambda-Exo protein expressed from plasmid pEE4. Panel C : 12% polyacrylamide gel (SDS-PAGE) analysis of the SXT-Exo purification procedure and purified SXT-Bet, SXT-Ssb, lambda-Bet and lambda-Exo proteins; lane 1: Benchmark protein ladder (Invitrogen); lane 2: pEA1-1/ E. coli <t>BL21</t> (DE3) <t>pLysS</t> <t>Rosetta</t> whole cell extract immediately prior to induction; lane 3: whole cell extract 6 hours after induction with IPTG; lane 4: supernatant from cell extract 6 hours post induction; lane 5: purified SXT-Exo; lane 6: purified SXT-Bet expressed from pX28-1; lane 7: purified SXT-Ssb expressed from pSB2; lane 8: purified lambda-Bet expressed from p1DB; lane 9: purified lambda-Exo expressed from pEE4.
    Strain Bl21∷De3, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Purification of SXT-Exo and lambda-Exo, and determination of their multimericity by size exclusion chromatography . Panel A : Size exclusion chromatogram of purified SXT-Exo protein expressed from plasmid pEA1-1. Panel B : Size exclusion chromatogram of purified lambda-Exo protein expressed from plasmid pEE4. Panel C : 12% polyacrylamide gel (SDS-PAGE) analysis of the SXT-Exo purification procedure and purified SXT-Bet, SXT-Ssb, lambda-Bet and lambda-Exo proteins; lane 1: Benchmark protein ladder (Invitrogen); lane 2: pEA1-1/ E. coli <t>BL21</t> (DE3) <t>pLysS</t> <t>Rosetta</t> whole cell extract immediately prior to induction; lane 3: whole cell extract 6 hours after induction with IPTG; lane 4: supernatant from cell extract 6 hours post induction; lane 5: purified SXT-Exo; lane 6: purified SXT-Bet expressed from pX28-1; lane 7: purified SXT-Ssb expressed from pSB2; lane 8: purified lambda-Bet expressed from p1DB; lane 9: purified lambda-Exo expressed from pEE4.
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    Purification of SXT-Exo and lambda-Exo, and determination of their multimericity by size exclusion chromatography . Panel A : Size exclusion chromatogram of purified SXT-Exo protein expressed from plasmid pEA1-1. Panel B : Size exclusion chromatogram of purified lambda-Exo protein expressed from plasmid pEE4. Panel C : 12% polyacrylamide gel (SDS-PAGE) analysis of the SXT-Exo purification procedure and purified SXT-Bet, SXT-Ssb, lambda-Bet and lambda-Exo proteins; lane 1: Benchmark protein ladder (Invitrogen); lane 2: pEA1-1/ E. coli <t>BL21</t> (DE3) <t>pLysS</t> <t>Rosetta</t> whole cell extract immediately prior to induction; lane 3: whole cell extract 6 hours after induction with IPTG; lane 4: supernatant from cell extract 6 hours post induction; lane 5: purified SXT-Exo; lane 6: purified SXT-Bet expressed from pX28-1; lane 7: purified SXT-Ssb expressed from pSB2; lane 8: purified lambda-Bet expressed from p1DB; lane 9: purified lambda-Exo expressed from pEE4.
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    SDS-PAGE analysis of a the purified native ckGL from C. kessleri and b recombinant ckGL (rckGL) produced in E. coli <t>BL21</t> . Lane M, protein molecular mass markers; lane 1, purified enzyme (2.9 μg protein); lane 2, recombinant enzyme in TF-ckGL form (0.1 μg); lane 3, rckGL (0.1 μg) produced from TF-ckGL by digestion with Factor Xa. The SDS-PAGE gels a and b were stained with Coomassie Brilliant Blue R-250 and Simply Blue Safe Stain (G-250), respectively
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    Image Search Results


    Expression analysis of recombinant ADAMTS1 in E. coli BL21 (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.

    Journal: Molecules

    Article Title: Fluorescence Resonance Energy Transfer Assay for High-Throughput Screening of ADAMTS1 Inhibitors

    doi: 10.3390/molecules161210709

    Figure Lengend Snippet: Expression analysis of recombinant ADAMTS1 in E. coli BL21 (DE3). ( A ) SDS-PAGE analysis of recombinant ADAMTS1 induced by IPTG. Lane 1: uninduced bacteria lysate; lane 2: IPTG wholly induced bacteria lysate; lane 3: supernatant of bacteria lysate; lane 4: precipitation of bacteria lysate; ( B ) SDS-PAGE analysis of purified fusion ADAMTS1 and ADAMTS1 on the Coomassie brilliant blue-stained gel; ( C ) Western blot analysis of purified fusion ADAMTS1 and ADAMTS1. Lane 1: purified fusion protein with NTA column; lane 2: the final purified protein after removal of thioredoxin using heparin-sepharose column.

    Article Snippet: Materials E . coli BL21 (DE3), E. coli DH5a, pET32a(+) vector and his-bind purification kit were purchased from Novagen.

    Techniques: Expressing, Recombinant, SDS Page, Purification, Staining, Western Blot

    Analysis of fusion protein by SDS-PAGE and Western blot. (a) Expression and purification of IFN-CSP. Lane M: protein molecular weight marker. Lanes 1 and 2: total proteins of E. coli BL21/pET-21b-IFN-CSP before and after induction. Lanes 3 and 4: supernatant and precipitation after ultrasonication and centrifugation. Lane 5: purified IFN-CSP using Ni affinity chromatography. Lane 6: Purified IFN-CSP using HiTrap affinity chromatography. (b) IFN-CSP was analyzed by SDS-PAGE, transferred to PVDF membrane, and detected by goat polyclonal anti-human IFN α antibody. Lane M: protein molecular weight marker. Lanes 1 and 2: total proteins of E. coli BL21/pET-21b-IFN-CSP before and after induction.

    Journal: BioMed Research International

    Article Title: Construction of a Novel Liver-Targeting Fusion Interferon by Incorporation of a Plasmodium Region I-Plus Peptide

    doi: 10.1155/2014/261631

    Figure Lengend Snippet: Analysis of fusion protein by SDS-PAGE and Western blot. (a) Expression and purification of IFN-CSP. Lane M: protein molecular weight marker. Lanes 1 and 2: total proteins of E. coli BL21/pET-21b-IFN-CSP before and after induction. Lanes 3 and 4: supernatant and precipitation after ultrasonication and centrifugation. Lane 5: purified IFN-CSP using Ni affinity chromatography. Lane 6: Purified IFN-CSP using HiTrap affinity chromatography. (b) IFN-CSP was analyzed by SDS-PAGE, transferred to PVDF membrane, and detected by goat polyclonal anti-human IFN α antibody. Lane M: protein molecular weight marker. Lanes 1 and 2: total proteins of E. coli BL21/pET-21b-IFN-CSP before and after induction.

    Article Snippet: Bacterial Strains, Plasmids, and Culture Media E. coli strain DH5α (Novagen, USA) and BL21 (DE3; Novagen, USA) were used as the host for gene manipulation and expression of fusion protein, respectively. pMD20-T (Takara, Japan) and pET-21b (Novagen, USA) were applied for gene cloning and expression, respectively.

    Techniques: SDS Page, Western Blot, Expressing, Purification, Molecular Weight, Marker, Positron Emission Tomography, Centrifugation, Affinity Chromatography

    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami DE3 and BL21 DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.

    Journal: PLoS ONE

    Article Title: The Quiescin Sulfhydryl Oxidase (hQSOX1b) Tunes the Expression of Resistin-Like Molecule Alpha (RELM-? or mFIZZ1) in a Wheat Germ Cell-Free Extract

    doi: 10.1371/journal.pone.0055621

    Figure Lengend Snippet: mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami DE3 and BL21 DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.

    Article Snippet: Plasmid DNA of mFIZZ1 was transformed into E. coli SHuffle™ T7 Express (BioLabs), Origami™ DE3 and BL21 DE3 (Novagen), grown in LB medium supplemented with 25 µg/ml ampicillin, induced at a cell density (OD600 nm ) of 0.7 with 1 mM isopropyl-b-D-thiogalactopyranoside (IPTG), and cultured for 6 h at 37°C except for SHuffle™ T7 cells, the expression done at 30°C.

    Techniques: Expressing, SDS Page, Staining, Stripping Membranes, Marker

    12% (w/v) SDS-PAGE analysis of recombinant Ldc1E. Lane 1, molecular mass standards. Lane 2, total protein of E . coli BL21 (DE3) pLysS harboring empty pET30a(+) (control). Lane 3, total protein of E . coli BL21 (DE3) pLysS harboring the recombinant ldc1E in pET30a(+). and Lane 4, protein was purified using the Ni-NTA column method. The black arrow indicates the recombinant Ldc1E.

    Journal: PLoS ONE

    Article Title: Identification and molecular characterization of a metagenome-derived L-lysine decarboxylase gene from subtropical soil microorganisms

    doi: 10.1371/journal.pone.0185060

    Figure Lengend Snippet: 12% (w/v) SDS-PAGE analysis of recombinant Ldc1E. Lane 1, molecular mass standards. Lane 2, total protein of E . coli BL21 (DE3) pLysS harboring empty pET30a(+) (control). Lane 3, total protein of E . coli BL21 (DE3) pLysS harboring the recombinant ldc1E in pET30a(+). and Lane 4, protein was purified using the Ni-NTA column method. The black arrow indicates the recombinant Ldc1E.

    Article Snippet: Plasmid pET-30a(+) (Novagen) and bacterial strain E . coli BL21 (DE3) pLysS (Novagen) were used as the expression vector and host, respectively.

    Techniques: SDS Page, Recombinant, Purification

    RP-HPLC separation of the heated cellular extract. Cellular extract of E. coli BL21 [DE3] (pMA24) were treated as described in Section 2.4 . Chromatogram was monitored at (A) λ = 220 nm and (B) λ = 280 nm. Peaks were collected and individually analyzed by MALDI-TOF MS.

    Journal: FEBS Open Bio

    Article Title: A new hybrid bacteriocin, Ent35-MccV, displays antimicrobial activity against pathogenic Gram-positive and Gram-negative bacteria

    doi: 10.1016/j.fob.2012.01.002

    Figure Lengend Snippet: RP-HPLC separation of the heated cellular extract. Cellular extract of E. coli BL21 [DE3] (pMA24) were treated as described in Section 2.4 . Chromatogram was monitored at (A) λ = 220 nm and (B) λ = 280 nm. Peaks were collected and individually analyzed by MALDI-TOF MS.

    Article Snippet: 2.3 Gene expression and bacteriocins purification for activity determinations Ent35–MccV was expressed from pMA24 in E. coli BL21 [DE3] (pLysS) grown in LB (Sigma) at 37 °C.

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry

    Expression of UspF protein by an IPTG‐inducible E. coli BL21 (DE3) pLyS strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Characterization of the universal stress protein F from atypical enteropathogenic Escherichia coli and its prevalence in Enterobacteriaceae

    doi: 10.1002/pro.3038

    Figure Lengend Snippet: Expression of UspF protein by an IPTG‐inducible E. coli BL21 (DE3) pLyS strain and purification of soluble fractions containing UspF protein. A – T0 total protein extract before induction; T2, total protein extract after induction (3 h); T3, total protein extract after induction (16–18 h). The arrow indicates position of the UspF protein (18.4 kDa). B – Purification of soluble fractions or UspF protein by affinity chromatography using a nickel‐containing resin. 1–Flow through; 2–30 m M , 3–50 m M , 4–100 m M ; 5–200 m M of imidazole.

    Article Snippet: Bacterial strains and plasmids The following E. coli K12 strains were used: DH10b (Stratagene, USA) and BL21 (DE3) pLyS (Novagen, USA).

    Techniques: Expressing, Purification, Affinity Chromatography, Flow Cytometry

    Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, BL21 Gold, BL21 Codon (+) and BL21 Rosetta in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.

    Journal: Protein expression and purification

    Article Title: A cost-effective protocol for the over-expression and purification of fully-functional and more stable Erwinia chrisanthemi ligand-gated ion channel

    doi: 10.1016/j.pep.2017.03.006

    Figure Lengend Snippet: Optimization of conditions for the overexpression of ELIC 1a . A cartoon representation of ELIC highlighting the membrane spanning pore forming domain (red helices), the extracellular domain (yellow B-sheets), and the boundaries of the cell membrane in relation to the channel structure. 1b . Upper panel, a western blot analysis of the expression levels of the ELIC channel made in the E. coli strains: C41, C43, BL21 Gold, BL21 Codon (+) and BL21 Rosetta in the following growth media: Terrific Broth (TB, yellow), Auto-Induction medium (AI, blue) and LB medium (red). Lower panel, normalized ELIC band density from the western blot (Penta-histidine antibody) were plotted against E. coli strains grouped by growth media. 1c. The effect of the cell culture volume on ELIC expression levels and final culture biomass was studied for the three most promising E. coli strains: BL21 Gold, BL21 Codon (+) and BL21 Rosetta. 1d. The effect of Zn 2+ and Mg 2+ as channel negative modifiers or the competitive antagonist ACh on ELIC expression levels is represented as a bar plot.

    Article Snippet: E. coli strains: BL21 DE3 Gold, BL21 DE3 Codon (+), BL21 DE3 Rosetta (Novagen), C41, and C43 (Lucigen) were tested for their ability to express the MBP-ELIC fusion protein in sufficient quantity and quality.

    Techniques: Over Expression, Western Blot, Expressing, Cell Culture

    Purification of SXT-Exo and lambda-Exo, and determination of their multimericity by size exclusion chromatography . Panel A : Size exclusion chromatogram of purified SXT-Exo protein expressed from plasmid pEA1-1. Panel B : Size exclusion chromatogram of purified lambda-Exo protein expressed from plasmid pEE4. Panel C : 12% polyacrylamide gel (SDS-PAGE) analysis of the SXT-Exo purification procedure and purified SXT-Bet, SXT-Ssb, lambda-Bet and lambda-Exo proteins; lane 1: Benchmark protein ladder (Invitrogen); lane 2: pEA1-1/ E. coli BL21 (DE3) pLysS Rosetta whole cell extract immediately prior to induction; lane 3: whole cell extract 6 hours after induction with IPTG; lane 4: supernatant from cell extract 6 hours post induction; lane 5: purified SXT-Exo; lane 6: purified SXT-Bet expressed from pX28-1; lane 7: purified SXT-Ssb expressed from pSB2; lane 8: purified lambda-Bet expressed from p1DB; lane 9: purified lambda-Exo expressed from pEE4.

    Journal: BMC Molecular Biology

    Article Title: Functional characterization of an alkaline exonuclease and single strand annealing protein from the SXT genetic element of Vibrio cholerae

    doi: 10.1186/1471-2199-12-16

    Figure Lengend Snippet: Purification of SXT-Exo and lambda-Exo, and determination of their multimericity by size exclusion chromatography . Panel A : Size exclusion chromatogram of purified SXT-Exo protein expressed from plasmid pEA1-1. Panel B : Size exclusion chromatogram of purified lambda-Exo protein expressed from plasmid pEE4. Panel C : 12% polyacrylamide gel (SDS-PAGE) analysis of the SXT-Exo purification procedure and purified SXT-Bet, SXT-Ssb, lambda-Bet and lambda-Exo proteins; lane 1: Benchmark protein ladder (Invitrogen); lane 2: pEA1-1/ E. coli BL21 (DE3) pLysS Rosetta whole cell extract immediately prior to induction; lane 3: whole cell extract 6 hours after induction with IPTG; lane 4: supernatant from cell extract 6 hours post induction; lane 5: purified SXT-Exo; lane 6: purified SXT-Bet expressed from pX28-1; lane 7: purified SXT-Ssb expressed from pSB2; lane 8: purified lambda-Bet expressed from p1DB; lane 9: purified lambda-Exo expressed from pEE4.

    Article Snippet: Protein expression was performed in E. coli BL21 (DE3) or BL21 (DE3) pLysS Rosetta (Novagen); inducing expression by the addition of isopropyl-1-thio-β-D-galactopyranoside (IPTG, USB) to between 0.1 to 0.5 mM; incubating cultures post-induction at 20-37°C.

    Techniques: Purification, Size-exclusion Chromatography, Plasmid Preparation, SDS Page

    SDS-PAGE analysis of a the purified native ckGL from C. kessleri and b recombinant ckGL (rckGL) produced in E. coli BL21 . Lane M, protein molecular mass markers; lane 1, purified enzyme (2.9 μg protein); lane 2, recombinant enzyme in TF-ckGL form (0.1 μg); lane 3, rckGL (0.1 μg) produced from TF-ckGL by digestion with Factor Xa. The SDS-PAGE gels a and b were stained with Coomassie Brilliant Blue R-250 and Simply Blue Safe Stain (G-250), respectively

    Journal: Applied Microbiology and Biotechnology

    Article Title: A novel galactolipase from a green microalga Chlorella kessleri: purification, characterization, molecular cloning, and heterologous expression

    doi: 10.1007/s00253-017-8713-7

    Figure Lengend Snippet: SDS-PAGE analysis of a the purified native ckGL from C. kessleri and b recombinant ckGL (rckGL) produced in E. coli BL21 . Lane M, protein molecular mass markers; lane 1, purified enzyme (2.9 μg protein); lane 2, recombinant enzyme in TF-ckGL form (0.1 μg); lane 3, rckGL (0.1 μg) produced from TF-ckGL by digestion with Factor Xa. The SDS-PAGE gels a and b were stained with Coomassie Brilliant Blue R-250 and Simply Blue Safe Stain (G-250), respectively

    Article Snippet: E. coli JM109 (Takara Bio., Shiga, Japan) was commonly used as the host strain for molecular cloning and strain BL21 (Novagen, Madison, WI) was employed for functional expression of ckGL.

    Techniques: SDS Page, Purification, Recombinant, Produced, Staining

    Sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) analysis of recombinant hG31P-P-113 expressed in E. coli BL21.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: High Level Expression and Purification of the Clinically Active Antimicrobial Peptide P-113 in Escherichia coli

    doi: 10.3390/molecules23040800

    Figure Lengend Snippet: Sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) analysis of recombinant hG31P-P-113 expressed in E. coli BL21.

    Article Snippet: Materials and Methods The expression vector pET-28a and host BL21 (DE3) were purchased from Novagen (Merck Millipore, Burlington, MA, USA).

    Techniques: Polyacrylamide Gel Electrophoresis, Recombinant