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 463 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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 103 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 99/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 99/100, based on 552 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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    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.
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    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: 86/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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.
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    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: 99/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore protein purification
    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.
    Protein Purification, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bacterial 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.
    Bacterial Bl21 De3, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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.
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    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.
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    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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    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.
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    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: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rosetta 2
    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.
    Rosetta 2, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1652 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.
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    Millipore bl21 de3 plyss 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.
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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

    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