escherichia coli strains Search Results


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  • 99
    ATCC e coli atcc 25922
    Bacteria inhibitions of 50% solution (v/v) of stingless bees honey, Apis mellifera white and yellow honeys on Staphylococcus aureus (ATCC 25923), Staphylococcus aureus (MRSA), Klebsiella pneumoniae (R), <t>Escherichia</t> coli (ATCC 25922) and Escherichia coli (R).
    E Coli Atcc 25922, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 11390 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore e coli strain bl21
    Bacteria inhibitions of 50% solution (v/v) of stingless bees honey, Apis mellifera white and yellow honeys on Staphylococcus aureus (ATCC 25923), Staphylococcus aureus (MRSA), Klebsiella pneumoniae (R), <t>Escherichia</t> coli (ATCC 25922) and Escherichia coli (R).
    E Coli Strain Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3093 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher e coli strain dh5α
    Bacteria inhibitions of 50% solution (v/v) of stingless bees honey, Apis mellifera white and yellow honeys on Staphylococcus aureus (ATCC 25923), Staphylococcus aureus (MRSA), Klebsiella pneumoniae (R), <t>Escherichia</t> coli (ATCC 25922) and Escherichia coli (R).
    E Coli Strain Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 918 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher e coli strains top10
    (A) Construction of plasmid pCMPG10652. Constitutive promoter P A , gene hpaA , and 4-Hydroxyphenylacetic acid (4-HPA) responsive promoter P BC were copied from plasmid pRA 2 (Prieto and García, 1997 ) and placed in plasmid pFPV25 (Valdivia and Falkow, 1996 ), upstream of gene gfp . This yields GFP production controlled by 4-HPA and 2-Phenylacetic Acid (PAA) concentrations, detected by HpaA. (B) Fluorescence measurements of GFP production of strain pCMPG10652/ E. coli <t>TOP10</t> in response to a range of 4-HPA concentrations. (C) Fluorescence measurements of GFP production of strain pCMPG10652/ E. coli TOP10 in response to a range of PAA concentrations. Auxin concentrations used in fluorescence measurements: 3 mM, 2 mM, 1.5 mM, 1 mM, 500 μM, 250 μM, 125 μM, 62 μM, 31.25 μM, 15.625 μM, and 0M. n = 8 per measured concentration.
    E Coli Strains Top10, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 199 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Stratagene e coli strain xl1 blue
    SDS-PAGE analysis of the PhaP-rPA fusion protein. Lane M, protein marker; lane 1, control; lane 2, lysate of E. coli <t>XL1-Blue</t> (pHBS01/pSPAr); lane 3, PHB granules isolated from E. coli XL1-Blue (pHBS01/pSPAr).
    E Coli Strain Xl1 Blue, supplied by Stratagene, used in various techniques. Bioz Stars score: 91/100, based on 580 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher e coli strain bl21
    Protein analysis of pET-SUMO-E2-T1 expression in E. coli <t>BL21</t> (DE3) . (A) Protein from soluble and insoluble fractions separated by electrophoresis on 10% Bis-Tris gel and stained with Coomassie blue. Lane 1, SeeBlue ® Plus2 MW standard; lane 2, soluble protein fraction at 0 hours; lane 3, insoluble protein fraction at 0 hours; lane 4, soluble protein fraction 2 hours post IPTG induction; lane 5, insoluble protein fraction 2 hours IPTG post induction; lane 6, E2-T1 purified from IB (0.4 μL); lane 7, E2-T1 purified from IB (2 μL). (B) Western blot image of E2-T1 protein expressed in E. coli BL21 (DE3). Equivalent amounts of protein from the soluble and insoluble fractions were transferred to Hybond C and incubated with an anti-his antibody and detected by ECL. Lane 1, soluble protein fraction 0 hours; lane 2, insoluble protein fraction 0 hours; lane 3, soluble protein fraction 2 hours post IPTG induction; lane 4, insoluble protein fraction 2 hours post IPTG induction.
    E Coli Strain Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1486 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore escherichia coli strain bl21 de3
    Protein analysis of pET-SUMO-E2-T1 expression in E. coli <t>BL21</t> (DE3) . (A) Protein from soluble and insoluble fractions separated by electrophoresis on 10% Bis-Tris gel and stained with Coomassie blue. Lane 1, SeeBlue ® Plus2 MW standard; lane 2, soluble protein fraction at 0 hours; lane 3, insoluble protein fraction at 0 hours; lane 4, soluble protein fraction 2 hours post IPTG induction; lane 5, insoluble protein fraction 2 hours IPTG post induction; lane 6, E2-T1 purified from IB (0.4 μL); lane 7, E2-T1 purified from IB (2 μL). (B) Western blot image of E2-T1 protein expressed in E. coli BL21 (DE3). Equivalent amounts of protein from the soluble and insoluble fractions were transferred to Hybond C and incubated with an anti-his antibody and detected by ECL. Lane 1, soluble protein fraction 0 hours; lane 2, insoluble protein fraction 0 hours; lane 3, soluble protein fraction 2 hours post IPTG induction; lane 4, insoluble protein fraction 2 hours post IPTG induction.
    Escherichia Coli Strain Bl21 De3, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 835 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Stratagene escherichia coli strain bl21
    Protein analysis of pET-SUMO-E2-T1 expression in E. coli <t>BL21</t> (DE3) . (A) Protein from soluble and insoluble fractions separated by electrophoresis on 10% Bis-Tris gel and stained with Coomassie blue. Lane 1, SeeBlue ® Plus2 MW standard; lane 2, soluble protein fraction at 0 hours; lane 3, insoluble protein fraction at 0 hours; lane 4, soluble protein fraction 2 hours post IPTG induction; lane 5, insoluble protein fraction 2 hours IPTG post induction; lane 6, E2-T1 purified from IB (0.4 μL); lane 7, E2-T1 purified from IB (2 μL). (B) Western blot image of E2-T1 protein expressed in E. coli BL21 (DE3). Equivalent amounts of protein from the soluble and insoluble fractions were transferred to Hybond C and incubated with an anti-his antibody and detected by ECL. Lane 1, soluble protein fraction 0 hours; lane 2, insoluble protein fraction 0 hours; lane 3, soluble protein fraction 2 hours post IPTG induction; lane 4, insoluble protein fraction 2 hours post IPTG induction.
    Escherichia Coli Strain Bl21, supplied by Stratagene, used in various techniques. Bioz Stars score: 93/100, based on 855 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Millipore escherichia coli strains
    Protein analysis of pET-SUMO-E2-T1 expression in E. coli <t>BL21</t> (DE3) . (A) Protein from soluble and insoluble fractions separated by electrophoresis on 10% Bis-Tris gel and stained with Coomassie blue. Lane 1, SeeBlue ® Plus2 MW standard; lane 2, soluble protein fraction at 0 hours; lane 3, insoluble protein fraction at 0 hours; lane 4, soluble protein fraction 2 hours post IPTG induction; lane 5, insoluble protein fraction 2 hours IPTG post induction; lane 6, E2-T1 purified from IB (0.4 μL); lane 7, E2-T1 purified from IB (2 μL). (B) Western blot image of E2-T1 protein expressed in E. coli BL21 (DE3). Equivalent amounts of protein from the soluble and insoluble fractions were transferred to Hybond C and incubated with an anti-his antibody and detected by ECL. Lane 1, soluble protein fraction 0 hours; lane 2, insoluble protein fraction 0 hours; lane 3, soluble protein fraction 2 hours post IPTG induction; lane 4, insoluble protein fraction 2 hours post IPTG induction.
    Escherichia Coli Strains, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Difco escherichia coli strains
    BinK orthology, conserved domains and squid-adapted binK alleles. ( A ) Unrooted maximum-likelihood (ML) phylogeny of all of the hybrid histidine kinases identified in V. fischeri genomes. Gene families were phylogenetically annotated using <t>Escherichia</t> coli references where possible (not shown), otherwise using the ES114 locus tag. DOI: http://dx.doi.org/10.7554/eLife.24414.006
    Escherichia Coli Strains, supplied by Difco, used in various techniques. Bioz Stars score: 92/100, based on 378 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher e coli strain dh10b
    BinK orthology, conserved domains and squid-adapted binK alleles. ( A ) Unrooted maximum-likelihood (ML) phylogeny of all of the hybrid histidine kinases identified in V. fischeri genomes. Gene families were phylogenetically annotated using <t>Escherichia</t> coli references where possible (not shown), otherwise using the ES114 locus tag. DOI: http://dx.doi.org/10.7554/eLife.24414.006
    E Coli Strain Dh10b, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 378 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Stratagene e coli strain bl21 codonplus de3 ril
    BinK orthology, conserved domains and squid-adapted binK alleles. ( A ) Unrooted maximum-likelihood (ML) phylogeny of all of the hybrid histidine kinases identified in V. fischeri genomes. Gene families were phylogenetically annotated using <t>Escherichia</t> coli references where possible (not shown), otherwise using the ES114 locus tag. DOI: http://dx.doi.org/10.7554/eLife.24414.006
    E Coli Strain Bl21 Codonplus De3 Ril, supplied by Stratagene, used in various techniques. Bioz Stars score: 89/100, based on 358 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher escherichia coli strain bl21 de3
    Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of <t>Escherichia</t> coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain <t>BL21</t> (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.
    Escherichia Coli Strain Bl21 De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 309 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher e coli strain bl21 star de3
    Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of <t>Escherichia</t> coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain <t>BL21</t> (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.
    E Coli Strain Bl21 Star De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 332 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Becton Dickinson escherichia coli strains
    Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of <t>Escherichia</t> coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain <t>BL21</t> (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.
    Escherichia Coli Strains, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 230 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Stratagene e coli strain bl21 de3
    Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of <t>Escherichia</t> coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain <t>BL21</t> (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.
    E Coli Strain Bl21 De3, supplied by Stratagene, used in various techniques. Bioz Stars score: 93/100, based on 493 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Promega escherichia coli strain jm109
    Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of <t>Escherichia</t> coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain <t>BL21</t> (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.
    Escherichia Coli Strain Jm109, supplied by Promega, used in various techniques. Bioz Stars score: 91/100, based on 199 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Bacteria inhibitions of 50% solution (v/v) of stingless bees honey, Apis mellifera white and yellow honeys on Staphylococcus aureus (ATCC 25923), Staphylococcus aureus (MRSA), Klebsiella pneumoniae (R), Escherichia coli (ATCC 25922) and Escherichia coli (R).

    Journal: BMC Complementary and Alternative Medicine

    Article Title: Antibacterial effects of Apis mellifera and stingless bees honeys on susceptible and resistant strains of Escherichia coli, Staphylococcus aureus and Klebsiella pneumoniae in Gondar, Northwest Ethiopia

    doi: 10.1186/1472-6882-13-269

    Figure Lengend Snippet: Bacteria inhibitions of 50% solution (v/v) of stingless bees honey, Apis mellifera white and yellow honeys on Staphylococcus aureus (ATCC 25923), Staphylococcus aureus (MRSA), Klebsiella pneumoniae (R), Escherichia coli (ATCC 25922) and Escherichia coli (R).

    Article Snippet: Discussion The inhibitions of Apis mellifera white Tigray honey (25 mm for Staphylococcus aureus (ATCC 25923) and 22 mm for Escherichia coli (ATCC 25922)) and stingless bees Gojam Tazma honey (27 mm for Staphylococcus aureus (ATCC 25923); 26 mm for Escherichia coli (ATCC 25922)) at concentration of 50% solution (w/v) were as effective as inhibitions of standard tetracycline discs already reported (83).

    Techniques:

    (A) Construction of plasmid pCMPG10652. Constitutive promoter P A , gene hpaA , and 4-Hydroxyphenylacetic acid (4-HPA) responsive promoter P BC were copied from plasmid pRA 2 (Prieto and García, 1997 ) and placed in plasmid pFPV25 (Valdivia and Falkow, 1996 ), upstream of gene gfp . This yields GFP production controlled by 4-HPA and 2-Phenylacetic Acid (PAA) concentrations, detected by HpaA. (B) Fluorescence measurements of GFP production of strain pCMPG10652/ E. coli TOP10 in response to a range of 4-HPA concentrations. (C) Fluorescence measurements of GFP production of strain pCMPG10652/ E. coli TOP10 in response to a range of PAA concentrations. Auxin concentrations used in fluorescence measurements: 3 mM, 2 mM, 1.5 mM, 1 mM, 500 μM, 250 μM, 125 μM, 62 μM, 31.25 μM, 15.625 μM, and 0M. n = 8 per measured concentration.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Design and Construction of a Whole Cell Bacterial 4-Hydroxyphenylacetic Acid and 2-Phenylacetic Acid Bioassay

    doi: 10.3389/fbioe.2015.00088

    Figure Lengend Snippet: (A) Construction of plasmid pCMPG10652. Constitutive promoter P A , gene hpaA , and 4-Hydroxyphenylacetic acid (4-HPA) responsive promoter P BC were copied from plasmid pRA 2 (Prieto and García, 1997 ) and placed in plasmid pFPV25 (Valdivia and Falkow, 1996 ), upstream of gene gfp . This yields GFP production controlled by 4-HPA and 2-Phenylacetic Acid (PAA) concentrations, detected by HpaA. (B) Fluorescence measurements of GFP production of strain pCMPG10652/ E. coli TOP10 in response to a range of 4-HPA concentrations. (C) Fluorescence measurements of GFP production of strain pCMPG10652/ E. coli TOP10 in response to a range of PAA concentrations. Auxin concentrations used in fluorescence measurements: 3 mM, 2 mM, 1.5 mM, 1 mM, 500 μM, 250 μM, 125 μM, 62 μM, 31.25 μM, 15.625 μM, and 0M. n = 8 per measured concentration.

    Article Snippet: All experiments were performed with E. coli TOP10 strains, purchased from Life Technologies Europe.

    Techniques: Plasmid Preparation, Fluorescence, Concentration Assay

    SDS-PAGE analysis of the PhaP-rPA fusion protein. Lane M, protein marker; lane 1, control; lane 2, lysate of E. coli XL1-Blue (pHBS01/pSPAr); lane 3, PHB granules isolated from E. coli XL1-Blue (pHBS01/pSPAr).

    Journal: Applied and Environmental Microbiology

    Article Title: Expression of Active Recombinant Human Tissue-Type Plasminogen Activator by Using In Vivo Polyhydroxybutyrate Granule Display ▿

    doi: 10.1128/AEM.01543-10

    Figure Lengend Snippet: SDS-PAGE analysis of the PhaP-rPA fusion protein. Lane M, protein marker; lane 1, control; lane 2, lysate of E. coli XL1-Blue (pHBS01/pSPAr); lane 3, PHB granules isolated from E. coli XL1-Blue (pHBS01/pSPAr).

    Article Snippet: E. coli strain XL1-Blue [ recA1 endA1 gyrA96 thi-1 hsdR17 supE44 relA1 lac F′ proAB lacI q Z ΔM15 Tn 10 (Tetr )] from Stratagene was used for recombinant protein expression.

    Techniques: SDS Page, Recombinase Polymerase Amplification, Marker, Isolation

    Cell growth and PHB accumulation of recombinant E. coli . The strains were cultivated in LB medium supplemented with 0.5% glucose. (A) Comparison of PHB content and cell mass in E. coli BL21/pHBS01 and XL1-Blue/pHBS01. (B) Fluorescence micrograph

    Journal: Applied and Environmental Microbiology

    Article Title: Expression of Active Recombinant Human Tissue-Type Plasminogen Activator by Using In Vivo Polyhydroxybutyrate Granule Display ▿

    doi: 10.1128/AEM.01543-10

    Figure Lengend Snippet: Cell growth and PHB accumulation of recombinant E. coli . The strains were cultivated in LB medium supplemented with 0.5% glucose. (A) Comparison of PHB content and cell mass in E. coli BL21/pHBS01 and XL1-Blue/pHBS01. (B) Fluorescence micrograph

    Article Snippet: E. coli strain XL1-Blue [ recA1 endA1 gyrA96 thi-1 hsdR17 supE44 relA1 lac F′ proAB lacI q Z ΔM15 Tn 10 (Tetr )] from Stratagene was used for recombinant protein expression.

    Techniques: Recombinant, Fluorescence

    Western blot analysis of the PhaP-rPA fusion protein. Lane M, protein marker; lane 1, control; lane 2, PHB granules isolated from E. coli XL1-Blue (pHBS01/pSPAr).

    Journal: Applied and Environmental Microbiology

    Article Title: Expression of Active Recombinant Human Tissue-Type Plasminogen Activator by Using In Vivo Polyhydroxybutyrate Granule Display ▿

    doi: 10.1128/AEM.01543-10

    Figure Lengend Snippet: Western blot analysis of the PhaP-rPA fusion protein. Lane M, protein marker; lane 1, control; lane 2, PHB granules isolated from E. coli XL1-Blue (pHBS01/pSPAr).

    Article Snippet: E. coli strain XL1-Blue [ recA1 endA1 gyrA96 thi-1 hsdR17 supE44 relA1 lac F′ proAB lacI q Z ΔM15 Tn 10 (Tetr )] from Stratagene was used for recombinant protein expression.

    Techniques: Western Blot, Recombinase Polymerase Amplification, Marker, Isolation

    Fibrin plate analysis of rPA activity. Equal amounts of the samples were spotted on the fibrin plate. (A) Cell debris from E. coli XL1-Blue (pSCP/pSPAr). (B) Isolated PHB granules from E. coli XL1-Blue (pHBS01/pSPAr).

    Journal: Applied and Environmental Microbiology

    Article Title: Expression of Active Recombinant Human Tissue-Type Plasminogen Activator by Using In Vivo Polyhydroxybutyrate Granule Display ▿

    doi: 10.1128/AEM.01543-10

    Figure Lengend Snippet: Fibrin plate analysis of rPA activity. Equal amounts of the samples were spotted on the fibrin plate. (A) Cell debris from E. coli XL1-Blue (pSCP/pSPAr). (B) Isolated PHB granules from E. coli XL1-Blue (pHBS01/pSPAr).

    Article Snippet: E. coli strain XL1-Blue [ recA1 endA1 gyrA96 thi-1 hsdR17 supE44 relA1 lac F′ proAB lacI q Z ΔM15 Tn 10 (Tetr )] from Stratagene was used for recombinant protein expression.

    Techniques: Recombinase Polymerase Amplification, Activity Assay, Isolation

    Selection of Phabs binding to TouRΔA. The number of phage bound to ELISA plates coated with 6xhis TouRΔA after each panning round is indicated. The bound phage were eluted from the plates by incubation with 0.1 M glycine (pH 2.5) as explained in Materials and Methods. After recovery, the titers of these phage were determined on E . coli XL-1 Blue cells and selected for AMP resistance. In each panning round, the number of input phage was kept constant at 2 × 10 11 PFU and the phage that did not bind 6xhis TouRΔA were removed by 40 washing steps with PBS. The increase in the number of bound phage after the second round of panning is indicative of a preferential amplification of Phab clones binding to 6xhis TouRΔA.

    Journal: Journal of Bacteriology

    Article Title: Monitoring Intracellular Levels of XylR in Pseudomonas putida with a Single-Chain Antibody Specific for Aromatic-Responsive Enhancer-Binding Proteins

    doi: 10.1128/JB.183.19.5571-5579.2001

    Figure Lengend Snippet: Selection of Phabs binding to TouRΔA. The number of phage bound to ELISA plates coated with 6xhis TouRΔA after each panning round is indicated. The bound phage were eluted from the plates by incubation with 0.1 M glycine (pH 2.5) as explained in Materials and Methods. After recovery, the titers of these phage were determined on E . coli XL-1 Blue cells and selected for AMP resistance. In each panning round, the number of input phage was kept constant at 2 × 10 11 PFU and the phage that did not bind 6xhis TouRΔA were removed by 40 washing steps with PBS. The increase in the number of bound phage after the second round of panning is indicative of a preferential amplification of Phab clones binding to 6xhis TouRΔA.

    Article Snippet: The E. coli strain XL-1 Blue ( recA1 gyrA96 relA1 endA1 hsdR17 supE44 thi1 lac [F′ proAB lacI q lacZ ΔM15 Tn 10 ] Tcr ; Stratagene) was used as host for bacteriophages and phagemids.

    Techniques: Selection, Binding Assay, Enzyme-linked Immunosorbent Assay, Incubation, Amplification, Clone Assay

    Amino acid sequence of scFv B7. The amino acid sequence of the scFv B7 polypeptide encoded by the phagemid is shown. The positions of the N-terminal signal peptide, the V H domain, the (Gly 4 Ser) 3 linker peptide, the V L domain, and the E tag are indicated. The complementarity-determining regions (CDR) of the V H and V L domains are labeled and underlined. The site of cleavage of the bacterial signal peptidase is marked by an arrow. The five amino acid changes found in the scFv B9 are marked below the sequence of scFv B7. When produced in E . coli XL-1 Blue cells ( supE ), these scFvs are also synthesized as hybrids with protein 3 of M13. The location of the suppressed stop codon (amber), which is placed between the scFv and protein 3 coding sequences, is indicated.

    Journal: Journal of Bacteriology

    Article Title: Monitoring Intracellular Levels of XylR in Pseudomonas putida with a Single-Chain Antibody Specific for Aromatic-Responsive Enhancer-Binding Proteins

    doi: 10.1128/JB.183.19.5571-5579.2001

    Figure Lengend Snippet: Amino acid sequence of scFv B7. The amino acid sequence of the scFv B7 polypeptide encoded by the phagemid is shown. The positions of the N-terminal signal peptide, the V H domain, the (Gly 4 Ser) 3 linker peptide, the V L domain, and the E tag are indicated. The complementarity-determining regions (CDR) of the V H and V L domains are labeled and underlined. The site of cleavage of the bacterial signal peptidase is marked by an arrow. The five amino acid changes found in the scFv B9 are marked below the sequence of scFv B7. When produced in E . coli XL-1 Blue cells ( supE ), these scFvs are also synthesized as hybrids with protein 3 of M13. The location of the suppressed stop codon (amber), which is placed between the scFv and protein 3 coding sequences, is indicated.

    Article Snippet: The E. coli strain XL-1 Blue ( recA1 gyrA96 relA1 endA1 hsdR17 supE44 thi1 lac [F′ proAB lacI q lacZ ΔM15 Tn 10 ] Tcr ; Stratagene) was used as host for bacteriophages and phagemids.

    Techniques: Sequencing, Labeling, Produced, Synthesized

    Protein analysis of pET-SUMO-E2-T1 expression in E. coli BL21 (DE3) . (A) Protein from soluble and insoluble fractions separated by electrophoresis on 10% Bis-Tris gel and stained with Coomassie blue. Lane 1, SeeBlue ® Plus2 MW standard; lane 2, soluble protein fraction at 0 hours; lane 3, insoluble protein fraction at 0 hours; lane 4, soluble protein fraction 2 hours post IPTG induction; lane 5, insoluble protein fraction 2 hours IPTG post induction; lane 6, E2-T1 purified from IB (0.4 μL); lane 7, E2-T1 purified from IB (2 μL). (B) Western blot image of E2-T1 protein expressed in E. coli BL21 (DE3). Equivalent amounts of protein from the soluble and insoluble fractions were transferred to Hybond C and incubated with an anti-his antibody and detected by ECL. Lane 1, soluble protein fraction 0 hours; lane 2, insoluble protein fraction 0 hours; lane 3, soluble protein fraction 2 hours post IPTG induction; lane 4, insoluble protein fraction 2 hours post IPTG induction.

    Journal: Microbial Cell Factories

    Article Title: Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregates

    doi: 10.1186/1475-2859-10-57

    Figure Lengend Snippet: Protein analysis of pET-SUMO-E2-T1 expression in E. coli BL21 (DE3) . (A) Protein from soluble and insoluble fractions separated by electrophoresis on 10% Bis-Tris gel and stained with Coomassie blue. Lane 1, SeeBlue ® Plus2 MW standard; lane 2, soluble protein fraction at 0 hours; lane 3, insoluble protein fraction at 0 hours; lane 4, soluble protein fraction 2 hours post IPTG induction; lane 5, insoluble protein fraction 2 hours IPTG post induction; lane 6, E2-T1 purified from IB (0.4 μL); lane 7, E2-T1 purified from IB (2 μL). (B) Western blot image of E2-T1 protein expressed in E. coli BL21 (DE3). Equivalent amounts of protein from the soluble and insoluble fractions were transferred to Hybond C and incubated with an anti-his antibody and detected by ECL. Lane 1, soluble protein fraction 0 hours; lane 2, insoluble protein fraction 0 hours; lane 3, soluble protein fraction 2 hours post IPTG induction; lane 4, insoluble protein fraction 2 hours post IPTG induction.

    Article Snippet: Positive clones were confirmed by sequencing (AGRF, Brisbane, Australia) and transformed into E. coli strain BL21 (DE3, Invitrogen) cells for protein expression.

    Techniques: Positron Emission Tomography, Expressing, Electrophoresis, Staining, Purification, Western Blot, Incubation

    BinK orthology, conserved domains and squid-adapted binK alleles. ( A ) Unrooted maximum-likelihood (ML) phylogeny of all of the hybrid histidine kinases identified in V. fischeri genomes. Gene families were phylogenetically annotated using Escherichia coli references where possible (not shown), otherwise using the ES114 locus tag. DOI: http://dx.doi.org/10.7554/eLife.24414.006

    Journal: eLife

    Article Title: Host-selected mutations converging on a global regulator drive an adaptive leap towards symbiosis in bacteria

    doi: 10.7554/eLife.24414

    Figure Lengend Snippet: BinK orthology, conserved domains and squid-adapted binK alleles. ( A ) Unrooted maximum-likelihood (ML) phylogeny of all of the hybrid histidine kinases identified in V. fischeri genomes. Gene families were phylogenetically annotated using Escherichia coli references where possible (not shown), otherwise using the ES114 locus tag. DOI: http://dx.doi.org/10.7554/eLife.24414.006

    Article Snippet: Escherichia coli strains were routinely grown in Luria-Bertani (LB) broth ( ) or in brain heart infusion medium (BHI) (Difco) at 37°C.

    Techniques:

    Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of Escherichia coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain BL21 (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Dengue-1 Envelope Protein Domain III along with PELC and CpG Oligodeoxynucleotides Synergistically Enhances Immune Responses

    doi: 10.1371/journal.pntd.0001645

    Figure Lengend Snippet: Expression and purification of recombinant D1ED III. (A) The DNA sequence of the D1ED III gene was derived using codon usage of Escherichia coli and fully synthesized using the assembly PCR method. The PCR product was cloned into the pET22b vector for recombinant D1ED III expression. The recombinant protein contained an additional HHHHHH sequence (HisTag) at the C-terminus and was expressed under the control of the T7 promoter. (B)The recombinant D1ED III protein purification process was monitored using 17.5% reducing SDS-PAGE followed stained by Coomassie Blue staining and immunoblotting using anti-HisTag antibodies. The recombinant D1ED III was expressed in Escherichia coli strain BL21 (DE3). Lane 1, recombinant D1ED III expression after IPTG induction; lane 2, protein expression in the absence of IPTG induction; lane 3, soluble fraction of recombinant D1ED III; lane 4, purified recombinant D1ED III. Lanes 5–8 show immunoblotting to monitor the recombinant D1ED III induction and purification processes, and the samples in these lanes are the same as those in lanes 1–4, respectively. The arrows indicate the electrophoretic positions of recombinant D1ED III in the gels or blots. (C) Recombinant D1ED III was digested with trypsin to assess their peptide mass fingerprinting. The results confirmed that the major peaks in the mass spectra were derived from recombinant D1ED III.

    Article Snippet: The Escherichia coli strain BL21 (DE3) (Invitrogen, Carlsbad, CA) was transformed with the expression plasmid pDen1E3 for protein expression.

    Techniques: Expressing, Purification, Recombinant, Sequencing, Derivative Assay, Synthesized, Polymerase Cycling Assembly, Polymerase Chain Reaction, Clone Assay, Plasmid Preparation, Protein Purification, SDS Page, Staining, Peptide Mass Fingerprinting