escherichia coli strains Thermo Fisher Search Results


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  • 99
    Thermo Fisher one shot 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.
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    98
    Thermo Fisher competent escherichia coli
    (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.
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    99
    Thermo Fisher e coli strain dh5α
    (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 Strain Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1088 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 1508 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher e coli strain dh10b
    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 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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    99
    Thermo Fisher one shot bl21 de3 chemically competent e coli
    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.
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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 competent e coli top10 cells
    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.
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    99
    Thermo Fisher e coli bl21
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    E Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4872 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher e coli strain bl21 star de3
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    E Coli Strain Bl21 Star De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 418 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher one shot top10 competent cells
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    One Shot Top10 Competent Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 719 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher escherichia coli strain top10f
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    Escherichia Coli Strain Top10f, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 191 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher multishot stripwell dh5α t1r competent cells
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    Multishot Stripwell Dh5α T1r Competent Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher escherichia coli strains
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    Escherichia Coli Strains, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 361 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher one shot stbl3
    Spot assays used for monitoring the growth performance of <t>BL21/pEZYHb</t> and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress
    One Shot Stbl3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 363 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    (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

    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

    Example of the Western blots used to estimate relative expression levels . Proteins were expressed in strain BL21-AI at 37°C. Whole cell extracts were subjected to SDS-PAGE and transferred to membranes. The blots were probed with anti-6-His antibodies. Overall, approximately 65% of the proteins were expressed in at least one condition, and the sizes of most of the expressed proteins were found to correspond approximately with their predicted sizes. Lane 1 PA2628 (MW = 32 kDa), Lane 2 Control 6-His tagged protein (MW = 60 kDa), Lane 3 PA3773 (MW = 39 kDa), Lane 4 PA5291 (MW = 73 kDa), Lane 5 Molecular weight markers with weights given in kDA, Lane 6 PA4083 (MW = 26 kDa), Lane 7 PA4417 (MW = 51 kDa), Lane 8 PA5199 (MW = 49 kDa).

    Journal: BMC Biotechnology

    Article Title: Recombinant Expression Screening of P. aeruginosa Bacterial Inner Membrane Proteins

    doi: 10.1186/1472-6750-10-83

    Figure Lengend Snippet: Example of the Western blots used to estimate relative expression levels . Proteins were expressed in strain BL21-AI at 37°C. Whole cell extracts were subjected to SDS-PAGE and transferred to membranes. The blots were probed with anti-6-His antibodies. Overall, approximately 65% of the proteins were expressed in at least one condition, and the sizes of most of the expressed proteins were found to correspond approximately with their predicted sizes. Lane 1 PA2628 (MW = 32 kDa), Lane 2 Control 6-His tagged protein (MW = 60 kDa), Lane 3 PA3773 (MW = 39 kDa), Lane 4 PA5291 (MW = 73 kDa), Lane 5 Molecular weight markers with weights given in kDA, Lane 6 PA4083 (MW = 26 kDa), Lane 7 PA4417 (MW = 51 kDa), Lane 8 PA5199 (MW = 49 kDa).

    Article Snippet: Expression Studies Destination Vectors were used to transform E. coli strain Bl21-AI (F-ompT hsdSB (rB-mB-) gal dcm araB::T7RNAP-tetA) (Invitrogen) (with lon and ompT protease deficiencies (Invitrogen), which has the T7 RNA polymerase under the control of the araBAD promoter for inducible expression, and E. coli strain C43(DE3) (which was derived fromBL21(DE3) [E. coli F-ompT hsdSB (rB-mB-) gal dcm (DE3)]) [ ].

    Techniques: Western Blot, Expressing, SDS Page, Molecular Weight

    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

    Spot assays used for monitoring the growth performance of BL21/pEZYHb and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress

    Journal: BMC Genomics

    Article Title: The alcohol dehydrogenase gene family in sugarcane and its involvement in cold stress regulation

    doi: 10.1186/s12864-020-06929-9

    Figure Lengend Snippet: Spot assays used for monitoring the growth performance of BL21/pEZYHb and BL21/pEZYHb- ScADH3 transformed E. coli cells on LB plates under cold stress. The growth performance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells on LB plates without supplements or stresses were used as controls. After spotting the sample on LB agar plates, incubation at 4 °C in darkness for 3 days, 7 days, and 14 days was used to study the tolerance of BL21/pEZYHb and BL21/ pEZYHb- ScADH3 cells under cold stress

    Article Snippet: E. coli BL21 with the empty vector pEZYHb was used as the control.

    Techniques: Transformation Assay, Incubation