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e. coli strain bl21 star (de3)  (Thermo Fisher)


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    Structured Review

    Thermo Fisher e. coli strain bl21 star (de3)
    E. Coli Strain Bl21 Star (De3), supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e%2E+coli+strain+bl21+star+(de3/e++coli+bl21++de3+/pm40616520-704-0-6
    Average 90 stars, based on 1 article reviews
    e. coli strain bl21 star (de3) - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Construct:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    Transformation Assay:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    Expressing:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    Recombinant:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    Purification:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    Mutagenesis:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    SDS Page:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.

    Western Blot:

    Article Title: Requirements for Septal Localization and Chromosome Segregation Activity of the DNA Translocase SftA from Bacillus subtilis.
    Article Snippet: E. coli strain XL1-Blue (Stratagene) was used for the construction and propagation of plasmids and E. coli strain BL21 Star DE3 (Invitrogen) for the heterologous overexpression of proteins.

    Article Title: Mutation of cysteine 21 inhibits nucleophosmin/B23 oligomerization and chaperone activity
    Article Snippet: This construct was transformed into E. Coli strain BL21 Star DE3 (Invitrogen, La Jolla, CA) for GST-fusion protein expression.

    Article Title: Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase fromTrametes multicolor
    Article Snippet: Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates.. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively.. Using oxygen as electron acceptor the mutant T169G was equally active with D-glucose and D-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate.



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    (a) Schematic representation of the pipeline for growth factor candidate selection and cell-based testing. (b) Western blot analysis of 11 high-value CFPS-derived growth factors. FGF-1, FGF-2, FGF-10, TNF-α, IL-1β, IFN-γ, and IL-15 were expressed in <t>E.</t> <t>coli</t> <t>BL21</t> <t>(DE3)</t> in-house cell-free lysates. IL-6, EGF, IGF-1, and IL-3 were expressed in SHuffle-based in-house cell-free lysates. Detection was performed using an anti-His- HRP antibody. Data shown are from one representative biological replicate out of three independent experiments. (c) In vitro proliferation assay comparing on-demand, locally produced in Canada (blue) and commercial (green) FGF-1 growth factors in NIH-3T3 cells. Cells were individually treated with varying concentrations (1, 5, 10, 50, 500, and 1000 ng/mL) of growth factor. Luminescence was measured using a conventional plate reader. Data are shown as mean ± SD, n = 3. (d) In vitro proliferation assay comparing on-demand, locally produced (blue) and commercial (green) IL-3 growth factors in TF-1 cells. Cells were individually treated with varying concentrations (0.025, 0.05, 0.1, 0.5, 1, and 5 ng/mL). This representative data was obtained using reagents produced on-site in Canada. Data are shown as mean ± SD, n = 3. (e) Growth factor expression and cell-based validation in a low-resource setting. In vitro proliferation assay using FGF-1 and NIH-3T3 cells. Cells were individually treated with varying concentrations (1, 5, 10, 50, 500, and 1000 ng/mL) of both in-house-produced (blue) and commercial (green) growth factors. This representative data was obtained using reagents produced on-site in Brazil. Relative fold proliferation was plotted as the fold-change compared to untreated, serum-starved cells under the same experimental conditions. Data are shown as mean ± SD, n = 3. Statistical differences were determined by two-way ANOVA with Šídák’s post hoc multiple comparisons test: ns p > 0.05, * p < 0.05, ** p < 0.01, *** p < 0.001. Abbreviations are: ns, not significantly different; kDa, kilodaltons.
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    Image Search Results


    (a) Schematic representation of the pipeline for growth factor candidate selection and cell-based testing. (b) Western blot analysis of 11 high-value CFPS-derived growth factors. FGF-1, FGF-2, FGF-10, TNF-α, IL-1β, IFN-γ, and IL-15 were expressed in E. coli BL21 (DE3) in-house cell-free lysates. IL-6, EGF, IGF-1, and IL-3 were expressed in SHuffle-based in-house cell-free lysates. Detection was performed using an anti-His- HRP antibody. Data shown are from one representative biological replicate out of three independent experiments. (c) In vitro proliferation assay comparing on-demand, locally produced in Canada (blue) and commercial (green) FGF-1 growth factors in NIH-3T3 cells. Cells were individually treated with varying concentrations (1, 5, 10, 50, 500, and 1000 ng/mL) of growth factor. Luminescence was measured using a conventional plate reader. Data are shown as mean ± SD, n = 3. (d) In vitro proliferation assay comparing on-demand, locally produced (blue) and commercial (green) IL-3 growth factors in TF-1 cells. Cells were individually treated with varying concentrations (0.025, 0.05, 0.1, 0.5, 1, and 5 ng/mL). This representative data was obtained using reagents produced on-site in Canada. Data are shown as mean ± SD, n = 3. (e) Growth factor expression and cell-based validation in a low-resource setting. In vitro proliferation assay using FGF-1 and NIH-3T3 cells. Cells were individually treated with varying concentrations (1, 5, 10, 50, 500, and 1000 ng/mL) of both in-house-produced (blue) and commercial (green) growth factors. This representative data was obtained using reagents produced on-site in Brazil. Relative fold proliferation was plotted as the fold-change compared to untreated, serum-starved cells under the same experimental conditions. Data are shown as mean ± SD, n = 3. Statistical differences were determined by two-way ANOVA with Šídák’s post hoc multiple comparisons test: ns p > 0.05, * p < 0.05, ** p < 0.01, *** p < 0.001. Abbreviations are: ns, not significantly different; kDa, kilodaltons.

    Journal: medRxiv

    Article Title: International Multi-site Implementation of Local Cell-Free Protein Biomanufacturing to Advance Health and Research Equity

    doi: 10.1101/2025.07.25.25332228

    Figure Lengend Snippet: (a) Schematic representation of the pipeline for growth factor candidate selection and cell-based testing. (b) Western blot analysis of 11 high-value CFPS-derived growth factors. FGF-1, FGF-2, FGF-10, TNF-α, IL-1β, IFN-γ, and IL-15 were expressed in E. coli BL21 (DE3) in-house cell-free lysates. IL-6, EGF, IGF-1, and IL-3 were expressed in SHuffle-based in-house cell-free lysates. Detection was performed using an anti-His- HRP antibody. Data shown are from one representative biological replicate out of three independent experiments. (c) In vitro proliferation assay comparing on-demand, locally produced in Canada (blue) and commercial (green) FGF-1 growth factors in NIH-3T3 cells. Cells were individually treated with varying concentrations (1, 5, 10, 50, 500, and 1000 ng/mL) of growth factor. Luminescence was measured using a conventional plate reader. Data are shown as mean ± SD, n = 3. (d) In vitro proliferation assay comparing on-demand, locally produced (blue) and commercial (green) IL-3 growth factors in TF-1 cells. Cells were individually treated with varying concentrations (0.025, 0.05, 0.1, 0.5, 1, and 5 ng/mL). This representative data was obtained using reagents produced on-site in Canada. Data are shown as mean ± SD, n = 3. (e) Growth factor expression and cell-based validation in a low-resource setting. In vitro proliferation assay using FGF-1 and NIH-3T3 cells. Cells were individually treated with varying concentrations (1, 5, 10, 50, 500, and 1000 ng/mL) of both in-house-produced (blue) and commercial (green) growth factors. This representative data was obtained using reagents produced on-site in Brazil. Relative fold proliferation was plotted as the fold-change compared to untreated, serum-starved cells under the same experimental conditions. Data are shown as mean ± SD, n = 3. Statistical differences were determined by two-way ANOVA with Šídák’s post hoc multiple comparisons test: ns p > 0.05, * p < 0.05, ** p < 0.01, *** p < 0.001. Abbreviations are: ns, not significantly different; kDa, kilodaltons.

    Article Snippet: E. coli BL21(DE3) (NEB, C2527I), ClearColi BL21(DE3) (Biosearch Technologies, 60810-1), E. coli SHuffle (NEB, C3028J), E. coli BL21 (DE3)-Gold-ΔLac (Addgene, 99247), and E. coli BL21(DE3) Star/CRISPRi+( ) strains were used for preparing cell-free lysates .

    Techniques: Selection, Western Blot, Derivative Assay, In Vitro, Proliferation Assay, Produced, Expressing, Biomarker Discovery

    (a) Schematic of the SARS-CoV-2 genome; the coding sequence for the SARS-CoV-2 nucleocapsid protein was optimized for translation in CFPS and ultimately used for Nuvax formulation. (b) Western blot analysis of CFPS-produced SARS-CoV-2 nucleocapsid protein exhibiting a distinct band at the expected molecular weight (49 kDa). The SARS-CoV-2 nucleocapsid protein from SinoBiologicals, a commercially available recombinant protein, was used as a positive control (Ctrl +). N (CFPS) refers to the antigen expressed using in-house CFPS reactions. The molecular weight ladder (in kilodaltons) is shown on the left. Data shown are from one representative biological replicate out of three independent experiments. (c) Endotoxin levels in CFPS-produced SARS-CoV-2 nucleocapsid protein. Three different strategies were used for antigen expression: 1) cell-free lysates made from E. coli BL21(DE3); 2) cell-free lysates from E. coli BL21(DE3) followed by endotoxin removal; 3) cell-free lysates prepared from ClearColi TM BL21(DE3), an engineered E. coli strain used to express endotoxin-free recombinant proteins, making it ideal for expression of therapeutic products. The dashed line indicates the standard guidelines for subunit-based vaccine formulations (<20 EU/mL). Data are shown as mean ± SD, n = 3. (d) Immunization schedule, indicating prime, boost and bleed timepoints, for the CFPS-derived Nuvax. Intramuscular (IM) vaccination was administered on days 0 (prime) and 15 (boost), and blood was drawn on days 7, 14, 21, and 28 to evaluate for induction of IgG production. (e) Robust neutralizing antibody response following Nuvax administration alongside group controls. Analysis was performed using ELISA and measured at OD 450 nm using a conventional plate reader. The data are presented as the mean ± SD for each group, with individual data points shown (control group that received only PBS, n = 5; control group that received only adjuvants, n = 5; Nuvax group, n = 5). Statistical differences were determined by two-way ANOVA with Tukey’s post hoc multiple comparisons test: ns p > 0.05, * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. Abbreviations are: ns, not significantly different; Ctrl, control; N, nucleocapsid; End, endotoxin; Ab, antibody; IM, intramuscular; CFPS, cell-free protein synthesis.

    Journal: medRxiv

    Article Title: International Multi-site Implementation of Local Cell-Free Protein Biomanufacturing to Advance Health and Research Equity

    doi: 10.1101/2025.07.25.25332228

    Figure Lengend Snippet: (a) Schematic of the SARS-CoV-2 genome; the coding sequence for the SARS-CoV-2 nucleocapsid protein was optimized for translation in CFPS and ultimately used for Nuvax formulation. (b) Western blot analysis of CFPS-produced SARS-CoV-2 nucleocapsid protein exhibiting a distinct band at the expected molecular weight (49 kDa). The SARS-CoV-2 nucleocapsid protein from SinoBiologicals, a commercially available recombinant protein, was used as a positive control (Ctrl +). N (CFPS) refers to the antigen expressed using in-house CFPS reactions. The molecular weight ladder (in kilodaltons) is shown on the left. Data shown are from one representative biological replicate out of three independent experiments. (c) Endotoxin levels in CFPS-produced SARS-CoV-2 nucleocapsid protein. Three different strategies were used for antigen expression: 1) cell-free lysates made from E. coli BL21(DE3); 2) cell-free lysates from E. coli BL21(DE3) followed by endotoxin removal; 3) cell-free lysates prepared from ClearColi TM BL21(DE3), an engineered E. coli strain used to express endotoxin-free recombinant proteins, making it ideal for expression of therapeutic products. The dashed line indicates the standard guidelines for subunit-based vaccine formulations (<20 EU/mL). Data are shown as mean ± SD, n = 3. (d) Immunization schedule, indicating prime, boost and bleed timepoints, for the CFPS-derived Nuvax. Intramuscular (IM) vaccination was administered on days 0 (prime) and 15 (boost), and blood was drawn on days 7, 14, 21, and 28 to evaluate for induction of IgG production. (e) Robust neutralizing antibody response following Nuvax administration alongside group controls. Analysis was performed using ELISA and measured at OD 450 nm using a conventional plate reader. The data are presented as the mean ± SD for each group, with individual data points shown (control group that received only PBS, n = 5; control group that received only adjuvants, n = 5; Nuvax group, n = 5). Statistical differences were determined by two-way ANOVA with Tukey’s post hoc multiple comparisons test: ns p > 0.05, * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. Abbreviations are: ns, not significantly different; Ctrl, control; N, nucleocapsid; End, endotoxin; Ab, antibody; IM, intramuscular; CFPS, cell-free protein synthesis.

    Article Snippet: E. coli BL21(DE3) (NEB, C2527I), ClearColi BL21(DE3) (Biosearch Technologies, 60810-1), E. coli SHuffle (NEB, C3028J), E. coli BL21 (DE3)-Gold-ΔLac (Addgene, 99247), and E. coli BL21(DE3) Star/CRISPRi+( ) strains were used for preparing cell-free lysates .

    Techniques: Sequencing, Formulation, Western Blot, Produced, Molecular Weight, Recombinant, Positive Control, Expressing, Derivative Assay, Enzyme-linked Immunosorbent Assay, Control