e. coli bl21 Search Results


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  • 99
    New England Biolabs e coli bl21
    E Coli Bl21, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1115 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore e coli bl21
    Schematic representation and purification process for RtxA and proRtxA. a Scheme of the K. kingae RtxA molecule, with several different areas predicted from homology with other RTX toxins. The arrowheads with a letter C indicate the predicted CRAC and CARC motifs. The RtxA (b) and proRtxA ( c ) proteins were produced in E. coli <t>BL21/pMM100</t> cells and purified by a combination of affinity and hydrophobic chromatographies. Lanes: 1, crude extract from uninduced cells; 2, crude extract from cells induced with isopropyl β-D-1-thiogalactopyranoside (IPTG) to produce RtxA/proRtxA; 3, clarified crude urea extract from induced cells; 4, Ni-NTA agarose column flowthrough; 5, Ni-NTA agarose column wash; 6, fraction of eluted 105-kDa RtxA/proRtxA; 7, phenyl-sepharose column flowthrough; 8, phenyl-sepharose column wash; 9, fraction of eluted RtxA/proRtxA; and St, molecular-mass standards. The samples were analyzed on 7.5% polyacrylamide gels and stained with Coomassie blue
    E Coli Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 11780 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare escherichia coli bl21
    Schematic representation and purification process for RtxA and proRtxA. a Scheme of the K. kingae RtxA molecule, with several different areas predicted from homology with other RTX toxins. The arrowheads with a letter C indicate the predicted CRAC and CARC motifs. The RtxA (b) and proRtxA ( c ) proteins were produced in E. coli <t>BL21/pMM100</t> cells and purified by a combination of affinity and hydrophobic chromatographies. Lanes: 1, crude extract from uninduced cells; 2, crude extract from cells induced with isopropyl β-D-1-thiogalactopyranoside (IPTG) to produce RtxA/proRtxA; 3, clarified crude urea extract from induced cells; 4, Ni-NTA agarose column flowthrough; 5, Ni-NTA agarose column wash; 6, fraction of eluted 105-kDa RtxA/proRtxA; 7, phenyl-sepharose column flowthrough; 8, phenyl-sepharose column wash; 9, fraction of eluted RtxA/proRtxA; and St, molecular-mass standards. The samples were analyzed on 7.5% polyacrylamide gels and stained with Coomassie blue
    Escherichia Coli Bl21, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 1593 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher e coli bl21
    Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli <t>BL21.</t> Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p
    E Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 4918 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Stratagene e coli bl21
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21, supplied by Stratagene, used in various techniques. Bioz Stars score: 93/100, based on 3182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher e coli bl21 de3
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21 De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 1338 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene e coli bl21 de3
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21 De3, supplied by Stratagene, used in various techniques. Bioz Stars score: 92/100, based on 863 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher e coli bl21 de3 cells
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21 De3 Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1179 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bl21 de3 chemically competent cells
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    Bl21 De3 Chemically Competent Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Agilent technologies e coli bl21
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 620 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene e coli bl21 codonplus de3 ril cells
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21 Codonplus De3 Ril Cells, supplied by Stratagene, used in various techniques. Bioz Stars score: 90/100, based on 608 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli bl21 codonplus de3 ril cells/product/Stratagene
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    Image Search Results


    Schematic representation and purification process for RtxA and proRtxA. a Scheme of the K. kingae RtxA molecule, with several different areas predicted from homology with other RTX toxins. The arrowheads with a letter C indicate the predicted CRAC and CARC motifs. The RtxA (b) and proRtxA ( c ) proteins were produced in E. coli BL21/pMM100 cells and purified by a combination of affinity and hydrophobic chromatographies. Lanes: 1, crude extract from uninduced cells; 2, crude extract from cells induced with isopropyl β-D-1-thiogalactopyranoside (IPTG) to produce RtxA/proRtxA; 3, clarified crude urea extract from induced cells; 4, Ni-NTA agarose column flowthrough; 5, Ni-NTA agarose column wash; 6, fraction of eluted 105-kDa RtxA/proRtxA; 7, phenyl-sepharose column flowthrough; 8, phenyl-sepharose column wash; 9, fraction of eluted RtxA/proRtxA; and St, molecular-mass standards. The samples were analyzed on 7.5% polyacrylamide gels and stained with Coomassie blue

    Journal: Emerging Microbes & Infections

    Article Title: Cytotoxic activity of Kingella kingae RtxA toxin depends on post-translational acylation of lysine residues and cholesterol binding

    doi: 10.1038/s41426-018-0179-x

    Figure Lengend Snippet: Schematic representation and purification process for RtxA and proRtxA. a Scheme of the K. kingae RtxA molecule, with several different areas predicted from homology with other RTX toxins. The arrowheads with a letter C indicate the predicted CRAC and CARC motifs. The RtxA (b) and proRtxA ( c ) proteins were produced in E. coli BL21/pMM100 cells and purified by a combination of affinity and hydrophobic chromatographies. Lanes: 1, crude extract from uninduced cells; 2, crude extract from cells induced with isopropyl β-D-1-thiogalactopyranoside (IPTG) to produce RtxA/proRtxA; 3, clarified crude urea extract from induced cells; 4, Ni-NTA agarose column flowthrough; 5, Ni-NTA agarose column wash; 6, fraction of eluted 105-kDa RtxA/proRtxA; 7, phenyl-sepharose column flowthrough; 8, phenyl-sepharose column wash; 9, fraction of eluted RtxA/proRtxA; and St, molecular-mass standards. The samples were analyzed on 7.5% polyacrylamide gels and stained with Coomassie blue

    Article Snippet: The E. coli strain BL21 (Novagen, Madison, WI) carrying the plasmid pMM100 (encoding LacI and tetracycline resistance) was used to express the RtxA proteins.

    Techniques: Purification, Produced, Staining

    Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli BL21. Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Journal: Vaccines

    Article Title: Gut Microbiota Abrogates Anti-α-Gal IgA Response in Lungs and Protects against Experimental Aspergillus Infection in Poultry

    doi: 10.3390/vaccines8020285

    Figure Lengend Snippet: Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli BL21. Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Article Snippet: Bacteria Culture and Oral Administration of Bacteria The bacterium E. coli O86:B7 (ATCC 12701) expresses high levels of α-Gal on its surface [ , ], which is not the case for E. coli BL21 (DE3, Invitrogen, Carlsbad, CA, USA) [ ].

    Techniques: Infection, Enzyme-linked Immunosorbent Assay, Standard Deviation

    Oral administration of E. coli O86:B7 protects turkeys against aspergillosis. Clinical examination revealed that A. fumigatus infection produces open-mouthed breathing (OMB) in turkeys treated with PBS or E. coli BL21. Turkeys treated with E. coli O86:B7 were protected from developing OMB ( A ). Pulmonary lesions (i.e., granulomas, delimited area and white arrow heads) were scored (see methods). Examples of lungs with scores 0 to 3 are shown ( B ). Granuloma score was lower in turkeys treated with E. coli O86:B7 ( C ). Lung samples were processed for histopathology and stained with hematoxylin-eosin-saffron (HES, D ) and periodic acid-schiff (PAS, E ). Histological lesions were scored (see methods). Examples of histopathology samples with scores 0 to 3 are shown. Visible peribronchial regions (asterisk) and granulomas (delimited area and black arrow heads) are shown (HES score, D ). The presence of fungal germ-tube/hyphae (black arrows) and mycelium (white arrows) was scored (see methods). Granulomas associated with fungal hyphae (delimited area and black arrow heads) are shown (PAS score, E ). HES and PAS scores were lower in turkeys treated with E. coli O86:B7 ( F , G ). The presence of viable Aspergillus in lungs was quantified by colony-forming unit (CFU) counting assay ( H ). Fungal DNA levels were measured by A. fumigatus -specific 28S qPCR normalizing against turkey actb and gapdh as host genes using the 2 −ΔΔ C t ratio method. Results are relative to 28S levels in the control group (i.e., PBS) ( I ). No significant change was observed in the amount of CFU and 28S fold change ( H , I ). Size of bars is indicated. 100X magnification. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (*** p

    Journal: Vaccines

    Article Title: Gut Microbiota Abrogates Anti-α-Gal IgA Response in Lungs and Protects against Experimental Aspergillus Infection in Poultry

    doi: 10.3390/vaccines8020285

    Figure Lengend Snippet: Oral administration of E. coli O86:B7 protects turkeys against aspergillosis. Clinical examination revealed that A. fumigatus infection produces open-mouthed breathing (OMB) in turkeys treated with PBS or E. coli BL21. Turkeys treated with E. coli O86:B7 were protected from developing OMB ( A ). Pulmonary lesions (i.e., granulomas, delimited area and white arrow heads) were scored (see methods). Examples of lungs with scores 0 to 3 are shown ( B ). Granuloma score was lower in turkeys treated with E. coli O86:B7 ( C ). Lung samples were processed for histopathology and stained with hematoxylin-eosin-saffron (HES, D ) and periodic acid-schiff (PAS, E ). Histological lesions were scored (see methods). Examples of histopathology samples with scores 0 to 3 are shown. Visible peribronchial regions (asterisk) and granulomas (delimited area and black arrow heads) are shown (HES score, D ). The presence of fungal germ-tube/hyphae (black arrows) and mycelium (white arrows) was scored (see methods). Granulomas associated with fungal hyphae (delimited area and black arrow heads) are shown (PAS score, E ). HES and PAS scores were lower in turkeys treated with E. coli O86:B7 ( F , G ). The presence of viable Aspergillus in lungs was quantified by colony-forming unit (CFU) counting assay ( H ). Fungal DNA levels were measured by A. fumigatus -specific 28S qPCR normalizing against turkey actb and gapdh as host genes using the 2 −ΔΔ C t ratio method. Results are relative to 28S levels in the control group (i.e., PBS) ( I ). No significant change was observed in the amount of CFU and 28S fold change ( H , I ). Size of bars is indicated. 100X magnification. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (*** p

    Article Snippet: Bacteria Culture and Oral Administration of Bacteria The bacterium E. coli O86:B7 (ATCC 12701) expresses high levels of α-Gal on its surface [ , ], which is not the case for E. coli BL21 (DE3, Invitrogen, Carlsbad, CA, USA) [ ].

    Techniques: Infection, Histopathology, Staining, Real-time Polymerase Chain Reaction, Standard Deviation

    Expression of turkey and chicken cytokine genes in response to oral administration of E. coli O86:B7 and E. coli BL21 and α-Gal-BSA immunization. The figure displays the mRNA expression levels of INFγ , IL6 , IL2 , IL10 and MyD88 in ceca ( A ) and lungs ( B ) of turkeys and IL6 and IL2 in lungs of chicken ( C ). Total RNA was extracted and gene expression levels were measured by qPCR normalizing against turkey actb and gapdh as housekeeping genes, using the using the 2 −ΔΔ C t ratio method. Expression levels are relative to the control group (i.e., PBS). Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Journal: Vaccines

    Article Title: Gut Microbiota Abrogates Anti-α-Gal IgA Response in Lungs and Protects against Experimental Aspergillus Infection in Poultry

    doi: 10.3390/vaccines8020285

    Figure Lengend Snippet: Expression of turkey and chicken cytokine genes in response to oral administration of E. coli O86:B7 and E. coli BL21 and α-Gal-BSA immunization. The figure displays the mRNA expression levels of INFγ , IL6 , IL2 , IL10 and MyD88 in ceca ( A ) and lungs ( B ) of turkeys and IL6 and IL2 in lungs of chicken ( C ). Total RNA was extracted and gene expression levels were measured by qPCR normalizing against turkey actb and gapdh as housekeeping genes, using the using the 2 −ΔΔ C t ratio method. Expression levels are relative to the control group (i.e., PBS). Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Article Snippet: Bacteria Culture and Oral Administration of Bacteria The bacterium E. coli O86:B7 (ATCC 12701) expresses high levels of α-Gal on its surface [ , ], which is not the case for E. coli BL21 (DE3, Invitrogen, Carlsbad, CA, USA) [ ].

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Standard Deviation

    PCR analysis of three disruption mutants. P1 to P8 refer to priming sites. PCR amplification for identifying the deletion of each target gene was performed using each E. coli BL21 mutant genomic DNA as a template. (A) Salvage pathway gene disruptions. M, size marker; lane 1, deoC and deoB region including deoA (2.0 kb); lane 2, Δ deoC :: cat ::Δ deoB (1.3 kb); lane 3, Δ( deoC-deoB ) (0.4 kb), represented to Δ deoA ; lane 4, tdk (0.6 kb); lane 5, Δ tdk :: cat (1.1 kb); lane 6, Δ tdk (0.2 kb); lane 7, udp (0.7 kb); lane 8, Δ udp :: cat (1.1 kb); lane 9, Δ udp (0.2 kb). The FRT (black bar)-flanked chloramphenicol-resistant gene was amplified by PCR. The linear disruption PCR fragment (gray bar) was transformed into a strain expressing the λ Red recombinase, and then chloramphenicol-resistant transformants were selected. The selective marker was eliminated by FLP recombinase system. (B) ung disruption. Lane 1, ung (0.7 kb); lane 2, Δ ung :: cat (1.1 kb); lane 3, Δ ung (0.2 kb).

    Journal: Applied and Environmental Microbiology

    Article Title: Fermentative Production of Thymidine by a Metabolically Engineered Escherichia coli Strain ▿

    doi: 10.1128/AEM.02328-08

    Figure Lengend Snippet: PCR analysis of three disruption mutants. P1 to P8 refer to priming sites. PCR amplification for identifying the deletion of each target gene was performed using each E. coli BL21 mutant genomic DNA as a template. (A) Salvage pathway gene disruptions. M, size marker; lane 1, deoC and deoB region including deoA (2.0 kb); lane 2, Δ deoC :: cat ::Δ deoB (1.3 kb); lane 3, Δ( deoC-deoB ) (0.4 kb), represented to Δ deoA ; lane 4, tdk (0.6 kb); lane 5, Δ tdk :: cat (1.1 kb); lane 6, Δ tdk (0.2 kb); lane 7, udp (0.7 kb); lane 8, Δ udp :: cat (1.1 kb); lane 9, Δ udp (0.2 kb). The FRT (black bar)-flanked chloramphenicol-resistant gene was amplified by PCR. The linear disruption PCR fragment (gray bar) was transformed into a strain expressing the λ Red recombinase, and then chloramphenicol-resistant transformants were selected. The selective marker was eliminated by FLP recombinase system. (B) ung disruption. Lane 1, ung (0.7 kb); lane 2, Δ ung :: cat (1.1 kb); lane 3, Δ ung (0.2 kb).

    Article Snippet: E. coli BL21 Star (Invitrogen, Groningen, The Netherlands) was used as the host for gene disruption and expression of foreign genes.

    Techniques: Polymerase Chain Reaction, Amplification, Mutagenesis, Marker, Transformation Assay, Expressing

    Thymidine degradation assay. Negative control with thymidine (•), BL21 Star (○), BLd (▾), BLdt (▿), and BLdtu (▪). Values are means ± standard deviations of the results from triplicate experiments.

    Journal: Applied and Environmental Microbiology

    Article Title: Fermentative Production of Thymidine by a Metabolically Engineered Escherichia coli Strain ▿

    doi: 10.1128/AEM.02328-08

    Figure Lengend Snippet: Thymidine degradation assay. Negative control with thymidine (•), BL21 Star (○), BLd (▾), BLdt (▿), and BLdtu (▪). Values are means ± standard deviations of the results from triplicate experiments.

    Article Snippet: E. coli BL21 Star (Invitrogen, Groningen, The Netherlands) was used as the host for gene disruption and expression of foreign genes.

    Techniques: Degradation Assay, Negative Control

    SDS-PAGE analysis of purified protein recombinant SllB in E. coli BL21 cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: SDS-PAGE analysis of purified protein recombinant SllB in E. coli BL21 cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: SDS Page, Purification, Recombinant, Marker

    A transmission electron microscopic observation on the E. coli BL21 with recombinant protein. (A) Normal E. coli BL21 was treated as control. (B) The E. coli BL21 cells recombinant S-layer protein. (C) Crystal lattice structures on surface of the E. coli BL21 cells recombinant S-layer protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: A transmission electron microscopic observation on the E. coli BL21 with recombinant protein. (A) Normal E. coli BL21 was treated as control. (B) The E. coli BL21 cells recombinant S-layer protein. (C) Crystal lattice structures on surface of the E. coli BL21 cells recombinant S-layer protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: Transmission Assay, Recombinant

    Expression of sllB in E. coli BL21 cells. (A) SDS-PAGE analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; lane M represent Takara Protein Marker (Broad). (B) Western blot analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; M, Takara Protein Marker (Broad). Lane M1, Precision plus protein standards; lane M2, perfect protein marker. Note the band pointed with arrows is the recombinant S-layer protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: Expression of sllB in E. coli BL21 cells. (A) SDS-PAGE analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; lane M represent Takara Protein Marker (Broad). (B) Western blot analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; M, Takara Protein Marker (Broad). Lane M1, Precision plus protein standards; lane M2, perfect protein marker. Note the band pointed with arrows is the recombinant S-layer protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: Expressing, SDS Page, Marker, Western Blot, Recombinant