e. coli dh5α Search Results


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  • 99
    ATCC e coli dh5α
    ( a ) The PCA results of E. coli <t>DH5α</t> incubated under different GO concentrations. 1 represents the control group and 2–6 principal components are from the samples incubated with different GO concentrations at 5, 20, 40, 80 and 120 μg/mL for 2 h. ( d ) The PCA results of time experiment. 1 represents the control group. 2–6 represent principal components obtained from the data incubated with GO (80 μg/mL) at different time: 0, 1, 2, 3 and 4 h. ( b , e ) show the relationship between GO concentration or incubation time and the parameter D as well as the cell viability rate of E. coli DH5α. ( c , f ) present the bivariate analysis results, and a significant negative correlation between the parameter D and cell viability rate were obtained in concentration experiment (Person’s correlation coefficient: −0.99, p
    E Coli Dh5α, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore escherichia coli dh5α cells
    ( a ) The PCA results of E. coli <t>DH5α</t> incubated under different GO concentrations. 1 represents the control group and 2–6 principal components are from the samples incubated with different GO concentrations at 5, 20, 40, 80 and 120 μg/mL for 2 h. ( d ) The PCA results of time experiment. 1 represents the control group. 2–6 represent principal components obtained from the data incubated with GO (80 μg/mL) at different time: 0, 1, 2, 3 and 4 h. ( b , e ) show the relationship between GO concentration or incubation time and the parameter D as well as the cell viability rate of E. coli DH5α. ( c , f ) present the bivariate analysis results, and a significant negative correlation between the parameter D and cell viability rate were obtained in concentration experiment (Person’s correlation coefficient: −0.99, p
    Escherichia Coli Dh5α Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega escherichia coli dh5α
    ( a ) The PCA results of E. coli <t>DH5α</t> incubated under different GO concentrations. 1 represents the control group and 2–6 principal components are from the samples incubated with different GO concentrations at 5, 20, 40, 80 and 120 μg/mL for 2 h. ( d ) The PCA results of time experiment. 1 represents the control group. 2–6 represent principal components obtained from the data incubated with GO (80 μg/mL) at different time: 0, 1, 2, 3 and 4 h. ( b , e ) show the relationship between GO concentration or incubation time and the parameter D as well as the cell viability rate of E. coli DH5α. ( c , f ) present the bivariate analysis results, and a significant negative correlation between the parameter D and cell viability rate were obtained in concentration experiment (Person’s correlation coefficient: −0.99, p
    Escherichia Coli Dh5α, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 433 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher e coli dh5α
    Confirmation of the intracellular location of ChiA74∆s p in Escherichia coli and Bacillus thuringiensis 4Q7 using a chimeric construct with the green fluorescent protein (GFP) gene. (A) Schematic illustration that shows the fusion of chiA74 ∆s p with gfp . Panel 1, two constructs were developed, under regulation of the chiA74 wildtype promoter (wp) or under control of the cytA - p/ STAB-SD system. Lollipop indicates transcriptional terminator. Oligonucleotides used to make chimeric construct with gfp are shown in Table 1 . Panel 2, confirmation of chimeric constructs by PCR, primers used for amplification are showed in parenthesis and in Table 1 . L, 1 kb (kilobase) DNA Ladder (New England Biolabs); Lane 1, pEHchiA74∆ sp - gfp (primers: chiA74-1, chiA74-3); lane 2, pEHchiA74∆ sp - gfp (primers: chiA74-1, gfp-3); lane 3, pEHchiA74∆ sp - gfp (primers: gfp-1, chiA74-4); lane 4, pEB chi A74∆sp- gfp (primers: cytSTAB-1, chiA74-4); Lane 5, pEB chi A74∆sp- gfp (primers: cytSTAB-1, gfp-3); lane 6, pEB chi A74∆sp- gfp (primers: gfp-1, chiA74-4). (B) Phase contrast (left) and fluorescence micrographs (right) of recombinant strains of E. coli and B. thuringiensis strain 4Q7 expressing the chimeric protein ChiA74∆sp-GFP. Panel 1, E. coli- pEHchiA74∆ sp - gfp ; panel 2, 4Q7 - pEHchiA74∆ sp - gfp ; panel 3, E. coli- pEBchiA74∆ sp - gfp ; panel 4, 4Q7 - pEBchiA74∆ sp - gfp ; panel 5, E. coli <t>DH5α;</t> panel 6, 4Q7. Samples of recombinant strains of B. thuringiensis were collected at ~ 72 h.
    E Coli Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3027 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene e coli dh5α
    Strategy for gene replacement in Streptomyces . ( A )IV (Apra R ), oriT of RK2, and two FRT sites was amplified by PCR by using primers containing 39-nt 5′ homology extensions corresponding to regions flanking the S. coelicolor target gene (dotted lines a and b) and 20-nt 3′ homology to the unique priming sites P1 and P2 of the disruption cassette. ( B ) The PCR product from A was used to transform E. coli BW25113/pIJ790 (expressing the λ-Red recombination functions), containing the Supercos-1 cosmid with the cloned target gene ( cyc2 ). ( C ) Apra R transformants were selected, and the recombinant cosmid was identified by PCR and restriction analysis. ( D ) The potent methyl-specific restriction system of S. coelicolor was circumvented by introducing the recombinant cosmid into the methylation-deficient E. coli host ET12567/pUZ8002. The cosmid was mobilized in trans by pUZ8002 to Streptomyces by conjugation. ( E ) Selected exconjugants (Apra R ) were screened for Kan S (loss of the Kan resistance gene neo ), and the double cross-over allelic exchange was confirmed by PCR and Southern blot analysis. ( F ) E. coli <t>DH5α</t> cells containing pCP20 were transformed with the mutagenized cosmid DNA, and FLP synthesis was induced. ( G) The loss of the disruption resistance marker was tested, and the cosmid was introduced by polyethylene glycol (PEG)-mediated transformation into the S. coelicolor mutant carrying a marked deletion within the gene of interest. ( H ) Kan R transformants arising from single cross-over events were restreaked nonselectively and screened for the loss of both Kan R and Apra R , indicating a successful replacement by the in-frame deletion marked only by a “scar” sequence of 81 bp containing priming sites P1 and P2 (underlined), and one FRT site.
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    Merck & Co e coli dh5α
    Strategy for gene replacement in Streptomyces . ( A )IV (Apra R ), oriT of RK2, and two FRT sites was amplified by PCR by using primers containing 39-nt 5′ homology extensions corresponding to regions flanking the S. coelicolor target gene (dotted lines a and b) and 20-nt 3′ homology to the unique priming sites P1 and P2 of the disruption cassette. ( B ) The PCR product from A was used to transform E. coli BW25113/pIJ790 (expressing the λ-Red recombination functions), containing the Supercos-1 cosmid with the cloned target gene ( cyc2 ). ( C ) Apra R transformants were selected, and the recombinant cosmid was identified by PCR and restriction analysis. ( D ) The potent methyl-specific restriction system of S. coelicolor was circumvented by introducing the recombinant cosmid into the methylation-deficient E. coli host ET12567/pUZ8002. The cosmid was mobilized in trans by pUZ8002 to Streptomyces by conjugation. ( E ) Selected exconjugants (Apra R ) were screened for Kan S (loss of the Kan resistance gene neo ), and the double cross-over allelic exchange was confirmed by PCR and Southern blot analysis. ( F ) E. coli <t>DH5α</t> cells containing pCP20 were transformed with the mutagenized cosmid DNA, and FLP synthesis was induced. ( G) The loss of the disruption resistance marker was tested, and the cosmid was introduced by polyethylene glycol (PEG)-mediated transformation into the S. coelicolor mutant carrying a marked deletion within the gene of interest. ( H ) Kan R transformants arising from single cross-over events were restreaked nonselectively and screened for the loss of both Kan R and Apra R , indicating a successful replacement by the in-frame deletion marked only by a “scar” sequence of 81 bp containing priming sites P1 and P2 (underlined), and one FRT site.
    E Coli Dh5α, supplied by Merck & Co, used in various techniques. Bioz Stars score: 95/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa e coli dh5α
    Western blot analysis of urease extracts by using anti-UreB. Cytosolic protein extracts (10 μg) were electrophoresed through an SDS-polyacrylamide gel, transferred to a PVDF membrane, and probed with anti-UreB as described in the Materials and Methods section. (A) Extracts from <t>DH5α</t> (pHP8080/pBluescript) and DH5α (pHP8080/pUEFs). (B) Extracts from SE5000 (pHP8080/pBluescript) and SE5000 (pHP8080/pUDFs). Density values are shown below individual blots. Results are representative of three experiments performed by using extracts prepared on 3 separate days. pBS, pBluescript; 808, pHP808; 8080, pHP8080.
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    Toyobo e coli dh5α
    Western blot analysis of urease extracts by using anti-UreB. Cytosolic protein extracts (10 μg) were electrophoresed through an SDS-polyacrylamide gel, transferred to a PVDF membrane, and probed with anti-UreB as described in the Materials and Methods section. (A) Extracts from <t>DH5α</t> (pHP8080/pBluescript) and DH5α (pHP8080/pUEFs). (B) Extracts from SE5000 (pHP8080/pBluescript) and SE5000 (pHP8080/pUDFs). Density values are shown below individual blots. Results are representative of three experiments performed by using extracts prepared on 3 separate days. pBS, pBluescript; 808, pHP808; 8080, pHP8080.
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    Merck KGaA escherichia coli dh5α
    Western blot analysis of urease extracts by using anti-UreB. Cytosolic protein extracts (10 μg) were electrophoresed through an SDS-polyacrylamide gel, transferred to a PVDF membrane, and probed with anti-UreB as described in the Materials and Methods section. (A) Extracts from <t>DH5α</t> (pHP8080/pBluescript) and DH5α (pHP8080/pUEFs). (B) Extracts from SE5000 (pHP8080/pBluescript) and SE5000 (pHP8080/pUDFs). Density values are shown below individual blots. Results are representative of three experiments performed by using extracts prepared on 3 separate days. pBS, pBluescript; 808, pHP808; 8080, pHP8080.
    Escherichia Coli Dh5α, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore e coli dh5α
    A map of the promoter trap vector pShuttleF (A) and β-Gal activities of 10 selective positive clones in E. coli (B) and B. subtilis (C). (A) The rep represents the replication protein in B. subtilis . ColEI, bgaB and Cm represent the E. coli ColEI replicon, the coding sequence of β-Gal and chloramphenicol-resistance marker, respectively. The unique restriction sites are marked on the outside of the map. (B). Production of β-Gal from 10 selective positive clones in E. coli <t>DH5α</t> after 24 h culture. Different letters on columns indicate significant differences (p
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    MCLAB e coli dh5α
    A map of the promoter trap vector pShuttleF (A) and β-Gal activities of 10 selective positive clones in E. coli (B) and B. subtilis (C). (A) The rep represents the replication protein in B. subtilis . ColEI, bgaB and Cm represent the E. coli ColEI replicon, the coding sequence of β-Gal and chloramphenicol-resistance marker, respectively. The unique restriction sites are marked on the outside of the map. (B). Production of β-Gal from 10 selective positive clones in E. coli <t>DH5α</t> after 24 h culture. Different letters on columns indicate significant differences (p
    E Coli Dh5α, supplied by MCLAB, used in various techniques. Bioz Stars score: 95/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    tiangen biotech co e coli dh5α
    Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli <t>DH5α</t> (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.
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    TransGen biotech co e coli dh5α
    Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli <t>DH5α</t> (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.
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    Meridian Life Science escherichia coli dh5α
    Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli <t>DH5α</t> (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.
    Escherichia Coli Dh5α, supplied by Meridian Life Science, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    BioMed Diagnostics Inc e coli dh5α
    Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli <t>DH5α</t> (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.
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    Sangon Biotech escherichia coli dh5α
    Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli <t>DH5α</t> (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.
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    Difco e coli dh5α
    Efficiency of electroporation of pTOPO/FNL10 and pFNLTP1 into E. coli <t>DH5α</t> or Francisella spp. ( F. tularensis LVS or F. novicida U112). The transformation efficiency, expressed as log CFU per microgram of DNA (mean ± standard deviation), was determined from three individual preparations of competent cells. Competent cells of E. coli were prepared with 10% glycerol, while 0.5 M sucrose was used to prepare competent cells of F. tularensis LVS and F. novicida U112. Most electroporations were performed with 100 ng of plasmid DNA; the only exception was the electroporation of pTOPO/FNL10 into F. tularensis LVS, for which 500 ng was used. The strains indicated in parentheses are the hosts from which plasmid DNA was isolated.
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    SolGent e coli dh5α
    Efficiency of electroporation of pTOPO/FNL10 and pFNLTP1 into E. coli <t>DH5α</t> or Francisella spp. ( F. tularensis LVS or F. novicida U112). The transformation efficiency, expressed as log CFU per microgram of DNA (mean ± standard deviation), was determined from three individual preparations of competent cells. Competent cells of E. coli were prepared with 10% glycerol, while 0.5 M sucrose was used to prepare competent cells of F. tularensis LVS and F. novicida U112. Most electroporations were performed with 100 ng of plasmid DNA; the only exception was the electroporation of pTOPO/FNL10 into F. tularensis LVS, for which 500 ng was used. The strains indicated in parentheses are the hosts from which plasmid DNA was isolated.
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    Bio-Rad e coli dh5α
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
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    GE Healthcare e coli dh5α
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
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    Vazyme Biotech Co e coli dh5α
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
    E Coli Dh5α, supplied by Vazyme Biotech Co, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Beijing CWBio escherichia coli dh5α
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
    Escherichia Coli Dh5α, supplied by Beijing CWBio, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    iNtRON Biotechnology e coli dh5α
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
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    Real Biotech Corporation e coli dh5α
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
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    Thermo Fisher escherichia coli dh5α t1r
    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
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    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli <t>DH5α</t> restores AI-2 activity. The error bars indicate standard deviations.
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    Thermo Fisher competent e coli dh5α
    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain <t>DH5α</t> expressing cI-DivIVA, detected with anti-cI antibodies.
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    Thermo Fisher purification e coli dh5α
    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain <t>DH5α</t> expressing cI-DivIVA, detected with anti-cI antibodies.
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    Thermo Fisher bioluminescent e coli dh5α
    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain <t>DH5α</t> expressing cI-DivIVA, detected with anti-cI antibodies.
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    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain <t>DH5α</t> expressing cI-DivIVA, detected with anti-cI antibodies.
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    Thermo Fisher transformation competent e coli dh5α
    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain <t>DH5α</t> expressing cI-DivIVA, detected with anti-cI antibodies.
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    Thermo Fisher nonpathogenic e coli dh5α
    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain <t>DH5α</t> expressing cI-DivIVA, detected with anti-cI antibodies.
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    Image Search Results


    ( a ) The PCA results of E. coli DH5α incubated under different GO concentrations. 1 represents the control group and 2–6 principal components are from the samples incubated with different GO concentrations at 5, 20, 40, 80 and 120 μg/mL for 2 h. ( d ) The PCA results of time experiment. 1 represents the control group. 2–6 represent principal components obtained from the data incubated with GO (80 μg/mL) at different time: 0, 1, 2, 3 and 4 h. ( b , e ) show the relationship between GO concentration or incubation time and the parameter D as well as the cell viability rate of E. coli DH5α. ( c , f ) present the bivariate analysis results, and a significant negative correlation between the parameter D and cell viability rate were obtained in concentration experiment (Person’s correlation coefficient: −0.99, p

    Journal: Scientific Reports

    Article Title: Rapidly Probing Antibacterial Activity of Graphene Oxide by Mass Spectrometry-based Metabolite Fingerprinting

    doi: 10.1038/srep28045

    Figure Lengend Snippet: ( a ) The PCA results of E. coli DH5α incubated under different GO concentrations. 1 represents the control group and 2–6 principal components are from the samples incubated with different GO concentrations at 5, 20, 40, 80 and 120 μg/mL for 2 h. ( d ) The PCA results of time experiment. 1 represents the control group. 2–6 represent principal components obtained from the data incubated with GO (80 μg/mL) at different time: 0, 1, 2, 3 and 4 h. ( b , e ) show the relationship between GO concentration or incubation time and the parameter D as well as the cell viability rate of E. coli DH5α. ( c , f ) present the bivariate analysis results, and a significant negative correlation between the parameter D and cell viability rate were obtained in concentration experiment (Person’s correlation coefficient: −0.99, p

    Article Snippet: Principal component analysis of metabolite fingerprinting of E. coli DH5α and ATCC 25922 after incubation with GO at different conditions shows metabolic disturbance of these bacteria ( a,d and a,b).

    Techniques: Incubation, Concentration Assay

    ( a ) The three principal components in PCA scores plot represent the E coli. DH5α control group (◾), GO group (▴) and AgNPs (▾) group (5 μg/mL, 2 h). ( b ) The three principal components in PCA scores plot represent the E coli. DH5α control group (◾), GO group (▴) and hydroxylated fullerene group (⦁) (80 μg/mL 2 h). ( c ) The three principal components in PCA scores plot represent the control group (▾), and the GO groups (▴) and hexagonal boron nitride (♦) group (80 μg/mL, 2 h). ( d–f ) The three principal components in PCA scores plot of ATCC 25922 represent the control group (◾), the GO group (▴) and AgNPs (▾) group (5 μg/mL, 2 h), hydroxylated fullerene group (⦁) (80 μg/mL 2 h) and hexagonal boron nitride (♦) incubation (80 μg/mL, 2 h), respectively.

    Journal: Scientific Reports

    Article Title: Rapidly Probing Antibacterial Activity of Graphene Oxide by Mass Spectrometry-based Metabolite Fingerprinting

    doi: 10.1038/srep28045

    Figure Lengend Snippet: ( a ) The three principal components in PCA scores plot represent the E coli. DH5α control group (◾), GO group (▴) and AgNPs (▾) group (5 μg/mL, 2 h). ( b ) The three principal components in PCA scores plot represent the E coli. DH5α control group (◾), GO group (▴) and hydroxylated fullerene group (⦁) (80 μg/mL 2 h). ( c ) The three principal components in PCA scores plot represent the control group (▾), and the GO groups (▴) and hexagonal boron nitride (♦) group (80 μg/mL, 2 h). ( d–f ) The three principal components in PCA scores plot of ATCC 25922 represent the control group (◾), the GO group (▴) and AgNPs (▾) group (5 μg/mL, 2 h), hydroxylated fullerene group (⦁) (80 μg/mL 2 h) and hexagonal boron nitride (♦) incubation (80 μg/mL, 2 h), respectively.

    Article Snippet: Principal component analysis of metabolite fingerprinting of E. coli DH5α and ATCC 25922 after incubation with GO at different conditions shows metabolic disturbance of these bacteria ( a,d and a,b).

    Techniques: Incubation

    Confirmation of the intracellular location of ChiA74∆s p in Escherichia coli and Bacillus thuringiensis 4Q7 using a chimeric construct with the green fluorescent protein (GFP) gene. (A) Schematic illustration that shows the fusion of chiA74 ∆s p with gfp . Panel 1, two constructs were developed, under regulation of the chiA74 wildtype promoter (wp) or under control of the cytA - p/ STAB-SD system. Lollipop indicates transcriptional terminator. Oligonucleotides used to make chimeric construct with gfp are shown in Table 1 . Panel 2, confirmation of chimeric constructs by PCR, primers used for amplification are showed in parenthesis and in Table 1 . L, 1 kb (kilobase) DNA Ladder (New England Biolabs); Lane 1, pEHchiA74∆ sp - gfp (primers: chiA74-1, chiA74-3); lane 2, pEHchiA74∆ sp - gfp (primers: chiA74-1, gfp-3); lane 3, pEHchiA74∆ sp - gfp (primers: gfp-1, chiA74-4); lane 4, pEB chi A74∆sp- gfp (primers: cytSTAB-1, chiA74-4); Lane 5, pEB chi A74∆sp- gfp (primers: cytSTAB-1, gfp-3); lane 6, pEB chi A74∆sp- gfp (primers: gfp-1, chiA74-4). (B) Phase contrast (left) and fluorescence micrographs (right) of recombinant strains of E. coli and B. thuringiensis strain 4Q7 expressing the chimeric protein ChiA74∆sp-GFP. Panel 1, E. coli- pEHchiA74∆ sp - gfp ; panel 2, 4Q7 - pEHchiA74∆ sp - gfp ; panel 3, E. coli- pEBchiA74∆ sp - gfp ; panel 4, 4Q7 - pEBchiA74∆ sp - gfp ; panel 5, E. coli DH5α; panel 6, 4Q7. Samples of recombinant strains of B. thuringiensis were collected at ~ 72 h.

    Journal: Microbial Cell Factories

    Article Title: Bacillus thuringiensis subsp. kurstaki HD1 as a factory to synthesize alkali-labile ChiA74?sp chitinase inclusions, Cry crystals and spores for applied use

    doi: 10.1186/1475-2859-13-15

    Figure Lengend Snippet: Confirmation of the intracellular location of ChiA74∆s p in Escherichia coli and Bacillus thuringiensis 4Q7 using a chimeric construct with the green fluorescent protein (GFP) gene. (A) Schematic illustration that shows the fusion of chiA74 ∆s p with gfp . Panel 1, two constructs were developed, under regulation of the chiA74 wildtype promoter (wp) or under control of the cytA - p/ STAB-SD system. Lollipop indicates transcriptional terminator. Oligonucleotides used to make chimeric construct with gfp are shown in Table 1 . Panel 2, confirmation of chimeric constructs by PCR, primers used for amplification are showed in parenthesis and in Table 1 . L, 1 kb (kilobase) DNA Ladder (New England Biolabs); Lane 1, pEHchiA74∆ sp - gfp (primers: chiA74-1, chiA74-3); lane 2, pEHchiA74∆ sp - gfp (primers: chiA74-1, gfp-3); lane 3, pEHchiA74∆ sp - gfp (primers: gfp-1, chiA74-4); lane 4, pEB chi A74∆sp- gfp (primers: cytSTAB-1, chiA74-4); Lane 5, pEB chi A74∆sp- gfp (primers: cytSTAB-1, gfp-3); lane 6, pEB chi A74∆sp- gfp (primers: gfp-1, chiA74-4). (B) Phase contrast (left) and fluorescence micrographs (right) of recombinant strains of E. coli and B. thuringiensis strain 4Q7 expressing the chimeric protein ChiA74∆sp-GFP. Panel 1, E. coli- pEHchiA74∆ sp - gfp ; panel 2, 4Q7 - pEHchiA74∆ sp - gfp ; panel 3, E. coli- pEBchiA74∆ sp - gfp ; panel 4, 4Q7 - pEBchiA74∆ sp - gfp ; panel 5, E. coli DH5α; panel 6, 4Q7. Samples of recombinant strains of B. thuringiensis were collected at ~ 72 h.

    Article Snippet: All constructs (Figure A) were propagated in E. coli DH5α [supE44, DlacU169 (F80lacZDM15 ) hsdR17 recA1 end A1 gyrA96 thi-1 relA1 ] (Invitrogen, Carlsbad CA, USA) and then used for transforming the acrystalliferous strain of B. thuringiensis subsp. israelensis 4Q7, (hereafter 4Q7), and B. thuringiensis subsp. kurstaki HD1 (hereafter HD1) (Bacillus Genetic Stock Center, Columbus, OH).

    Techniques: Construct, Polymerase Chain Reaction, Amplification, Fluorescence, Recombinant, Expressing

    Expression of ChiA74Δsp in Escherichia coli DH5α and Bacillus thuringiensis 4Q7. (A) Schematic illustration of the strategy used to delete the secretion signal peptide-encoding sequence (shown as a rectangle inside the open reading frame) of chiA74 to generate chiA74∆ s p. Two constructs were developed, the first under regulation of wildtype promoter (wp) and the second under control of the strong cytA-p /STAB-SD promoter system. Lollipop indicates the putative transcriptional terminator site. Oligonucleotide sequences used to delete the signal peptide-coding sequence are shown in Table 1 . (B) Evaluation of endochitinase activity using solubilized intracellular proteins produced in E. coli. Panel 1: Zymogram using 4-MU-(GlcNAc) 3 for detection. Lane 1, E. coli- pEHchiA74∆s p ; lane 2, without sample; lane 3, E. coli- pEBchiA74∆s p; lane 4, E. coli DH5α . Black arrow indicates the position of ChiA74∆s p in recombinant E. coli strains . Panel 2: (a) E. coli- pEHchiA74∆s p , (b) E. coli- pEBchiA74∆s p. No endochitinase activity was observed with E. coli DH5α . (C) Phase contrast microscopy of recombinant strains of B. thuringiensis . Panel 1, 4Q7; panel 2, 4Q7 - pEHchiA74∆s p ; panel 3, 4Q7 - pEBchiA74∆s p . Black arrows indicate the positions of ChiA74∆s p inclusions. (D) Endochitinase activity determined using solubilized intracellular proteins of recombinant strains of B. thuringiensis. Panel 1: lane 1, 4Q7; lane 2, 4Q7 - pEHchiA74∆s p ; lane 3, 4Q7 - pEBchiA74∆s p. Black arrow indicates the position of ChiA74∆s p in recombinant 4Q7 strains . Panel 2: (a) 4Q7 - pEHchiA74∆s p , (b) 4Q7 - pEBchiA74∆s p . Activity of recombinant bacteria was normalized with the residual intracellular endochitinase activity of 4Q7.

    Journal: Microbial Cell Factories

    Article Title: Bacillus thuringiensis subsp. kurstaki HD1 as a factory to synthesize alkali-labile ChiA74?sp chitinase inclusions, Cry crystals and spores for applied use

    doi: 10.1186/1475-2859-13-15

    Figure Lengend Snippet: Expression of ChiA74Δsp in Escherichia coli DH5α and Bacillus thuringiensis 4Q7. (A) Schematic illustration of the strategy used to delete the secretion signal peptide-encoding sequence (shown as a rectangle inside the open reading frame) of chiA74 to generate chiA74∆ s p. Two constructs were developed, the first under regulation of wildtype promoter (wp) and the second under control of the strong cytA-p /STAB-SD promoter system. Lollipop indicates the putative transcriptional terminator site. Oligonucleotide sequences used to delete the signal peptide-coding sequence are shown in Table 1 . (B) Evaluation of endochitinase activity using solubilized intracellular proteins produced in E. coli. Panel 1: Zymogram using 4-MU-(GlcNAc) 3 for detection. Lane 1, E. coli- pEHchiA74∆s p ; lane 2, without sample; lane 3, E. coli- pEBchiA74∆s p; lane 4, E. coli DH5α . Black arrow indicates the position of ChiA74∆s p in recombinant E. coli strains . Panel 2: (a) E. coli- pEHchiA74∆s p , (b) E. coli- pEBchiA74∆s p. No endochitinase activity was observed with E. coli DH5α . (C) Phase contrast microscopy of recombinant strains of B. thuringiensis . Panel 1, 4Q7; panel 2, 4Q7 - pEHchiA74∆s p ; panel 3, 4Q7 - pEBchiA74∆s p . Black arrows indicate the positions of ChiA74∆s p inclusions. (D) Endochitinase activity determined using solubilized intracellular proteins of recombinant strains of B. thuringiensis. Panel 1: lane 1, 4Q7; lane 2, 4Q7 - pEHchiA74∆s p ; lane 3, 4Q7 - pEBchiA74∆s p. Black arrow indicates the position of ChiA74∆s p in recombinant 4Q7 strains . Panel 2: (a) 4Q7 - pEHchiA74∆s p , (b) 4Q7 - pEBchiA74∆s p . Activity of recombinant bacteria was normalized with the residual intracellular endochitinase activity of 4Q7.

    Article Snippet: All constructs (Figure A) were propagated in E. coli DH5α [supE44, DlacU169 (F80lacZDM15 ) hsdR17 recA1 end A1 gyrA96 thi-1 relA1 ] (Invitrogen, Carlsbad CA, USA) and then used for transforming the acrystalliferous strain of B. thuringiensis subsp. israelensis 4Q7, (hereafter 4Q7), and B. thuringiensis subsp. kurstaki HD1 (hereafter HD1) (Bacillus Genetic Stock Center, Columbus, OH).

    Techniques: Expressing, Sequencing, Construct, Activity Assay, Produced, Recombinant, Microscopy

    Evaluation of OmpT-mediated release and small-scale purification of displayed Affibody molecule. A . Flow-cytometric analysis for comparison of surface expression of recombinant proteins between p AraBAD -Z IgG -EC in OmpT-negative E. coli BL21 and p AraBAD -Z IgG -EC in OmpT-positive E. coli DH5α. B . SDS-PAGE showing IMAC-purified supernatants from p AraBAD -Z IgG -EC in OmpT-negative E. coli BL21 and p AraBAD -Z IgG -EC in OmpT-positive E. coli DH5α. Supernatants from non-induced samples, indicated with (−), were included as controls. C . Mass spectrum from ESI-MS analysis of IMAC-purified supernatants from p AraBAD -Z IgG -EC in OmpT-positive E. coli DH5α. Theoretical molecular weight of the OmpT-cleaved Z IgG -His 6 is 9712 Da. D . SPR-based biosensor analysis on the IMAC-purified Z IgG -His 6 . Response units (RU) on the y-axis and time on the x-axis. Representative sensorgrams from injection of Z IgG -His 6 at three different concentrations over human IgG immobilized on the chip surface. Injections were performed in duplicates.

    Journal: Microbial Cell Factories

    Article Title: An engineered autotransporter-based surface expression vector enables efficient display of Affibody molecules on OmpT-negative E. coli as well as protease-mediated secretion in OmpT-positive strains

    doi: 10.1186/s12934-014-0179-z

    Figure Lengend Snippet: Evaluation of OmpT-mediated release and small-scale purification of displayed Affibody molecule. A . Flow-cytometric analysis for comparison of surface expression of recombinant proteins between p AraBAD -Z IgG -EC in OmpT-negative E. coli BL21 and p AraBAD -Z IgG -EC in OmpT-positive E. coli DH5α. B . SDS-PAGE showing IMAC-purified supernatants from p AraBAD -Z IgG -EC in OmpT-negative E. coli BL21 and p AraBAD -Z IgG -EC in OmpT-positive E. coli DH5α. Supernatants from non-induced samples, indicated with (−), were included as controls. C . Mass spectrum from ESI-MS analysis of IMAC-purified supernatants from p AraBAD -Z IgG -EC in OmpT-positive E. coli DH5α. Theoretical molecular weight of the OmpT-cleaved Z IgG -His 6 is 9712 Da. D . SPR-based biosensor analysis on the IMAC-purified Z IgG -His 6 . Response units (RU) on the y-axis and time on the x-axis. Representative sensorgrams from injection of Z IgG -His 6 at three different concentrations over human IgG immobilized on the chip surface. Injections were performed in duplicates.

    Article Snippet: The plasmid and PCR fragment were ligated using a T4 DNA ligase (New England Biolabs), and transformed to E. coli DH5α cells (Invitrogen) by heat shock.

    Techniques: Purification, Flow Cytometry, Expressing, Recombinant, SDS Page, Mass Spectrometry, Molecular Weight, SPR Assay, Injection, Chromatin Immunoprecipitation

    Strategy for gene replacement in Streptomyces . ( A )IV (Apra R ), oriT of RK2, and two FRT sites was amplified by PCR by using primers containing 39-nt 5′ homology extensions corresponding to regions flanking the S. coelicolor target gene (dotted lines a and b) and 20-nt 3′ homology to the unique priming sites P1 and P2 of the disruption cassette. ( B ) The PCR product from A was used to transform E. coli BW25113/pIJ790 (expressing the λ-Red recombination functions), containing the Supercos-1 cosmid with the cloned target gene ( cyc2 ). ( C ) Apra R transformants were selected, and the recombinant cosmid was identified by PCR and restriction analysis. ( D ) The potent methyl-specific restriction system of S. coelicolor was circumvented by introducing the recombinant cosmid into the methylation-deficient E. coli host ET12567/pUZ8002. The cosmid was mobilized in trans by pUZ8002 to Streptomyces by conjugation. ( E ) Selected exconjugants (Apra R ) were screened for Kan S (loss of the Kan resistance gene neo ), and the double cross-over allelic exchange was confirmed by PCR and Southern blot analysis. ( F ) E. coli DH5α cells containing pCP20 were transformed with the mutagenized cosmid DNA, and FLP synthesis was induced. ( G) The loss of the disruption resistance marker was tested, and the cosmid was introduced by polyethylene glycol (PEG)-mediated transformation into the S. coelicolor mutant carrying a marked deletion within the gene of interest. ( H ) Kan R transformants arising from single cross-over events were restreaked nonselectively and screened for the loss of both Kan R and Apra R , indicating a successful replacement by the in-frame deletion marked only by a “scar” sequence of 81 bp containing priming sites P1 and P2 (underlined), and one FRT site.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin

    doi: 10.1073/pnas.0337542100

    Figure Lengend Snippet: Strategy for gene replacement in Streptomyces . ( A )IV (Apra R ), oriT of RK2, and two FRT sites was amplified by PCR by using primers containing 39-nt 5′ homology extensions corresponding to regions flanking the S. coelicolor target gene (dotted lines a and b) and 20-nt 3′ homology to the unique priming sites P1 and P2 of the disruption cassette. ( B ) The PCR product from A was used to transform E. coli BW25113/pIJ790 (expressing the λ-Red recombination functions), containing the Supercos-1 cosmid with the cloned target gene ( cyc2 ). ( C ) Apra R transformants were selected, and the recombinant cosmid was identified by PCR and restriction analysis. ( D ) The potent methyl-specific restriction system of S. coelicolor was circumvented by introducing the recombinant cosmid into the methylation-deficient E. coli host ET12567/pUZ8002. The cosmid was mobilized in trans by pUZ8002 to Streptomyces by conjugation. ( E ) Selected exconjugants (Apra R ) were screened for Kan S (loss of the Kan resistance gene neo ), and the double cross-over allelic exchange was confirmed by PCR and Southern blot analysis. ( F ) E. coli DH5α cells containing pCP20 were transformed with the mutagenized cosmid DNA, and FLP synthesis was induced. ( G) The loss of the disruption resistance marker was tested, and the cosmid was introduced by polyethylene glycol (PEG)-mediated transformation into the S. coelicolor mutant carrying a marked deletion within the gene of interest. ( H ) Kan R transformants arising from single cross-over events were restreaked nonselectively and screened for the loss of both Kan R and Apra R , indicating a successful replacement by the in-frame deletion marked only by a “scar” sequence of 81 bp containing priming sites P1 and P2 (underlined), and one FRT site.

    Article Snippet: E. coli DH5α (Stratagene) was used as a host for plasmid constructions.

    Techniques: Amplification, Polymerase Chain Reaction, Expressing, Clone Assay, Recombinant, Methylation, Conjugation Assay, Southern Blot, Transformation Assay, Cosmid DNA, Marker, Mutagenesis, Sequencing

    Western blot analysis of urease extracts by using anti-UreB. Cytosolic protein extracts (10 μg) were electrophoresed through an SDS-polyacrylamide gel, transferred to a PVDF membrane, and probed with anti-UreB as described in the Materials and Methods section. (A) Extracts from DH5α (pHP8080/pBluescript) and DH5α (pHP8080/pUEFs). (B) Extracts from SE5000 (pHP8080/pBluescript) and SE5000 (pHP8080/pUDFs). Density values are shown below individual blots. Results are representative of three experiments performed by using extracts prepared on 3 separate days. pBS, pBluescript; 808, pHP808; 8080, pHP8080.

    Journal: Journal of Bacteriology

    Article Title: Isolation of Helicobacter pylori Genes That Modulate Urease Activity

    doi:

    Figure Lengend Snippet: Western blot analysis of urease extracts by using anti-UreB. Cytosolic protein extracts (10 μg) were electrophoresed through an SDS-polyacrylamide gel, transferred to a PVDF membrane, and probed with anti-UreB as described in the Materials and Methods section. (A) Extracts from DH5α (pHP8080/pBluescript) and DH5α (pHP8080/pUEFs). (B) Extracts from SE5000 (pHP8080/pBluescript) and SE5000 (pHP8080/pUDFs). Density values are shown below individual blots. Results are representative of three experiments performed by using extracts prepared on 3 separate days. pBS, pBluescript; 808, pHP808; 8080, pHP8080.

    Article Snippet: E. coli DH5α [F− supE44 Δ lacU169 (φ80 lacZ ΔM15) hsdR17 recA1 endA1 gyrA96 thi-1 relA1 ] (Clontech, Palo Alto, Calif.), SE5000 [F− araD193 Δ( argF lac ) U169 rpsL150 relA1 flbB5301 deoC1 ptsF25 rbsR recA56 ] , XL1-Blue MRF′ ( thi-1 gyrA96 relA1 recA1 endA1 supE44 hsdR17 lac F′ [ proAB lacI q Z ΔM15 Tn 10 ]) (Stratagene, La Jolla, Calif.), and SURE ( thi-1 gyrA96 relA1 recJ recB endA1 sbcC lac Δ[ mcrCB-hsdMR-mrr ] 177 uvrC umu ::Tn 5 F′ [( proAB lacI q Z ΔM15 Tn 10 ]) (Clontech) were grown in Luria (L) broth and in Luria agar plus appropriate antibiotics (ampicillin [100 μg/ml], chloramphenicol [20 μg/ml], tetracycline [10 μg/ml], and/or kanamycin [50 μg/ml]) for maintenance of plasmids.

    Techniques: Western Blot

    A map of the promoter trap vector pShuttleF (A) and β-Gal activities of 10 selective positive clones in E. coli (B) and B. subtilis (C). (A) The rep represents the replication protein in B. subtilis . ColEI, bgaB and Cm represent the E. coli ColEI replicon, the coding sequence of β-Gal and chloramphenicol-resistance marker, respectively. The unique restriction sites are marked on the outside of the map. (B). Production of β-Gal from 10 selective positive clones in E. coli DH5α after 24 h culture. Different letters on columns indicate significant differences (p

    Journal: PLoS ONE

    Article Title: Generation of an Artificial Double Promoter for Protein Expression in Bacillus subtilis through a Promoter Trap System

    doi: 10.1371/journal.pone.0056321

    Figure Lengend Snippet: A map of the promoter trap vector pShuttleF (A) and β-Gal activities of 10 selective positive clones in E. coli (B) and B. subtilis (C). (A) The rep represents the replication protein in B. subtilis . ColEI, bgaB and Cm represent the E. coli ColEI replicon, the coding sequence of β-Gal and chloramphenicol-resistance marker, respectively. The unique restriction sites are marked on the outside of the map. (B). Production of β-Gal from 10 selective positive clones in E. coli DH5α after 24 h culture. Different letters on columns indicate significant differences (p

    Article Snippet: E. coli DH5α was purchased from Novagen (Darmstadt, Germany).

    Techniques: Plasmid Preparation, Clone Assay, Sequencing, Marker

    Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli DH5α (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.

    Journal: PLoS ONE

    Article Title: Phenotypic Pattern-Based Assay for Dynamically Monitoring Host Cellular Responses to Salmonella Infections

    doi: 10.1371/journal.pone.0026544

    Figure Lengend Snippet: Dynamic monitoring of intestinal epithelial cell responses to intestinal bacteria. HT-29 cells (10,000 cells per well) were seeded into E-plates. The next day, cells were infected with Y. enterocolitica (A), S. flexneri (B), L. monocytogenes (C), E. coli DH5α (E), and Lactobacillus (F). Arrows, bacterial addition. Representative curves are an average of four replicate wells.

    Article Snippet: E. coli DH5α was from Tiangen Biotech (Beijing, China).

    Techniques: Infection

    Efficiency of electroporation of pTOPO/FNL10 and pFNLTP1 into E. coli DH5α or Francisella spp. ( F. tularensis LVS or F. novicida U112). The transformation efficiency, expressed as log CFU per microgram of DNA (mean ± standard deviation), was determined from three individual preparations of competent cells. Competent cells of E. coli were prepared with 10% glycerol, while 0.5 M sucrose was used to prepare competent cells of F. tularensis LVS and F. novicida U112. Most electroporations were performed with 100 ng of plasmid DNA; the only exception was the electroporation of pTOPO/FNL10 into F. tularensis LVS, for which 500 ng was used. The strains indicated in parentheses are the hosts from which plasmid DNA was isolated.

    Journal: Applied and Environmental Microbiology

    Article Title: Construction and Characterization of a Highly Efficient Francisella Shuttle Plasmid

    doi: 10.1128/AEM.70.12.7511-7519.2004

    Figure Lengend Snippet: Efficiency of electroporation of pTOPO/FNL10 and pFNLTP1 into E. coli DH5α or Francisella spp. ( F. tularensis LVS or F. novicida U112). The transformation efficiency, expressed as log CFU per microgram of DNA (mean ± standard deviation), was determined from three individual preparations of competent cells. Competent cells of E. coli were prepared with 10% glycerol, while 0.5 M sucrose was used to prepare competent cells of F. tularensis LVS and F. novicida U112. Most electroporations were performed with 100 ng of plasmid DNA; the only exception was the electroporation of pTOPO/FNL10 into F. tularensis LVS, for which 500 ng was used. The strains indicated in parentheses are the hosts from which plasmid DNA was isolated.

    Article Snippet: E. coli DH5α and HB101 were grown at 37°C aerobically in Luria-Bertani (LB) medium (Difco) supplemented with kanamycin (50 μg ml−1 ), streptomycin (100 μg ml−1 ), or ampicillin (100 μg ml−1 ) when required.

    Techniques: Electroporation, Transformation Assay, Standard Deviation, Plasmid Preparation, Isolation

    H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli DH5α restores AI-2 activity. The error bars indicate standard deviations.

    Journal: Journal of Bacteriology

    Article Title: Evidence for a Signaling System in Helicobacter pylori: Detection of a luxS-Encoded Autoinducer

    doi:

    Figure Lengend Snippet: H. pylori produces a luxS -dependent AI-2 activity. Cell-free supernatants were tested for the ability to induce luminescence expression in V. harveyi BB170. Ten percent cell-free supernatants or sterile media were mixed with the reporter strain in microtiter plates and incubated at 30°C on a rotary shaker. Aliquots were taken, and both cell density and light production were determined. Activity is reported as fold activation of luminescence of BB170 over the level of luminescence when sterile media were added. Assays were repeated at least two times. (A) Wild-type H. pylori and Typhimurium 14028 supernatants contain signaling substances that induce expression of luminescence in V. harveyi BB170, while the luxS deletion strain EJ103 does not. (B) H. pylori luxS expression in E. coli DH5α restores AI-2 activity. The error bars indicate standard deviations.

    Article Snippet: The bacterial strains used were the clinical isolate H. pylori Alston, a generous gift from David Cave (St. Elizabeth's Hospital, Boston, Mass.), V. harveyi BB170 , and E. coli DH5α (Bio-Rad Laboratories).

    Techniques: Activity Assay, Expressing, Incubation, Activation Assay

    Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain DH5α expressing cI-DivIVA, detected with anti-cI antibodies.

    Journal: Journal of Bacteriology

    Article Title: Streptococcus pneumoniae DivIVA: Localization and Interactions in a MinCD-Free Context ▿ DivIVA: Localization and Interactions in a MinCD-Free Context ▿ †

    doi: 10.1128/JB.01168-06

    Figure Lengend Snippet: Immunoprecipitation to determine the specificity of DivIVA interactions. (A) Immunoprecipitation of GFP-DivIVA-cI-Spo0J complex (lane 1), GFP-Spo0J-cI-DivIVA complex (lane 2), GFP-FtsZ-cI-DivIVA complex (lane 3), and GFP-DivIVA-cI-FtsZ complex (lane 4). (B) Immunoprecipitation of cI-DivIVA-GFP-PrfA complex (lane 1). Protein extracts were immunoprecipitated with anti-GFP antibodies and were detected with anti-cI rabbit polyclonal antibodies by Western blotting as described in Materials and Methods. Lane M contained molecular weight markers. In panel B lane 2 contained crude extract of E. coli strain DH5α expressing cI-DivIVA, detected with anti-cI antibodies.

    Article Snippet: The ligation mixture was transformed into E. coli DH5α competent cells (Invitrogen), and transformants were selected after overnight growth on LB medium plates with ampicillin.

    Techniques: Immunoprecipitation, Western Blot, Molecular Weight, Expressing