coli strains dh5α Search Results


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  • 90
    Thermo Fisher escherichia coli k12 strain dh5α
    Escherichia Coli K12 Strain Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Thermo Fisher coli strains dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Strains Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 67 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    RBC Bioscience coli strain dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Strain Dh5α, supplied by RBC Bioscience, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    tiangen biotech co coli strain dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Strain Dh5α, supplied by tiangen biotech co, used in various techniques. Bioz Stars score: 85/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore coli strains dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Strains Dh5α, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene coli strains dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Strains Dh5α, supplied by Stratagene, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa coli strains dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Strains Dh5α, supplied by TaKaRa, used in various techniques. Bioz Stars score: 83/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa escherchia coli dh5α strain
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Escherchia Coli Dh5α Strain, supplied by TaKaRa, used in various techniques. Bioz Stars score: 83/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher coli dh5α laciq strains
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Coli Dh5α Laciq Strains, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Stratagene escherichia coli strains dh5α
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    Escherichia Coli Strains Dh5α, supplied by Stratagene, used in various techniques. Bioz Stars score: 81/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore e coli dh5α strain
    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. <t>DH5α</t> 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.
    E Coli Dh5α Strain, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa e coli strain dh5α
    Effects of M30-35 on whole plant growth ( A – C ), shoot fresh weight (FW) ( D ), shoot dry weight (DW) ( E ) and root volume ( F ) of ryegrass under various salt treatments (0, 150 and 300 mM NaCl). For ( A – C ), from left to right: Luria broth (LB) medium, <t>DH5α</t> and M30-35 treatments; from top to bottom: 0, 150 and 300 mM NaCl treatments. Values are means and bars indicate standard errors (SEs) ( n = 12). Columns with different letters indicate significant differences among treatments at p
    E Coli Strain Dh5α, supplied by TaKaRa, used in various techniques. Bioz Stars score: 98/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega dh5α escherichia coli strain
    Illustration of the construction and detection of LT mutants e2m to e11m and LT with LT A1 epitope e2, e3, e4, e5, e6, e7, e8, e9, e10, or e11 substituted by the MBP epitope KDAQTNSSS. (A) LT mutant genetic structure and chimeric gene construction. Primers pBR/LT-F and pBR/LT-R were specific for the substitution of each LT A1 epitope with the MBP epitope. (B) Western blot with anti-LT antiserum to detect LT B subunit, mutated LT A subunit, and AB 5 holotoxin-structured LT mutants. Lanes: (+), LT from recombinant LT strain 8460; (−), proteins from host strain E. coli <t>DH5α.</t> M, molecular marker, in kilodaltons.
    Dh5α Escherichia Coli Strain, supplied by Promega, used in various techniques. Bioz Stars score: 89/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Toyobo e coli strain dh5α
    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli <t>DH5α</t> (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P
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    Promega bacterial strains escherichia coli strains dh5α
    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli <t>DH5α</t> (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P
    Bacterial Strains Escherichia Coli Strains Dh5α, supplied by Promega, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare escherichia coli strain dh5α
    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli <t>DH5α</t> (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P
    Escherichia Coli Strain Dh5α, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher coli k 12 strain dh5α
    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli <t>DH5α</t> (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P
    Coli K 12 Strain Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli <t>DH5α</t> (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P
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    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli <t>DH5α</t> (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Growth analysis of BL21(DE3) with or without TetX and <t>DH5α</t> with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.
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    Image Search Results


    ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. DH5α 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.

    Journal: PLoS Genetics

    Article Title: Viral Evasion of a Bacterial Suicide System by RNA-Based Molecular Mimicry Enables Infectious Altruism

    doi: 10.1371/journal.pgen.1003023

    Figure Lengend Snippet: ΦTE-F expresses ToxI RNA during infection. (A) Upper panel; an S1-nuclease protection assay was used to detect ToxI levels from a ToxIN plasmid during ΦTE wt infection, using an antisense probe against the full 5.5 repeat ToxI sequence [46] . The antisense ToxI-probe was first hybridised to 10 µg of total RNA prepared from Pba ToxIN (pMJ4) at different times after ΦTE infection, and then followed by S1-nuclease treatment. Numbers (+) indicate the time (min) after infection or (−) without the addition of phage. Pba ToxIN-FS (pTA47) and Pba serve as positive and negative controls, respectively. A non-hybridized S1-digested probe (+S1) serves as a further negative control. DH5α 1.5 repeats (pTA96), a non-S1 digested probe (−S1) and an in vitro transcribed Hammerhead ribozyme (HHRz), which cleaves itself during transcription, serve as size markers. HHRz was prepared as described previously [45] . Lower panel; Western blot targeting C-terminal FLAG tagged ToxN contained within total protein harvested from Pba ToxIN (pMJ4) at different time points, with (+, left) and without (−, right) phage infection. Time 0 indicates a sample taken immediately after infection. Total protein from Pba ToxIN (pMJ4) (−) serves as positive control. (B) Infection with escape phage ΦTE-F. Levels of ToxI were determined by S1-assay (upper) as described in (A) with and without infection. ToxN levels were estimated by Western blotting (lower) as described in (A). (C) Expression of the ΦTE-F ToxI locus. An S1-nuclease assay targeting ToxI was performed on total RNA of Pba (pBR322) at different times during ΦTE-F infection. Pba ToxIN (pMJ4) and DH5α serve as positive and negative controls, respectively.

    Article Snippet: All experiments were performed with E. coli strain DH5α (Gibco/BRL) or Pectobacterium atrosepticum SCRI1043 and derivatives thereof.

    Techniques: Infection, Plasmid Preparation, Sequencing, Negative Control, In Vitro, Western Blot, Positive Control, Expressing, Nuclease Assay

    Analysis of pseudo-ToxI as a potential antitoxin. (A) Alignment of the pseudo-ToxI and ToxI RNA sequences. Pseudo-ToxI nucleotides are coloured to match (B) and (C), with the green and purple bases denoting the 5′ and 3′ ends of a single pseudoknot, respectively. Mutated nucleotides in pseudo-ToxI are coloured orange and numbered according to their grouping, whilst the asterisk indicates the additional 3′ nucleotide. The dotted line connecting the U in group 3 indicates the uracil that is deleted in the case of expanded repeats with 2T sequences rather than 3T. (B) Schematic of the ToxI pseudoknot. Each position containing a mutation in the pseudo-ToxI RNA has been bracketed, with the ToxI base separated from the pseudo-ToxI base by a ‘/’. The mutations have been grouped 1–5, according to position, and highlighted in orange, with the 5′ and 3′ termini in green and violet, respectively. Indels, such as U17 that is deleted in some pseudo-ToxI repeats, and the additional A* inserted in all, have been bordered by a dashed line. Base interactions are indicated by black lines, and duplex and triplex base-interactions are bordered in grey. (C) Detail of the ToxIN trimer with each pseudoknot shown either in blue, purple or beige. Each ToxN monomer is shown as a grey surface. The blue pseudoknot is oriented relative to (B). The positions of mutation groups are shown, with the group number encircled in the same colour as the corresponding pseudoknot. The additional nucleotide of group 5 is not visible as this was not in the original solved ToxIN structure. PDB: 2XDB. (D) Pseudo-ToxI cannot protect from ToxN in an over-expression assay. Protection assays were conducted as per Materials and Methods using strains of E. coli DH5α carrying both pTA49 (inducible ToxN) and a second inducible antitoxin vector as shown, including use of pTA100 as a vector-only control, “vector”. Error bars indicate the standard deviation of triplicate data. (E) Protection assays using mutants of ToxI carried out as in (D) with the antitoxin mutations in each construct numbered as per (B). (F) Protection assays carried out as in (D), testing the full escape loci of ΦTE wt, ΦTE-A and ΦTE-F with full ToxI as a positive control. Under these conditions, there was sufficient antitoxin present to inhibit induced ToxN even without specific induction of the ToxI and ΦTE-F constructs.

    Journal: PLoS Genetics

    Article Title: Viral Evasion of a Bacterial Suicide System by RNA-Based Molecular Mimicry Enables Infectious Altruism

    doi: 10.1371/journal.pgen.1003023

    Figure Lengend Snippet: Analysis of pseudo-ToxI as a potential antitoxin. (A) Alignment of the pseudo-ToxI and ToxI RNA sequences. Pseudo-ToxI nucleotides are coloured to match (B) and (C), with the green and purple bases denoting the 5′ and 3′ ends of a single pseudoknot, respectively. Mutated nucleotides in pseudo-ToxI are coloured orange and numbered according to their grouping, whilst the asterisk indicates the additional 3′ nucleotide. The dotted line connecting the U in group 3 indicates the uracil that is deleted in the case of expanded repeats with 2T sequences rather than 3T. (B) Schematic of the ToxI pseudoknot. Each position containing a mutation in the pseudo-ToxI RNA has been bracketed, with the ToxI base separated from the pseudo-ToxI base by a ‘/’. The mutations have been grouped 1–5, according to position, and highlighted in orange, with the 5′ and 3′ termini in green and violet, respectively. Indels, such as U17 that is deleted in some pseudo-ToxI repeats, and the additional A* inserted in all, have been bordered by a dashed line. Base interactions are indicated by black lines, and duplex and triplex base-interactions are bordered in grey. (C) Detail of the ToxIN trimer with each pseudoknot shown either in blue, purple or beige. Each ToxN monomer is shown as a grey surface. The blue pseudoknot is oriented relative to (B). The positions of mutation groups are shown, with the group number encircled in the same colour as the corresponding pseudoknot. The additional nucleotide of group 5 is not visible as this was not in the original solved ToxIN structure. PDB: 2XDB. (D) Pseudo-ToxI cannot protect from ToxN in an over-expression assay. Protection assays were conducted as per Materials and Methods using strains of E. coli DH5α carrying both pTA49 (inducible ToxN) and a second inducible antitoxin vector as shown, including use of pTA100 as a vector-only control, “vector”. Error bars indicate the standard deviation of triplicate data. (E) Protection assays using mutants of ToxI carried out as in (D) with the antitoxin mutations in each construct numbered as per (B). (F) Protection assays carried out as in (D), testing the full escape loci of ΦTE wt, ΦTE-A and ΦTE-F with full ToxI as a positive control. Under these conditions, there was sufficient antitoxin present to inhibit induced ToxN even without specific induction of the ToxI and ΦTE-F constructs.

    Article Snippet: All experiments were performed with E. coli strain DH5α (Gibco/BRL) or Pectobacterium atrosepticum SCRI1043 and derivatives thereof.

    Techniques: Mutagenesis, Over Expression, Plasmid Preparation, Standard Deviation, Construct, Positive Control

    Effects of M30-35 on whole plant growth ( A – C ), shoot fresh weight (FW) ( D ), shoot dry weight (DW) ( E ) and root volume ( F ) of ryegrass under various salt treatments (0, 150 and 300 mM NaCl). For ( A – C ), from left to right: Luria broth (LB) medium, DH5α and M30-35 treatments; from top to bottom: 0, 150 and 300 mM NaCl treatments. Values are means and bars indicate standard errors (SEs) ( n = 12). Columns with different letters indicate significant differences among treatments at p

    Journal: International Journal of Molecular Sciences

    Article Title: Induced Salt Tolerance of Perennial Ryegrass by a Novel Bacterium Strain from the Rhizosphere of a Desert Shrub Haloxylon ammodendron

    doi: 10.3390/ijms19020469

    Figure Lengend Snippet: Effects of M30-35 on whole plant growth ( A – C ), shoot fresh weight (FW) ( D ), shoot dry weight (DW) ( E ) and root volume ( F ) of ryegrass under various salt treatments (0, 150 and 300 mM NaCl). For ( A – C ), from left to right: Luria broth (LB) medium, DH5α and M30-35 treatments; from top to bottom: 0, 150 and 300 mM NaCl treatments. Values are means and bars indicate standard errors (SEs) ( n = 12). Columns with different letters indicate significant differences among treatments at p

    Article Snippet: Strain M30-35 was in our laboratory at Lanzhou University, Lanzhou, China, and E. coli strain DH5α was purchased from Takara Biotechnology (Dalian) Co., Ltd., Dalian, China.

    Techniques:

    Illustration of the construction and detection of LT mutants e2m to e11m and LT with LT A1 epitope e2, e3, e4, e5, e6, e7, e8, e9, e10, or e11 substituted by the MBP epitope KDAQTNSSS. (A) LT mutant genetic structure and chimeric gene construction. Primers pBR/LT-F and pBR/LT-R were specific for the substitution of each LT A1 epitope with the MBP epitope. (B) Western blot with anti-LT antiserum to detect LT B subunit, mutated LT A subunit, and AB 5 holotoxin-structured LT mutants. Lanes: (+), LT from recombinant LT strain 8460; (−), proteins from host strain E. coli DH5α. M, molecular marker, in kilodaltons.

    Journal: Applied and Environmental Microbiology

    Article Title: Significance of Enterotoxigenic Escherichia coli (ETEC) Heat-Labile Toxin (LT) Enzymatic Subunit Epitopes in LT Enterotoxicity and Immunogenicity

    doi: 10.1128/AEM.00849-18

    Figure Lengend Snippet: Illustration of the construction and detection of LT mutants e2m to e11m and LT with LT A1 epitope e2, e3, e4, e5, e6, e7, e8, e9, e10, or e11 substituted by the MBP epitope KDAQTNSSS. (A) LT mutant genetic structure and chimeric gene construction. Primers pBR/LT-F and pBR/LT-R were specific for the substitution of each LT A1 epitope with the MBP epitope. (B) Western blot with anti-LT antiserum to detect LT B subunit, mutated LT A subunit, and AB 5 holotoxin-structured LT mutants. Lanes: (+), LT from recombinant LT strain 8460; (−), proteins from host strain E. coli DH5α. M, molecular marker, in kilodaltons.

    Article Snippet: Mutant LT genes with nucleotides coding each LTA1 epitope substituted with MBP epitope KDAQTNSSS were cloned in pBR322 vector and expressed in E. coli strain DH5α (Promega).

    Techniques: Mutagenesis, Western Blot, Recombinant, Marker

    Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli DH5α (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P

    Journal: PLoS ONE

    Article Title: Pseudomonas aeruginosa serA Gene Is Required for Bacterial Translocation through Caco-2 Cell Monolayers

    doi: 10.1371/journal.pone.0169367

    Figure Lengend Snippet: Fly survival experiments. Virulence of the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), E . coli DH5α (as a negative control), and WT in the presence of L -serine (10, 20, 30, 40, and 50 mM) was evaluated. Significant differences, based on the log-rank test, were observed between WT and DH5α (*: P

    Article Snippet: E . coli DH5α strain was used as a control strain that does not penetrate epithelial cell monolayers [ ] and was purchased from TOYOBO, Japan.

    Techniques: Mutagenesis, Negative Control

    Bacterial adherence to Caco-2 cells for the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), PAO1Tn:: flgE mutant ( ΔflgE ), E . coli DH5α (as a negative control), and WT in the presence of L -serine (20, 30, 40, and 50 mM). Bacterial adherence was determined based on the number of adhered bacteria per Caco-2 cell. The assay was performed in six replicates, and the results are expressed as the mean ± SD. Significant differences were observed between WT and ΔserA (*: P

    Journal: PLoS ONE

    Article Title: Pseudomonas aeruginosa serA Gene Is Required for Bacterial Translocation through Caco-2 Cell Monolayers

    doi: 10.1371/journal.pone.0169367

    Figure Lengend Snippet: Bacterial adherence to Caco-2 cells for the wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), PAO1Tn:: flgE mutant ( ΔflgE ), E . coli DH5α (as a negative control), and WT in the presence of L -serine (20, 30, 40, and 50 mM). Bacterial adherence was determined based on the number of adhered bacteria per Caco-2 cell. The assay was performed in six replicates, and the results are expressed as the mean ± SD. Significant differences were observed between WT and ΔserA (*: P

    Article Snippet: E . coli DH5α strain was used as a control strain that does not penetrate epithelial cell monolayers [ ] and was purchased from TOYOBO, Japan.

    Techniques: Mutagenesis, Negative Control

    Penetration activity of P . aeruginosa strains. (A) The wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), and PAO1Tn:: flgE mutant ( ΔflgE ) were inoculated onto the apical surfaces of Caco-2 cell monolayers at an MOI of 100, and the number of bacteria in the basolateral medium was counted at 6 h after infection. The assay was performed in triplicate, and the results are expressed as the mean ± SD. E . coli DH5α was used as a negative control. *#: P

    Journal: PLoS ONE

    Article Title: Pseudomonas aeruginosa serA Gene Is Required for Bacterial Translocation through Caco-2 Cell Monolayers

    doi: 10.1371/journal.pone.0169367

    Figure Lengend Snippet: Penetration activity of P . aeruginosa strains. (A) The wild-type strain (WT), PAO1Tn:: serA mutant ( ΔserA ), PAO1Tn:: serA (pUCP19- serA ) complementary strain (+ serA ), and PAO1Tn:: flgE mutant ( ΔflgE ) were inoculated onto the apical surfaces of Caco-2 cell monolayers at an MOI of 100, and the number of bacteria in the basolateral medium was counted at 6 h after infection. The assay was performed in triplicate, and the results are expressed as the mean ± SD. E . coli DH5α was used as a negative control. *#: P

    Article Snippet: E . coli DH5α strain was used as a control strain that does not penetrate epithelial cell monolayers [ ] and was purchased from TOYOBO, Japan.

    Techniques: Activity Assay, Mutagenesis, Infection, Negative Control

    PGDH activity assay. (A) SDS-PAGE analysis to verify overexpression of the P . aeruginosa serA and synthesis of SerA proteins in crude extract isolated from DH5α (ptac-85- serA ) culture (SerA) and from DH5α (ptac-85) culture (mock). The red arrow indicates an overexpressed band at the expected size of 44 kDa for P . aeruginosa SerA. (B) Inhibitory effect of 50 mM L -serine on PGDH activity of SerA proteins (mU/mg) in crude extract isolated from DH5α (ptac-85- serA ) culture (SerA) and from DH5α (ptac-85) culture (mock). The assay was performed in five replicates, and the results are expressed as the mean ± SD. Significant differences were observed between SerA and mock (*: P

    Journal: PLoS ONE

    Article Title: Pseudomonas aeruginosa serA Gene Is Required for Bacterial Translocation through Caco-2 Cell Monolayers

    doi: 10.1371/journal.pone.0169367

    Figure Lengend Snippet: PGDH activity assay. (A) SDS-PAGE analysis to verify overexpression of the P . aeruginosa serA and synthesis of SerA proteins in crude extract isolated from DH5α (ptac-85- serA ) culture (SerA) and from DH5α (ptac-85) culture (mock). The red arrow indicates an overexpressed band at the expected size of 44 kDa for P . aeruginosa SerA. (B) Inhibitory effect of 50 mM L -serine on PGDH activity of SerA proteins (mU/mg) in crude extract isolated from DH5α (ptac-85- serA ) culture (SerA) and from DH5α (ptac-85) culture (mock). The assay was performed in five replicates, and the results are expressed as the mean ± SD. Significant differences were observed between SerA and mock (*: P

    Article Snippet: E . coli DH5α strain was used as a control strain that does not penetrate epithelial cell monolayers [ ] and was purchased from TOYOBO, Japan.

    Techniques: Activity Assay, SDS Page, Over Expression, Isolation

    Motility assays. (A) Swimming motility of WT, ΔserA , + serA , and E . coli DH5α (as a negative control). A representative image from the swimming motility assay is shown. The major axis of swimming is the longest length of the swimming area. The assay was performed in triplicate, and the results are expressed as the mean ± SD. Significant differences were observed between WT and ΔserA (*: P

    Journal: PLoS ONE

    Article Title: Pseudomonas aeruginosa serA Gene Is Required for Bacterial Translocation through Caco-2 Cell Monolayers

    doi: 10.1371/journal.pone.0169367

    Figure Lengend Snippet: Motility assays. (A) Swimming motility of WT, ΔserA , + serA , and E . coli DH5α (as a negative control). A representative image from the swimming motility assay is shown. The major axis of swimming is the longest length of the swimming area. The assay was performed in triplicate, and the results are expressed as the mean ± SD. Significant differences were observed between WT and ΔserA (*: P

    Article Snippet: E . coli DH5α strain was used as a control strain that does not penetrate epithelial cell monolayers [ ] and was purchased from TOYOBO, Japan.

    Techniques: Negative Control, Motility Assay

    Growth analysis of BL21(DE3) with or without TetX and DH5α with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.

    Journal: Synthetic and Systems Biotechnology

    Article Title: A genetically engineered Escherichia coli that senses and degrades tetracycline antibiotic residue

    doi: 10.1016/j.synbio.2018.05.001

    Figure Lengend Snippet: Growth analysis of BL21(DE3) with or without TetX and DH5α with or without TetX-GFP fusion protein. (a) culture of BL21(DE3) with empty pET-22b(+) plasmid (upper panel) or pET-22b(+)-tet(X) (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 20, 50 μg/mL Tc. Expression of TetX in BL21(DE3) resists the bacteriostatic effect by modification and inactivation of tetracycline. (b) culture of DH5α with pSB1C3- P Tet -gfp plasmid (upper panel) or pSB1C3- P Tet -tet(X)-gfp (lower panel) was diluted 1, 10, 100, 1000 fold and spotted on LB agar plate with 0, 5, 20 μg/mL Tc. TetX and GFP fusion protein in DH5α still maintains its activity for modification and inactivation of tetracycline.

    Article Snippet: All plasmids were assembled, amplified and tested using E. coli strain DH5α (Transgene Biotech CD201).

    Techniques: Positron Emission Tomography, Plasmid Preparation, Expressing, Modification, Activity Assay