e coli k12 Search Results


90
ATCC k 12 dh5alpha
Bacterial cell cultures used in this study to test and optimise FISH probes.
K 12 Dh5alpha, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad e coli strain hb101
Bacterial cell cultures used in this study to test and optimise FISH probes.
E Coli Strain Hb101, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Addgene inc rat trka intracellular domain
Bacterial cell cultures used in this study to test and optimise FISH probes.
Rat Trka Intracellular Domain, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Addgene inc e coli k12 strain mg1655
The KH-S1 portal is crucial for PNPase-sRNA-Hfq complex formation (A–C) Electrophoretic mobility shift assays (EMSAs) of wild-type PNPase and KH-S1 mutants with 400 nM RyhB (A), 3ʹETS leuZ (B), and CyaR (C) in the absence and presence of 400 nM Hfq hexamer. Ternary complexes are highlighted with a red dot. Two different PNPase concentrations were used for every PNPase construct (1:1 and 1:3 RNA:PNPase trimer molar ratio), represented by a concentration bar. (D and E) RNA half-life experiments to determine RyhB and CyaR sRNA stabilities in an <t>E.</t> <t>coli</t> strain expressing a 3X-FLAG tagged construct of PNPase WT and mutants. RyhB and CyaR signal intensities were quantified using northern blots and normalized to their corresponding loading controls (SsrA). sRNA decay curves were generated by fitting the normalized signal intensities for each time point. Points and error bars in the curves represent the means and the standard errors (SEM) of at least three independent experiments. Northern blots for RyhB and CyaR half-life measurements corresponding to RNA stability curves are shown and values tabulated in . (F and G) Cell extracts prepared from late exponential phase cultures of E. coli strains expressing WT PNPase, or FLAG-tagged PNPase WT and mutants were used to assess coprecipitation of sRNAs, which were analyzed using northern blot. (G) Fold enrichment of a given RNA upon immunoprecipitation was determined by first calculating the signal intensity per microgram of RNA for the input and the elution from the northern blots in (F). The normalized elution signal was then divided by the input signal. An untagged wild-type strain (WT) was used as a control for data presented in (F) and (G). S1x2: PNPase K657A, R658A; KHx2: PNPase K566A, K571A; S1x4: PNPase R681A, Q682A, R684A, R686A.
E Coli K12 Strain Mg1655, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
Addgene inc chromosomal terminus
The KH-S1 portal is crucial for PNPase-sRNA-Hfq complex formation (A–C) Electrophoretic mobility shift assays (EMSAs) of wild-type PNPase and KH-S1 mutants with 400 nM RyhB (A), 3ʹETS leuZ (B), and CyaR (C) in the absence and presence of 400 nM Hfq hexamer. Ternary complexes are highlighted with a red dot. Two different PNPase concentrations were used for every PNPase construct (1:1 and 1:3 RNA:PNPase trimer molar ratio), represented by a concentration bar. (D and E) RNA half-life experiments to determine RyhB and CyaR sRNA stabilities in an <t>E.</t> <t>coli</t> strain expressing a 3X-FLAG tagged construct of PNPase WT and mutants. RyhB and CyaR signal intensities were quantified using northern blots and normalized to their corresponding loading controls (SsrA). sRNA decay curves were generated by fitting the normalized signal intensities for each time point. Points and error bars in the curves represent the means and the standard errors (SEM) of at least three independent experiments. Northern blots for RyhB and CyaR half-life measurements corresponding to RNA stability curves are shown and values tabulated in . (F and G) Cell extracts prepared from late exponential phase cultures of E. coli strains expressing WT PNPase, or FLAG-tagged PNPase WT and mutants were used to assess coprecipitation of sRNAs, which were analyzed using northern blot. (G) Fold enrichment of a given RNA upon immunoprecipitation was determined by first calculating the signal intensity per microgram of RNA for the input and the elution from the northern blots in (F). The normalized elution signal was then divided by the input signal. An untagged wild-type strain (WT) was used as a control for data presented in (F) and (G). S1x2: PNPase K657A, R658A; KHx2: PNPase K566A, K571A; S1x4: PNPase R681A, Q682A, R684A, R686A.
Chromosomal Terminus, supplied by Addgene inc, 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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91
Addgene inc midreplichore
The KH-S1 portal is crucial for PNPase-sRNA-Hfq complex formation (A–C) Electrophoretic mobility shift assays (EMSAs) of wild-type PNPase and KH-S1 mutants with 400 nM RyhB (A), 3ʹETS leuZ (B), and CyaR (C) in the absence and presence of 400 nM Hfq hexamer. Ternary complexes are highlighted with a red dot. Two different PNPase concentrations were used for every PNPase construct (1:1 and 1:3 RNA:PNPase trimer molar ratio), represented by a concentration bar. (D and E) RNA half-life experiments to determine RyhB and CyaR sRNA stabilities in an <t>E.</t> <t>coli</t> strain expressing a 3X-FLAG tagged construct of PNPase WT and mutants. RyhB and CyaR signal intensities were quantified using northern blots and normalized to their corresponding loading controls (SsrA). sRNA decay curves were generated by fitting the normalized signal intensities for each time point. Points and error bars in the curves represent the means and the standard errors (SEM) of at least three independent experiments. Northern blots for RyhB and CyaR half-life measurements corresponding to RNA stability curves are shown and values tabulated in . (F and G) Cell extracts prepared from late exponential phase cultures of E. coli strains expressing WT PNPase, or FLAG-tagged PNPase WT and mutants were used to assess coprecipitation of sRNAs, which were analyzed using northern blot. (G) Fold enrichment of a given RNA upon immunoprecipitation was determined by first calculating the signal intensity per microgram of RNA for the input and the elution from the northern blots in (F). The normalized elution signal was then divided by the input signal. An untagged wild-type strain (WT) was used as a control for data presented in (F) and (G). S1x2: PNPase K657A, R658A; KHx2: PNPase K566A, K571A; S1x4: PNPase R681A, Q682A, R684A, R686A.
Midreplichore, supplied by Addgene inc, 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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midreplichore - by Bioz Stars, 2026-09
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90
Biogenesis Inc e. coli k12
Antibodies investigated for cross-reactivity
E. Coli K12, supplied by Biogenesis Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Ocimum Biosolutions e. coli k12 arrays
Antibodies investigated for cross-reactivity
E. Coli K12 Arrays, supplied by Ocimum Biosolutions, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Federation of European Neuroscience Societies e. coli k 12
Antibodies investigated for cross-reactivity
E. Coli K 12, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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BioResource International Inc e. coli mg1655 (me7986)
Constructed plasmids and generated strains in this study
E. Coli Mg1655 (Me7986), supplied by BioResource International Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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BEI Resources e. coli strain k-12
Constructed plasmids and generated strains in this study
E. Coli Strain K 12, supplied by BEI Resources, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Bacterial cell cultures used in this study to test and optimise FISH probes.

Journal: Scientific Reports

Article Title: Fluorescence in situ hybridisation in Carnoy’s fixed tonsil tissue

doi: 10.1038/s41598-022-16309-w

Figure Lengend Snippet: Bacterial cell cultures used in this study to test and optimise FISH probes.

Article Snippet: Escherichia coli , K-12 DH5alpha, ATCC PTA-4079 , LabPLUS.

Techniques:

The KH-S1 portal is crucial for PNPase-sRNA-Hfq complex formation (A–C) Electrophoretic mobility shift assays (EMSAs) of wild-type PNPase and KH-S1 mutants with 400 nM RyhB (A), 3ʹETS leuZ (B), and CyaR (C) in the absence and presence of 400 nM Hfq hexamer. Ternary complexes are highlighted with a red dot. Two different PNPase concentrations were used for every PNPase construct (1:1 and 1:3 RNA:PNPase trimer molar ratio), represented by a concentration bar. (D and E) RNA half-life experiments to determine RyhB and CyaR sRNA stabilities in an E. coli strain expressing a 3X-FLAG tagged construct of PNPase WT and mutants. RyhB and CyaR signal intensities were quantified using northern blots and normalized to their corresponding loading controls (SsrA). sRNA decay curves were generated by fitting the normalized signal intensities for each time point. Points and error bars in the curves represent the means and the standard errors (SEM) of at least three independent experiments. Northern blots for RyhB and CyaR half-life measurements corresponding to RNA stability curves are shown and values tabulated in . (F and G) Cell extracts prepared from late exponential phase cultures of E. coli strains expressing WT PNPase, or FLAG-tagged PNPase WT and mutants were used to assess coprecipitation of sRNAs, which were analyzed using northern blot. (G) Fold enrichment of a given RNA upon immunoprecipitation was determined by first calculating the signal intensity per microgram of RNA for the input and the elution from the northern blots in (F). The normalized elution signal was then divided by the input signal. An untagged wild-type strain (WT) was used as a control for data presented in (F) and (G). S1x2: PNPase K657A, R658A; KHx2: PNPase K566A, K571A; S1x4: PNPase R681A, Q682A, R684A, R686A.

Journal: Molecular Cell

Article Title: A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation

doi: 10.1016/j.molcel.2021.05.032

Figure Lengend Snippet: The KH-S1 portal is crucial for PNPase-sRNA-Hfq complex formation (A–C) Electrophoretic mobility shift assays (EMSAs) of wild-type PNPase and KH-S1 mutants with 400 nM RyhB (A), 3ʹETS leuZ (B), and CyaR (C) in the absence and presence of 400 nM Hfq hexamer. Ternary complexes are highlighted with a red dot. Two different PNPase concentrations were used for every PNPase construct (1:1 and 1:3 RNA:PNPase trimer molar ratio), represented by a concentration bar. (D and E) RNA half-life experiments to determine RyhB and CyaR sRNA stabilities in an E. coli strain expressing a 3X-FLAG tagged construct of PNPase WT and mutants. RyhB and CyaR signal intensities were quantified using northern blots and normalized to their corresponding loading controls (SsrA). sRNA decay curves were generated by fitting the normalized signal intensities for each time point. Points and error bars in the curves represent the means and the standard errors (SEM) of at least three independent experiments. Northern blots for RyhB and CyaR half-life measurements corresponding to RNA stability curves are shown and values tabulated in . (F and G) Cell extracts prepared from late exponential phase cultures of E. coli strains expressing WT PNPase, or FLAG-tagged PNPase WT and mutants were used to assess coprecipitation of sRNAs, which were analyzed using northern blot. (G) Fold enrichment of a given RNA upon immunoprecipitation was determined by first calculating the signal intensity per microgram of RNA for the input and the elution from the northern blots in (F). The normalized elution signal was then divided by the input signal. An untagged wild-type strain (WT) was used as a control for data presented in (F) and (G). S1x2: PNPase K657A, R658A; KHx2: PNPase K566A, K571A; S1x4: PNPase R681A, Q682A, R684A, R686A.

Article Snippet: All strains used in this study are derivatives of E. coli K12 strain MG1655 (RRID:Addgene_61440) or BL21DE3.

Techniques: Electrophoretic Mobility Shift Assay, Construct, Concentration Assay, Expressing, Northern Blot, Generated, Immunoprecipitation, Control

Journal: Molecular Cell

Article Title: A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation

doi: 10.1016/j.molcel.2021.05.032

Figure Lengend Snippet:

Article Snippet: All strains used in this study are derivatives of E. coli K12 strain MG1655 (RRID:Addgene_61440) or BL21DE3.

Techniques: Virus, Recombinant, Software

Antibodies investigated for cross-reactivity

Journal:

Article Title: Solid-Phase Capture of Proteins, Spores, and Bacteria

doi: 10.1128/AEM.67.3.1300-1307.2001

Figure Lengend Snippet: Antibodies investigated for cross-reactivity

Article Snippet: E. coli K12 , Cells , Mouse , 1103/77 , E950831 , Biogenesis Inc. d.

Techniques:

List of antibodies and their modifications used to capture BSA, OVA, B. globigii spores, and  E. coli  O157:H7

Journal:

Article Title: Solid-Phase Capture of Proteins, Spores, and Bacteria

doi: 10.1128/AEM.67.3.1300-1307.2001

Figure Lengend Snippet: List of antibodies and their modifications used to capture BSA, OVA, B. globigii spores, and E. coli O157:H7

Article Snippet: E. coli K12 , Cells , Mouse , 1103/77 , E950831 , Biogenesis Inc. d.

Techniques:

Standard curve of capture of B. globigii spores in PBST (A) and E. coli O157:H7 in meat extract and PBST (B) using 3-mm-diameter PEG-modified glass beads. Standard errors of the means are masked by the symbols. The y axis indicates absorbance.

Journal:

Article Title: Solid-Phase Capture of Proteins, Spores, and Bacteria

doi: 10.1128/AEM.67.3.1300-1307.2001

Figure Lengend Snippet: Standard curve of capture of B. globigii spores in PBST (A) and E. coli O157:H7 in meat extract and PBST (B) using 3-mm-diameter PEG-modified glass beads. Standard errors of the means are masked by the symbols. The y axis indicates absorbance.

Article Snippet: E. coli K12 , Cells , Mouse , 1103/77 , E950831 , Biogenesis Inc. d.

Techniques: Modification

Storage and blocking buffers used to test 3-mm-diameter anti-  E. coli  O157:H7 PEG-modified glass beads

Journal:

Article Title: Solid-Phase Capture of Proteins, Spores, and Bacteria

doi: 10.1128/AEM.67.3.1300-1307.2001

Figure Lengend Snippet: Storage and blocking buffers used to test 3-mm-diameter anti- E. coli O157:H7 PEG-modified glass beads

Article Snippet: E. coli K12 , Cells , Mouse , 1103/77 , E950831 , Biogenesis Inc. d.

Techniques: Blocking Assay

Effect of blocking buffers on signal generation using 103 total E. coli O157:H7 cells over time stored at 25°C (⧫) and 7°C (◊). Standard errors of the means are masked by the symbols.

Journal:

Article Title: Solid-Phase Capture of Proteins, Spores, and Bacteria

doi: 10.1128/AEM.67.3.1300-1307.2001

Figure Lengend Snippet: Effect of blocking buffers on signal generation using 103 total E. coli O157:H7 cells over time stored at 25°C (⧫) and 7°C (◊). Standard errors of the means are masked by the symbols.

Article Snippet: E. coli K12 , Cells , Mouse , 1103/77 , E950831 , Biogenesis Inc. d.

Techniques: Blocking Assay

Confocal image of captured E. coli O157:H7 cells. Live cells are stained green, and dead cells are stained red. Slides were coated with PEG and anti-E. coli O157:H7 Ab.

Journal:

Article Title: Solid-Phase Capture of Proteins, Spores, and Bacteria

doi: 10.1128/AEM.67.3.1300-1307.2001

Figure Lengend Snippet: Confocal image of captured E. coli O157:H7 cells. Live cells are stained green, and dead cells are stained red. Slides were coated with PEG and anti-E. coli O157:H7 Ab.

Article Snippet: E. coli K12 , Cells , Mouse , 1103/77 , E950831 , Biogenesis Inc. d.

Techniques: Staining

Constructed plasmids and generated strains in this study

Journal: Applied and Environmental Microbiology

Article Title: Chromosome Engineering To Generate Plasmid-Free Phenylalanine- and Tyrosine-Overproducing Escherichia coli Strains That Can Be Applied in the Generation of Aromatic-Compound-Producing Bacteria

doi: 10.1128/AEM.00525-20

Figure Lengend Snippet: Constructed plasmids and generated strains in this study

Article Snippet: E. coli MG1655 (ME7986) was obtained from the National Institute of Genetics of Japan (National BioResource Project), and its λDE3 lysogen, MG1655(DE3), was used as the host strain for generating Phe- and Tyr-producing strains.

Techniques: Construct, Generated, Variant Assay, Derivative Assay, Transduction

Relationship between the chromosomal locus of PT7lac-lacZ and the β-galactosidase activity (reporter assay). Strain AR-G65 is a BW25113 derived strain harboring PT7lac-lacZ at the tyrR locus of the chromosome (41). (A) The β-galactosidase activities of the respective strains are shown as relative values when the value of strain AR-G65 was 100%. The data were obtained from three independent cultures, and error bars indicate standard deviations. (B) SDS-PAGE analysis of strains harboring T7-controlled shikimate pathway genes integrated into the respective loci of the chromosome. Cont., control strain MG1655(DE3). Combinations of integrated genes and loci are indicated as follows: M-ARG10, PT7lac-ppsA at the adhE locus; M-ARG3, PT7lac-aroGfbr at the tyrR locus; M-ARG4, PT7lac-pheAfbr at the ldhA locus; M-ARG14, PT7lac-tktA at the pflDC locus; M-ARG7, PT7lac-aroA at the pykF locus; and M-ARG99, PT7lac-aroB at the ascF locus.

Journal: Applied and Environmental Microbiology

Article Title: Chromosome Engineering To Generate Plasmid-Free Phenylalanine- and Tyrosine-Overproducing Escherichia coli Strains That Can Be Applied in the Generation of Aromatic-Compound-Producing Bacteria

doi: 10.1128/AEM.00525-20

Figure Lengend Snippet: Relationship between the chromosomal locus of PT7lac-lacZ and the β-galactosidase activity (reporter assay). Strain AR-G65 is a BW25113 derived strain harboring PT7lac-lacZ at the tyrR locus of the chromosome (41). (A) The β-galactosidase activities of the respective strains are shown as relative values when the value of strain AR-G65 was 100%. The data were obtained from three independent cultures, and error bars indicate standard deviations. (B) SDS-PAGE analysis of strains harboring T7-controlled shikimate pathway genes integrated into the respective loci of the chromosome. Cont., control strain MG1655(DE3). Combinations of integrated genes and loci are indicated as follows: M-ARG10, PT7lac-ppsA at the adhE locus; M-ARG3, PT7lac-aroGfbr at the tyrR locus; M-ARG4, PT7lac-pheAfbr at the ldhA locus; M-ARG14, PT7lac-tktA at the pflDC locus; M-ARG7, PT7lac-aroA at the pykF locus; and M-ARG99, PT7lac-aroB at the ascF locus.

Article Snippet: E. coli MG1655 (ME7986) was obtained from the National Institute of Genetics of Japan (National BioResource Project), and its λDE3 lysogen, MG1655(DE3), was used as the host strain for generating Phe- and Tyr-producing strains.

Techniques: Activity Assay, Reporter Assay, Derivative Assay, SDS Page, Control

Comparison of recent Phe- and Tyr-producing  E. coli  strains

Journal: Applied and Environmental Microbiology

Article Title: Chromosome Engineering To Generate Plasmid-Free Phenylalanine- and Tyrosine-Overproducing Escherichia coli Strains That Can Be Applied in the Generation of Aromatic-Compound-Producing Bacteria

doi: 10.1128/AEM.00525-20

Figure Lengend Snippet: Comparison of recent Phe- and Tyr-producing E. coli strains

Article Snippet: E. coli MG1655 (ME7986) was obtained from the National Institute of Genetics of Japan (National BioResource Project), and its λDE3 lysogen, MG1655(DE3), was used as the host strain for generating Phe- and Tyr-producing strains.

Techniques: Comparison, Plasmid Preparation

Synthetic routes for aromatic compounds. The genes used for modification of M-PAR-120 were ldhA(re) from Cupriavidus necator (synonym, Ralstonia eutropha), tdc(lb) from Lactobacillus brevis, ppd(ab) from Azospirillum brasilense, and yahK from Escherichia coli.

Journal: Applied and Environmental Microbiology

Article Title: Chromosome Engineering To Generate Plasmid-Free Phenylalanine- and Tyrosine-Overproducing Escherichia coli Strains That Can Be Applied in the Generation of Aromatic-Compound-Producing Bacteria

doi: 10.1128/AEM.00525-20

Figure Lengend Snippet: Synthetic routes for aromatic compounds. The genes used for modification of M-PAR-120 were ldhA(re) from Cupriavidus necator (synonym, Ralstonia eutropha), tdc(lb) from Lactobacillus brevis, ppd(ab) from Azospirillum brasilense, and yahK from Escherichia coli.

Article Snippet: E. coli MG1655 (ME7986) was obtained from the National Institute of Genetics of Japan (National BioResource Project), and its λDE3 lysogen, MG1655(DE3), was used as the host strain for generating Phe- and Tyr-producing strains.

Techniques: Modification, Full Display Name