dh5α New England Biolabs Search Results


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  • 99
    New England Biolabs dh5α
    Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 197 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α recalacz
    Dh5α Recalacz, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 84/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs competent dh5α
    Instability of octarepeats during DNA replication in mismatch repair-deficient XL-1 Red cells. (A) Mutant clones from replication of pOct5 in XL-1 Red E.coli cells. Plasmid DNA samples were prepared from XL-1 Red colonies after transformation with pOct5 and re-transformed into <t>DH5α</t> cells. Plasmid DNAs from the resulting DH5α colonies were digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 4 DH5α colonies that produced two octarepeat bands of equal molar ratio. (B) Mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Same as in (A) except that pOct11b was used. Shown are plasmid DNAs from 4 colonies that produced two octarepeat bands of equal molar ratio. (C–D) Unusual mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Shown are plasmid DNAs from two pOct11b-transformed XL-1 Red colonies that produced 2–3 octarepeat bands upon digestion with Sac II and Spe I, of which the template-sized band is much stronger than the mutant bands (C). The unequal molar ratio of the octarepeat bands suggests the presence of mixed plasmid DNA species in these colonies. Further transformation of these plasmid DNAs into DH5α cells resulted in separation of the mixed plasmid DNA species and produced colonies that each contained only one of the plasmid DNA species as confirmed by restriction analysis and sequencing (D). For all panels, the octarepeat sequence is indicated above each lane, the arrowhead points to the band whose sequence is shown above the lane, and the black box marks the template-sized Oct5 or Oct11 band from a non-mutant clone. Rep. No., number of repeats; M,100-bp DNA Ladder.
    Competent Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    New England Biolabs dh5α f iq
    Instability of octarepeats during DNA replication in mismatch repair-deficient XL-1 Red cells. (A) Mutant clones from replication of pOct5 in XL-1 Red E.coli cells. Plasmid DNA samples were prepared from XL-1 Red colonies after transformation with pOct5 and re-transformed into <t>DH5α</t> cells. Plasmid DNAs from the resulting DH5α colonies were digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 4 DH5α colonies that produced two octarepeat bands of equal molar ratio. (B) Mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Same as in (A) except that pOct11b was used. Shown are plasmid DNAs from 4 colonies that produced two octarepeat bands of equal molar ratio. (C–D) Unusual mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Shown are plasmid DNAs from two pOct11b-transformed XL-1 Red colonies that produced 2–3 octarepeat bands upon digestion with Sac II and Spe I, of which the template-sized band is much stronger than the mutant bands (C). The unequal molar ratio of the octarepeat bands suggests the presence of mixed plasmid DNA species in these colonies. Further transformation of these plasmid DNAs into DH5α cells resulted in separation of the mixed plasmid DNA species and produced colonies that each contained only one of the plasmid DNA species as confirmed by restriction analysis and sequencing (D). For all panels, the octarepeat sequence is indicated above each lane, the arrowhead points to the band whose sequence is shown above the lane, and the black box marks the template-sized Oct5 or Oct11 band from a non-mutant clone. Rep. No., number of repeats; M,100-bp DNA Ladder.
    Dh5α F Iq, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    83
    New England Biolabs strain dh5α
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Strain Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 83/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α bacteria
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5α Bacteria, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5alpha
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5alpha, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α f laci q
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5α F Laci Q, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 82/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α electrocompetent cells
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5α Electrocompetent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs escherichia coli dh5α
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Escherichia Coli Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 293 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α component cells
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5α Component Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α competent bacteria
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5α Competent Bacteria, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs dh5α chemo competent bacteria
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Dh5α Chemo Competent Bacteria, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs ecoli dh5alpha
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Ecoli Dh5alpha, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 84/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs e coli dh5α mcr
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    E Coli Dh5α Mcr, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs electromax dh5α e electrocompetent cells
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Electromax Dh5α E Electrocompetent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs escherichia coli strain dh5α
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Escherichia Coli Strain Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs e coli k 12 dh5α
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    E Coli K 12 Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs chemically competent dh5α e coli
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Chemically Competent Dh5α E Coli, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs subcloning competent dh5α escherichia coli
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Subcloning Competent Dh5α Escherichia Coli, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs cacl2 competent escherichia coli dh5α f
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
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    New England Biolabs plasmid construction escherichia coli dh5α
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Plasmid Construction Escherichia Coli Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 80/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs escherichia coli dh5α turbo competent cells
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Escherichia Coli Dh5α Turbo Competent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs e coli dh5α chemical competent cells
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    E Coli Dh5α Chemical Competent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 87/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs plasmids e coli strains dh5α
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    Plasmids E Coli Strains Dh5α, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/plasmids e coli strains dh5α/product/New England Biolabs
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    plasmids e coli strains dh5α - by Bioz Stars, 2020-02
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    New England Biolabs e s cherichia coli dh5alpha
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    E S Cherichia Coli Dh5alpha, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 87/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e s cherichia coli dh5alpha/product/New England Biolabs
    Average 87 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
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    New England Biolabs e coli strain dh5α competent cells
    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli <t>DH5α</t> to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.
    E Coli Strain Dh5α Competent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 87/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli strain dh5α competent cells/product/New England Biolabs
    Average 87 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    e coli strain dh5α competent cells - by Bioz Stars, 2020-02
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    Instability of octarepeats during DNA replication in mismatch repair-deficient XL-1 Red cells. (A) Mutant clones from replication of pOct5 in XL-1 Red E.coli cells. Plasmid DNA samples were prepared from XL-1 Red colonies after transformation with pOct5 and re-transformed into DH5α cells. Plasmid DNAs from the resulting DH5α colonies were digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 4 DH5α colonies that produced two octarepeat bands of equal molar ratio. (B) Mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Same as in (A) except that pOct11b was used. Shown are plasmid DNAs from 4 colonies that produced two octarepeat bands of equal molar ratio. (C–D) Unusual mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Shown are plasmid DNAs from two pOct11b-transformed XL-1 Red colonies that produced 2–3 octarepeat bands upon digestion with Sac II and Spe I, of which the template-sized band is much stronger than the mutant bands (C). The unequal molar ratio of the octarepeat bands suggests the presence of mixed plasmid DNA species in these colonies. Further transformation of these plasmid DNAs into DH5α cells resulted in separation of the mixed plasmid DNA species and produced colonies that each contained only one of the plasmid DNA species as confirmed by restriction analysis and sequencing (D). For all panels, the octarepeat sequence is indicated above each lane, the arrowhead points to the band whose sequence is shown above the lane, and the black box marks the template-sized Oct5 or Oct11 band from a non-mutant clone. Rep. No., number of repeats; M,100-bp DNA Ladder.

    Journal: PLoS ONE

    Article Title: Instability of the Octarepeat Region of the Human Prion Protein Gene

    doi: 10.1371/journal.pone.0026635

    Figure Lengend Snippet: Instability of octarepeats during DNA replication in mismatch repair-deficient XL-1 Red cells. (A) Mutant clones from replication of pOct5 in XL-1 Red E.coli cells. Plasmid DNA samples were prepared from XL-1 Red colonies after transformation with pOct5 and re-transformed into DH5α cells. Plasmid DNAs from the resulting DH5α colonies were digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 4 DH5α colonies that produced two octarepeat bands of equal molar ratio. (B) Mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Same as in (A) except that pOct11b was used. Shown are plasmid DNAs from 4 colonies that produced two octarepeat bands of equal molar ratio. (C–D) Unusual mutant clones from replication of pOct11b in XL-1 Red E.coli cells. Shown are plasmid DNAs from two pOct11b-transformed XL-1 Red colonies that produced 2–3 octarepeat bands upon digestion with Sac II and Spe I, of which the template-sized band is much stronger than the mutant bands (C). The unequal molar ratio of the octarepeat bands suggests the presence of mixed plasmid DNA species in these colonies. Further transformation of these plasmid DNAs into DH5α cells resulted in separation of the mixed plasmid DNA species and produced colonies that each contained only one of the plasmid DNA species as confirmed by restriction analysis and sequencing (D). For all panels, the octarepeat sequence is indicated above each lane, the arrowhead points to the band whose sequence is shown above the lane, and the black box marks the template-sized Oct5 or Oct11 band from a non-mutant clone. Rep. No., number of repeats; M,100-bp DNA Ladder.

    Article Snippet: The PCR products were treated with the Wizard PCR clean-up kit (Promega, WI, USA), ligated to pGEM-T (for Pwo-amplified products, A-tailing was done first with Taq DNA polymerase in PCR buffer with 0.2 mM dATP) and transformed into competent DH5α cells (New England Biolabs, MA, USA) on LB-agar plates with X-gal.

    Techniques: Mutagenesis, Clone Assay, Plasmid Preparation, Transformation Assay, Agarose Gel Electrophoresis, Produced, Sequencing

    Mutant plasmids from octarepeat replication in DH5α are all head-to-head dimers. (A) Restriction analysis of replication-mutant plasmids with Spe I, Sac II and Sca I. pOct5 or pOct11b were transformed into DH5α. Plasmid DNAs were prepared from two mutant colonies and two control (non-mutant) colonies each for pOct5 and pOct11b, digested with Spe I, Sac II or Sca I, and separated by agarose gel electrophoresis. All mutant colonies appear to contain a minute amount of monomer plasmids. M1, 100-bp DNA ladder; M2, 1-kb DNA ladder. (B) Diagram of the head-to-head plasmid dimers. The top panel depicts the parental plasmid monomer; the bottom panel depicts the dimer where the newly generated monomer unit is highlighted in thicker lines. The boxes denote the octarepeat inserts.

    Journal: PLoS ONE

    Article Title: Instability of the Octarepeat Region of the Human Prion Protein Gene

    doi: 10.1371/journal.pone.0026635

    Figure Lengend Snippet: Mutant plasmids from octarepeat replication in DH5α are all head-to-head dimers. (A) Restriction analysis of replication-mutant plasmids with Spe I, Sac II and Sca I. pOct5 or pOct11b were transformed into DH5α. Plasmid DNAs were prepared from two mutant colonies and two control (non-mutant) colonies each for pOct5 and pOct11b, digested with Spe I, Sac II or Sca I, and separated by agarose gel electrophoresis. All mutant colonies appear to contain a minute amount of monomer plasmids. M1, 100-bp DNA ladder; M2, 1-kb DNA ladder. (B) Diagram of the head-to-head plasmid dimers. The top panel depicts the parental plasmid monomer; the bottom panel depicts the dimer where the newly generated monomer unit is highlighted in thicker lines. The boxes denote the octarepeat inserts.

    Article Snippet: The PCR products were treated with the Wizard PCR clean-up kit (Promega, WI, USA), ligated to pGEM-T (for Pwo-amplified products, A-tailing was done first with Taq DNA polymerase in PCR buffer with 0.2 mM dATP) and transformed into competent DH5α cells (New England Biolabs, MA, USA) on LB-agar plates with X-gal.

    Techniques: Mutagenesis, Transformation Assay, Plasmid Preparation, Agarose Gel Electrophoresis, Generated

    Schematic diagrams for analysis of octarepeat mutation rate during PCR or replication in E.coli . (A) Measurement of octarepeat mutants resulting from PCR amplification of octarepeats. Cloned PrP ORF sequences (PrP-Oct5 and PrP-Oct11a) were subjected to PCR with primers HP20 and HP306r. The PCR products (depicted in a shaded box), which contained input (green line) and PCR-mutant (red line) octarepeat sequences as well as “paired” molecules (two parallel lines), were cleaned up and ligated to the pGEM-T vector, producing 4 kinds of ligation products: mutant monomer, wild type monomer, wild type dimer, and mutant dimer. The ligation products were transformed into DH5α competent cells, and the resulting colonies were directly examined by PCR with primers HP50f and HP293r. Plasmid DNAs were extracted from colonies containing mutant octarepeats, subjected to restriction analysis with Sac II and Spe I, and sequenced. The number of mutant colonies over the total number of colonies screened was calculated to represent the octarepeat mutation rate during the PCR process. Small oval: individual E.coli cell; big dashed-line oval: E.coli colony. (B) Measurement of octarepeat mutants resulting from DNA replication in E.coli . pOct5 or pOct11b was used to transform competent DH5α or XL-1 Red E.coli cells, and plasmid DNA sample prepared from a single colony (depicted in a shaded box) was used to transform competent DH5α cells. The mutant colonies (containing only mutant plasmid, red dashed-line oval) and new mutant colonies [containing some cells with the NEW replication-mutant octarepeat insert (light purple), light blue dashed-line oval] were screened out as in (A). The number of mutant colonies (excluding the new mutant colonies) over the total number of colonies examined should reflect the octarepeat mutation rate during the 1 st round of plasmid replication and cell division in E.coli (DH5α or XL-1 Red).

    Journal: PLoS ONE

    Article Title: Instability of the Octarepeat Region of the Human Prion Protein Gene

    doi: 10.1371/journal.pone.0026635

    Figure Lengend Snippet: Schematic diagrams for analysis of octarepeat mutation rate during PCR or replication in E.coli . (A) Measurement of octarepeat mutants resulting from PCR amplification of octarepeats. Cloned PrP ORF sequences (PrP-Oct5 and PrP-Oct11a) were subjected to PCR with primers HP20 and HP306r. The PCR products (depicted in a shaded box), which contained input (green line) and PCR-mutant (red line) octarepeat sequences as well as “paired” molecules (two parallel lines), were cleaned up and ligated to the pGEM-T vector, producing 4 kinds of ligation products: mutant monomer, wild type monomer, wild type dimer, and mutant dimer. The ligation products were transformed into DH5α competent cells, and the resulting colonies were directly examined by PCR with primers HP50f and HP293r. Plasmid DNAs were extracted from colonies containing mutant octarepeats, subjected to restriction analysis with Sac II and Spe I, and sequenced. The number of mutant colonies over the total number of colonies screened was calculated to represent the octarepeat mutation rate during the PCR process. Small oval: individual E.coli cell; big dashed-line oval: E.coli colony. (B) Measurement of octarepeat mutants resulting from DNA replication in E.coli . pOct5 or pOct11b was used to transform competent DH5α or XL-1 Red E.coli cells, and plasmid DNA sample prepared from a single colony (depicted in a shaded box) was used to transform competent DH5α cells. The mutant colonies (containing only mutant plasmid, red dashed-line oval) and new mutant colonies [containing some cells with the NEW replication-mutant octarepeat insert (light purple), light blue dashed-line oval] were screened out as in (A). The number of mutant colonies (excluding the new mutant colonies) over the total number of colonies examined should reflect the octarepeat mutation rate during the 1 st round of plasmid replication and cell division in E.coli (DH5α or XL-1 Red).

    Article Snippet: The PCR products were treated with the Wizard PCR clean-up kit (Promega, WI, USA), ligated to pGEM-T (for Pwo-amplified products, A-tailing was done first with Taq DNA polymerase in PCR buffer with 0.2 mM dATP) and transformed into competent DH5α cells (New England Biolabs, MA, USA) on LB-agar plates with X-gal.

    Techniques: Mutagenesis, Polymerase Chain Reaction, Amplification, Clone Assay, Plasmid Preparation, Ligation, Transformation Assay

    Instability of octarepeats during DNA replication in DH5α cells. (A) Mutant clones from replication of pOct5 in DH5α cells. pOct5 was transformed into DH5α. Plasmid DNAs were prepared from the resulting colonies, digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 3 colonies that produced two octarepeat bands of equal molar ratio. (B) Mutant clones from replication of pOct11b in DH5α cells. pOct11b was transformed into DH5α. Plasmid DNAs were prepared from the resulting colonies, digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 4 colonies that produced two octarepeat bands of equal molar ratio. (C–D) Unusual mutant clones from replication of pOct11b in DH5α cells. Shown are plasmid DNAs from two pOct11b-transformed DH5α colonies that produced 2–3 octarepeat bands upon digestion with Sac II and Spe I, of which the template-sized band is much stronger than the mutant bands (C). The unequal molar ratio of the octarepeat bands suggests the presence in these colonies of mixed plasmid DNA species where each species produced one of the octarepeat bands. Re-transformation of these plasmid DNAs into DH5α cells resulted in separation of the mixed plasmid DNA species and produced colonies that each contained only one plasmid DNA species as confirmed by restriction analysis and sequencing (D). For all panels, the octarepeat sequence is indicated above each lane, the arrowhead points to the band whose sequence is shown above the lane, and the black box marks the template-sized Oct5 or Oct11 band from a non-mutant clone. Rep. No., number of repeats; M,100-bp DNA Ladder.

    Journal: PLoS ONE

    Article Title: Instability of the Octarepeat Region of the Human Prion Protein Gene

    doi: 10.1371/journal.pone.0026635

    Figure Lengend Snippet: Instability of octarepeats during DNA replication in DH5α cells. (A) Mutant clones from replication of pOct5 in DH5α cells. pOct5 was transformed into DH5α. Plasmid DNAs were prepared from the resulting colonies, digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 3 colonies that produced two octarepeat bands of equal molar ratio. (B) Mutant clones from replication of pOct11b in DH5α cells. pOct11b was transformed into DH5α. Plasmid DNAs were prepared from the resulting colonies, digested with Sac II and Spe I and separated on a 2% agarose gel. Shown are plasmid DNAs from 4 colonies that produced two octarepeat bands of equal molar ratio. (C–D) Unusual mutant clones from replication of pOct11b in DH5α cells. Shown are plasmid DNAs from two pOct11b-transformed DH5α colonies that produced 2–3 octarepeat bands upon digestion with Sac II and Spe I, of which the template-sized band is much stronger than the mutant bands (C). The unequal molar ratio of the octarepeat bands suggests the presence in these colonies of mixed plasmid DNA species where each species produced one of the octarepeat bands. Re-transformation of these plasmid DNAs into DH5α cells resulted in separation of the mixed plasmid DNA species and produced colonies that each contained only one plasmid DNA species as confirmed by restriction analysis and sequencing (D). For all panels, the octarepeat sequence is indicated above each lane, the arrowhead points to the band whose sequence is shown above the lane, and the black box marks the template-sized Oct5 or Oct11 band from a non-mutant clone. Rep. No., number of repeats; M,100-bp DNA Ladder.

    Article Snippet: The PCR products were treated with the Wizard PCR clean-up kit (Promega, WI, USA), ligated to pGEM-T (for Pwo-amplified products, A-tailing was done first with Taq DNA polymerase in PCR buffer with 0.2 mM dATP) and transformed into competent DH5α cells (New England Biolabs, MA, USA) on LB-agar plates with X-gal.

    Techniques: Mutagenesis, Clone Assay, Transformation Assay, Plasmid Preparation, Agarose Gel Electrophoresis, Produced, Sequencing

    The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli DH5α to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.

    Journal: Journal of Biological Engineering

    Article Title: Utilising datasheets for the informed automated design and build of a synthetic metabolic pathway

    doi: 10.1186/s13036-019-0141-z

    Figure Lengend Snippet: The biological parts utilised for combinatorial construction of a lycopene biosynthetic pathway. a The carotenoid lycopene is produced in E. coli through a heterologous biosynthetic pathway composed of three enzymes (CrtE. CrtB and CrtI). The heterologous proteins use FPP, which is a product of MEP pathway, as a precursor. b : Table S1). The pathway library was assembled and expressed in E. coli DH5α to test lycopene titres. The relative effects of the different design factors had on the titres level of lycopene were modelled using JMP. The model identified biological parts which effected titre levels, this can help aid future designing of the lycopene biosynthetic pathway.

    Article Snippet: The E. coli strain DH5α (NEB, USA) was used for all DNA cloning.

    Techniques: Produced