bst dna polymerase  (New England Biolabs)


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    Name:
    Bst 3 0 DNA Polymerase
    Description:
    Bst 3 0 DNA Polymerase 8 000 units
    Catalog Number:
    m0374l
    Price:
    278
    Size:
    8 000 units
    Category:
    Thermostable DNA Polymerases
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    Structured Review

    New England Biolabs bst dna polymerase
    Bst 3 0 DNA Polymerase
    Bst 3 0 DNA Polymerase 8 000 units
    https://www.bioz.com/result/bst dna polymerase/product/New England Biolabs
    Average 99 stars, based on 114 article reviews
    Price from $9.99 to $1999.99
    bst dna polymerase - by Bioz Stars, 2020-08
    99/100 stars

    Images

    1) Product Images from "Evolution of a General RNA-Cleaving FANA Enzyme"

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme

    Journal: Nature Communications

    doi: 10.1038/s41467-018-07611-1

    FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)
    Figure Legend Snippet: FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)

    Techniques Used: In Vitro, Activity Assay, Purification, Polyacrylamide Gel Electrophoresis, Mutagenesis

    2) Product Images from "Real-time kinetics and high-resolution melt curves in single-molecule digital LAMP to differentiate and study specific and non-specific amplification"

    Article Title: Real-time kinetics and high-resolution melt curves in single-molecule digital LAMP to differentiate and study specific and non-specific amplification

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkaa099

    Impacts of host (human) genomic DNA in human haploid genome equivalents (HHGE) on specific and non-specific amplification. Plots of T m as a function TTP using Bst 2.0 at ( A ) 0 HHGE per μl; ( B ) 0.01 HHGE per μL, ( C ) 1 HHGE per μl, ( D ) 100 HHGE per μl and ( E ) 5000 HHGE per μl; and using Bst 3.0 at ( F ) 0 HHGE per μl, ( G ) 0.01 HHGE per μl, ( H ) 1 HHGE per μl, ( I ) 100 HHGE per μl ( J ) 5000 HHGE per μl in the presence of template (blue) and NTC (red). N = 3 for all conditions, except Bst 3.0 at 0 and 100 HHGE per μl in the presence of template, where N = 6.
    Figure Legend Snippet: Impacts of host (human) genomic DNA in human haploid genome equivalents (HHGE) on specific and non-specific amplification. Plots of T m as a function TTP using Bst 2.0 at ( A ) 0 HHGE per μl; ( B ) 0.01 HHGE per μL, ( C ) 1 HHGE per μl, ( D ) 100 HHGE per μl and ( E ) 5000 HHGE per μl; and using Bst 3.0 at ( F ) 0 HHGE per μl, ( G ) 0.01 HHGE per μl, ( H ) 1 HHGE per μl, ( I ) 100 HHGE per μl ( J ) 5000 HHGE per μl in the presence of template (blue) and NTC (red). N = 3 for all conditions, except Bst 3.0 at 0 and 100 HHGE per μl in the presence of template, where N = 6.

    Techniques Used: Amplification

    3) Product Images from "Evolution of a General RNA-Cleaving FANA Enzyme"

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme

    Journal: Nature Communications

    doi: 10.1038/s41467-018-07611-1

    FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)
    Figure Legend Snippet: FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)

    Techniques Used: In Vitro, Activity Assay, Purification, Polyacrylamide Gel Electrophoresis, Mutagenesis

    Related Articles

    Gel Extraction:

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme
    Article Snippet: .. ThermoPol buffer, Taq DNA polymerase, G. stearothermophilus Bst DNA polymerase, LF, and its variants Bst 2.0 DNA polymerase (2.0), and Bst 3.0 DNA polymerase (3.0), DH5α competent cells, and Monarch DNA gel extraction kits were purchased from New England Biolabs (Ipswich, MA). .. 3′–5′ exonuclease-deficient (exo−) archaeal polymerases isolated from Thermococcus sp. 9°N (9°N), Pyrococcus sp. deep vent (DV), T. gorgonarius (Tgo), T. kodakarensis (Kod), and G. stearothermophilus Bst DNA polymerase, LF* were expressed and purified from E. coli of the XL1-Blue strain from Agilent Technologies (Santa Clara, CA) as previously described .

    Amplification:

    Article Title: Development of a thermostabilised triplex LAMP assay with dry-reagent four target lateral flow dipstick for detection of Entamoeba histolytica and non-pathogenic Entamoeba spp.
    Article Snippet: .. This study highlighted the development of a four target nitrocellulose-based nucleic acid lateral flow immunoassay biosensor in a dry-reagent strip format for interpretation of double-labelled double-stranded amplicons from thermostabilised triplex loop-mediated isothermal amplification assay. .. This study highlighted the development of a four target nitrocellulose-based nucleic acid lateral flow immunoassay biosensor in a dry-reagent strip format for interpretation of double-labelled double-stranded amplicons from thermostabilised triplex loop-mediated isothermal amplification assay.

    Article Title: Stable fabrication of a large nanopore by controlled dielectric breakdown in a high-pH solution for the detection of various-sized molecules
    Article Snippet: .. The elongation reaction was performed in 50-μL reaction volumes consisting of 3 μM primer, 3 μM ssDNA, 320 U Bst 3.0 DNA polymerase, 1X isothermal amplification buffer, 1 mM dNTPs and 1 mM MgSO4 (New England Biolabs, Ipswich, MA). .. The product after the elongation reaction was purified using NucleoSpin® Gel and PCR Clean-up (Takara Bio Inc, Japan).

    Blocking Assay:

    Article Title: Development of a thermostabilised triplex LAMP assay with dry-reagent four target lateral flow dipstick for detection of Entamoeba histolytica and non-pathogenic Entamoeba spp.
    Article Snippet: .. This study highlighted the development of a four target nitrocellulose-based nucleic acid lateral flow immunoassay biosensor in a dry-reagent strip format for interpretation of double-labelled double-stranded amplicons from thermostabilised triplex loop-mediated isothermal amplification assay. .. This study highlighted the development of a four target nitrocellulose-based nucleic acid lateral flow immunoassay biosensor in a dry-reagent strip format for interpretation of double-labelled double-stranded amplicons from thermostabilised triplex loop-mediated isothermal amplification assay.

    Purification:

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme
    Article Snippet: .. We evaluated three commercial versions of Bst DNA polymerase (LF, 2.0, and 3.0 from New England Biolabs), along with a second version of the wild-type LF polymerase (LF*) that was expressed and purified from Escherichia coli . .. Surprisingly, each of the enzymes tested exhibited strong FANA reverse transcriptase activity following a short 30 min incubation at 50 °C with dNTP substrates (Fig. ).

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme
    Article Snippet: .. We evaluated three commercial versions of Bst DNA polymerase (LF, 2.0, and 3.0 from New England Biolabs), along with a second version of the wild-type LF polymerase (LF*) that was expressed and purified from Escherichia coli . .. Surprisingly, each of the enzymes tested exhibited strong FANA reverse transcriptase activity following a short 30 min incubation at 50 °C with dNTP substrates (Fig. ).

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    New England Biolabs bst 3 0 dna polymerase
    LAMP assay outputs comparing agarose gel electrophoresis (top of panels) and Sybr Green I end-point detection (bottom of panels). Specific F3/B3 primers and genomic DNA from ( a )  Methanoculleus , ( b )  Methanothermobacter , ( c )  Methanococcus,  and ( d )  Methanobrevibacter  were used in assays performed with either Bst 3.0 ( a , c , d ) or Bst 2.0 ( b ). Bacterial DNA (blue line) originated from  Escherichia coli  (lane 1),  Staphylococcus epidermidis  (lane 2), and  Bacillus  sp. 3PL (lane 3). Archaeal DNA (orange line) originated from  Methanococcus maripaludis  (lane 4),  Methanoculleus marisnigri  (lane 5), and  Methanothermobacter thermoautotrophicus  (lane 6), eukaryotic DNA was extracted from wheat root rhizobiome (green line, lane 7). For ( d ), eDNA extracted from two  Methanobrevibacter  positive (see  Figure 2 ) stool samples was used as a template (yellow line). A non-template control (NTC) was included in all assays.
    Bst 3 0 Dna Polymerase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bst 3 0 dna polymerase/product/New England Biolabs
    Average 99 stars, based on 95 article reviews
    Price from $9.99 to $1999.99
    bst 3 0 dna polymerase - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    Image Search Results


    LAMP assay outputs comparing agarose gel electrophoresis (top of panels) and Sybr Green I end-point detection (bottom of panels). Specific F3/B3 primers and genomic DNA from ( a )  Methanoculleus , ( b )  Methanothermobacter , ( c )  Methanococcus,  and ( d )  Methanobrevibacter  were used in assays performed with either Bst 3.0 ( a , c , d ) or Bst 2.0 ( b ). Bacterial DNA (blue line) originated from  Escherichia coli  (lane 1),  Staphylococcus epidermidis  (lane 2), and  Bacillus  sp. 3PL (lane 3). Archaeal DNA (orange line) originated from  Methanococcus maripaludis  (lane 4),  Methanoculleus marisnigri  (lane 5), and  Methanothermobacter thermoautotrophicus  (lane 6), eukaryotic DNA was extracted from wheat root rhizobiome (green line, lane 7). For ( d ), eDNA extracted from two  Methanobrevibacter  positive (see  Figure 2 ) stool samples was used as a template (yellow line). A non-template control (NTC) was included in all assays.

    Journal: Microorganisms

    Article Title: A Rapid, Sensitive, Low-Cost Assay for Detecting Hydrogenotrophic Methanogens in Anaerobic Digesters Using Loop-Mediated Isothermal Amplification

    doi: 10.3390/microorganisms8050740

    Figure Lengend Snippet: LAMP assay outputs comparing agarose gel electrophoresis (top of panels) and Sybr Green I end-point detection (bottom of panels). Specific F3/B3 primers and genomic DNA from ( a ) Methanoculleus , ( b ) Methanothermobacter , ( c ) Methanococcus, and ( d ) Methanobrevibacter were used in assays performed with either Bst 3.0 ( a , c , d ) or Bst 2.0 ( b ). Bacterial DNA (blue line) originated from Escherichia coli (lane 1), Staphylococcus epidermidis (lane 2), and Bacillus sp. 3PL (lane 3). Archaeal DNA (orange line) originated from Methanococcus maripaludis (lane 4), Methanoculleus marisnigri (lane 5), and Methanothermobacter thermoautotrophicus (lane 6), eukaryotic DNA was extracted from wheat root rhizobiome (green line, lane 7). For ( d ), eDNA extracted from two Methanobrevibacter positive (see Figure 2 ) stool samples was used as a template (yellow line). A non-template control (NTC) was included in all assays.

    Article Snippet: LAMP reactions with Mcu and Mco primers were performed in technical duplicates using 2.5 μL 10× reaction buffer, 1.5 μL 100 mM MgSO4, 3.5 μL 10 mM dNTPs (source), 2.5 μL 10× primer mix (see LAMP assay section), 1 μL Bst 3.0 enzyme (NEB, #M0374S), and 1 μL (10 ng/μL–0.001 ng/μL) DNA.

    Techniques: Lamp Assay, Agarose Gel Electrophoresis, SYBR Green Assay

    LAMP assay outputs comparing agarose gel electrophoresis (top of panels) and Sybr Green I end-point detection (bottom of panels). Assays used primers targeted to species with the genera  Methanoculleus  ( a ),  Methanothermobacter  ( b ),  Methanococcus  ( c ), and  Methanobrevibacter  ( d ). Assays were performed with Bst 3.0 ( a , c , d ) or Warm Start Bst 2.0 chemistry ( b ). Genomic DNA (20 ng) from  Methanoculleus  ( a ) , Methanothermobacter  ( b ), or  Methanococcus  ( c ) was used as a positive control (lane 1, red line). LAMP assays were performed with metagenomic DNA from process scale mesophilic digesters (lanes 2, 3), lab-scale mesophilic digesters (lanes 4, 5), lab-scale thermophilic anaerobic digesters (lanes 6, 7; green line), salt marsh sediment (lanes 8, 9; orange line), garden soil (lane 10; orange line), or human stool samples (lanes 11, 12; blue line). A non-template control (NTC) was included in all assays.

    Journal: Microorganisms

    Article Title: A Rapid, Sensitive, Low-Cost Assay for Detecting Hydrogenotrophic Methanogens in Anaerobic Digesters Using Loop-Mediated Isothermal Amplification

    doi: 10.3390/microorganisms8050740

    Figure Lengend Snippet: LAMP assay outputs comparing agarose gel electrophoresis (top of panels) and Sybr Green I end-point detection (bottom of panels). Assays used primers targeted to species with the genera Methanoculleus ( a ), Methanothermobacter ( b ), Methanococcus ( c ), and Methanobrevibacter ( d ). Assays were performed with Bst 3.0 ( a , c , d ) or Warm Start Bst 2.0 chemistry ( b ). Genomic DNA (20 ng) from Methanoculleus ( a ) , Methanothermobacter ( b ), or Methanococcus ( c ) was used as a positive control (lane 1, red line). LAMP assays were performed with metagenomic DNA from process scale mesophilic digesters (lanes 2, 3), lab-scale mesophilic digesters (lanes 4, 5), lab-scale thermophilic anaerobic digesters (lanes 6, 7; green line), salt marsh sediment (lanes 8, 9; orange line), garden soil (lane 10; orange line), or human stool samples (lanes 11, 12; blue line). A non-template control (NTC) was included in all assays.

    Article Snippet: LAMP reactions with Mcu and Mco primers were performed in technical duplicates using 2.5 μL 10× reaction buffer, 1.5 μL 100 mM MgSO4, 3.5 μL 10 mM dNTPs (source), 2.5 μL 10× primer mix (see LAMP assay section), 1 μL Bst 3.0 enzyme (NEB, #M0374S), and 1 μL (10 ng/μL–0.001 ng/μL) DNA.

    Techniques: Lamp Assay, Agarose Gel Electrophoresis, SYBR Green Assay, Positive Control

    FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)

    Journal: Nature Communications

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme

    doi: 10.1038/s41467-018-07611-1

    Figure Lengend Snippet: FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)

    Article Snippet: We evaluated three commercial versions of Bst DNA polymerase (LF, 2.0, and 3.0 from New England Biolabs), along with a second version of the wild-type LF polymerase (LF*) that was expressed and purified from Escherichia coli .

    Techniques: In Vitro, Activity Assay, Purification, Polyacrylamide Gel Electrophoresis, Mutagenesis

    Impacts of host (human) genomic DNA in human haploid genome equivalents (HHGE) on specific and non-specific amplification. Plots of T m as a function TTP using Bst 2.0 at ( A ) 0 HHGE per μl; ( B ) 0.01 HHGE per μL, ( C ) 1 HHGE per μl, ( D ) 100 HHGE per μl and ( E ) 5000 HHGE per μl; and using Bst 3.0 at ( F ) 0 HHGE per μl, ( G ) 0.01 HHGE per μl, ( H ) 1 HHGE per μl, ( I ) 100 HHGE per μl ( J ) 5000 HHGE per μl in the presence of template (blue) and NTC (red). N = 3 for all conditions, except Bst 3.0 at 0 and 100 HHGE per μl in the presence of template, where N = 6.

    Journal: Nucleic Acids Research

    Article Title: Real-time kinetics and high-resolution melt curves in single-molecule digital LAMP to differentiate and study specific and non-specific amplification

    doi: 10.1093/nar/gkaa099

    Figure Lengend Snippet: Impacts of host (human) genomic DNA in human haploid genome equivalents (HHGE) on specific and non-specific amplification. Plots of T m as a function TTP using Bst 2.0 at ( A ) 0 HHGE per μl; ( B ) 0.01 HHGE per μL, ( C ) 1 HHGE per μl, ( D ) 100 HHGE per μl and ( E ) 5000 HHGE per μl; and using Bst 3.0 at ( F ) 0 HHGE per μl, ( G ) 0.01 HHGE per μl, ( H ) 1 HHGE per μl, ( I ) 100 HHGE per μl ( J ) 5000 HHGE per μl in the presence of template (blue) and NTC (red). N = 3 for all conditions, except Bst 3.0 at 0 and 100 HHGE per μl in the presence of template, where N = 6.

    Article Snippet: LAMP reagents IsoAmp I (#B0537S), IsoAmp II (#B0374S), MgSO4 (#B1003S), deoxynucleotide solution (#N0447S), Bovine Serum Albumen (BSA, #B9000S0), Bst 2.0 (8,000 U/ml, #M0537S) and Bst 3.0 (8000 U/ml, #M0374S) were purchased from New England Biolabs (Ipswich, MA, USA).

    Techniques: Amplification

    FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)

    Journal: Nature Communications

    Article Title: Evolution of a General RNA-Cleaving FANA Enzyme

    doi: 10.1038/s41467-018-07611-1

    Figure Lengend Snippet: FANA transcription and reverse transcription in vitro. a Constitutional structures for 2’-deoxyribonucleic acid (DNA) and 2’-fluoroarabino nucleic acid (FANA). b FANA transcription activity for wild-type archaeal DNA polymerases (exo−) from 9°N, DV, Kod, and Tgo (left panel). Samples were analyzed after 15 and 30 min at 55 °C. FANA reverse transcriptase activity of Bst DNA polymerase LF, 2.0, 3.0, and LF* (right panel). LF* denotes wild-type Bst DNA polymerase, large fragment, expressed and purified from E. coli . Samples were analyzed after 30 min at 50 °C. All samples were resolved on denaturing PAGE and visualized using a LI-COR Odyssey CLx. c Fidelity profile observed for FANA replication using Tgo and Bst LF* polymerases. The mutation profile reveals a mutation rate of 8 × 10 -4 and an overall fidelity of ~99.9%. d Catalytic rates observed for FANA synthesis with Tgo (left panel) and reverse transcription with Bst LF* (right panel)

    Article Snippet: We evaluated three commercial versions of Bst DNA polymerase (LF, 2.0, and 3.0 from New England Biolabs), along with a second version of the wild-type LF polymerase (LF*) that was expressed and purified from Escherichia coli .

    Techniques: In Vitro, Activity Assay, Purification, Polyacrylamide Gel Electrophoresis, Mutagenesis