klenow fragment  (New England Biolabs)


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    Name:
    DNA Polymerase I Klenow Fragment
    Description:
    DNA Polymerase I Klenow Fragment 1 000 units
    Catalog Number:
    M0210L
    Price:
    248
    Category:
    DNA Polymerases
    Size:
    1 000 units
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    Structured Review

    New England Biolabs klenow fragment
    DNA Polymerase I Klenow Fragment
    DNA Polymerase I Klenow Fragment 1 000 units
    https://www.bioz.com/result/klenow fragment/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    klenow fragment - by Bioz Stars, 2021-04
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    Images

    1) Product Images from "5?CAG and 5?CTG Repeats Create Differential Impediment to the Progression of a Minimal Reconstituted T4 Replisome Depending on the Concentration of dNTPs"

    Article Title: 5?CAG and 5?CTG Repeats Create Differential Impediment to the Progression of a Minimal Reconstituted T4 Replisome Depending on the Concentration of dNTPs

    Journal: Molecular Biology International

    doi: 10.4061/2011/213824

    DNA synthesis activity of minimal reconstituted T4 replisomes across a minifork containing a random sequence. The minifork was prepared with the plasmid p-Empty and thus contains a random sequence to be replicated. gp43, gp41, and gp59 are the DNA polymerase, the helicase and the helicase loader of bacteriophage T4, respectively. (A) Gp43 was incubated with the minifork, alone (lane 2), with gp41 (lanes 3–8) or with gp41 and gp59 (lanes 9–15). The reaction was quenched at various times and the samples were loaded on a denaturing sequencing gel. (a) corresponds to the radiolabelled p821 primer. (b) corresponds to radiolabelled p821 extended by 15 nts up to the base of the 5′ ss tail of the lagging strand template. (c) corresponds to the radiolabelled p821 extended up to the end of the leading strand template after strand displacement DNA synthesis. The (a), (b), and (c) DNAs are also shown in the context of the minifork on the right side of the figure. Major transient intermediate products are indicated by backward arrows. The four sequencing reactions (A, T, C, and G) of the leading strand template of the minifork are shown on the left side of the figure. (B) The minifork was incubated with Klenow fragment alone (lanes 2 and 5), together with gp41 (lanes 3 and 6) or with gp41 and gp59 (lanes 4 and 7) for 20 minutes. The reaction products were resolved on a denaturing sequencing gel. Two amounts of Klenow fragment were tested (1 mU/ μ L, lanes 2–4; 10 mU/ μ L, lanes 5–7). (a) and (c) are as in 3A.
    Figure Legend Snippet: DNA synthesis activity of minimal reconstituted T4 replisomes across a minifork containing a random sequence. The minifork was prepared with the plasmid p-Empty and thus contains a random sequence to be replicated. gp43, gp41, and gp59 are the DNA polymerase, the helicase and the helicase loader of bacteriophage T4, respectively. (A) Gp43 was incubated with the minifork, alone (lane 2), with gp41 (lanes 3–8) or with gp41 and gp59 (lanes 9–15). The reaction was quenched at various times and the samples were loaded on a denaturing sequencing gel. (a) corresponds to the radiolabelled p821 primer. (b) corresponds to radiolabelled p821 extended by 15 nts up to the base of the 5′ ss tail of the lagging strand template. (c) corresponds to the radiolabelled p821 extended up to the end of the leading strand template after strand displacement DNA synthesis. The (a), (b), and (c) DNAs are also shown in the context of the minifork on the right side of the figure. Major transient intermediate products are indicated by backward arrows. The four sequencing reactions (A, T, C, and G) of the leading strand template of the minifork are shown on the left side of the figure. (B) The minifork was incubated with Klenow fragment alone (lanes 2 and 5), together with gp41 (lanes 3 and 6) or with gp41 and gp59 (lanes 4 and 7) for 20 minutes. The reaction products were resolved on a denaturing sequencing gel. Two amounts of Klenow fragment were tested (1 mU/ μ L, lanes 2–4; 10 mU/ μ L, lanes 5–7). (a) and (c) are as in 3A.

    Techniques Used: DNA Synthesis, Activity Assay, Sequencing, Plasmid Preparation, Incubation

    2) Product Images from "Protein Displacement by Herpes Helicase-Primase and the Key Role of UL42 During Helicase-Coupled DNA Synthesis by the Herpes Polymerase"

    Article Title: Protein Displacement by Herpes Helicase-Primase and the Key Role of UL42 During Helicase-Coupled DNA Synthesis by the Herpes Polymerase

    Journal: Biochemistry

    doi: 10.1021/acs.biochem.6b01128

    UL30 inhibits the minicircle replication in the absence of UL42 Reactions contained helicase, polymerase(s), DNA MC70-2 (A) and were quenched after 30 minutes. (B) Lanes 1–6 contained 100 nM Klenow Fragment and increasing concentrations of UL30 (0, 10, 50, 100, 150 or 200 nM). Lanes 7–12 contained 100 nM UL30 and increasing concentrations of Klenow Fragment (0, 10, 50, 100, 150 or 200 nM). DNA products were separated using 1.5% alkaline agarose gel electrophoresis. (C) Amount of dNTPs incorporated was measured using ImageQuant.
    Figure Legend Snippet: UL30 inhibits the minicircle replication in the absence of UL42 Reactions contained helicase, polymerase(s), DNA MC70-2 (A) and were quenched after 30 minutes. (B) Lanes 1–6 contained 100 nM Klenow Fragment and increasing concentrations of UL30 (0, 10, 50, 100, 150 or 200 nM). Lanes 7–12 contained 100 nM UL30 and increasing concentrations of Klenow Fragment (0, 10, 50, 100, 150 or 200 nM). DNA products were separated using 1.5% alkaline agarose gel electrophoresis. (C) Amount of dNTPs incorporated was measured using ImageQuant.

    Techniques Used: Agarose Gel Electrophoresis

    Non-cognate polymerases can replace UL30-UL42 during minicircle replication Either Klenow Fragment or T4 DNA Polymerase were titrated into assays containing DNA MC70 (A) and 100 nM UL5-UL8-UL52. (B) DNA products were separated with 1.5% alkaline agarose gel electrophoresis.
    Figure Legend Snippet: Non-cognate polymerases can replace UL30-UL42 during minicircle replication Either Klenow Fragment or T4 DNA Polymerase were titrated into assays containing DNA MC70 (A) and 100 nM UL5-UL8-UL52. (B) DNA products were separated with 1.5% alkaline agarose gel electrophoresis.

    Techniques Used: Agarose Gel Electrophoresis

    Related Articles

    Ethanol Precipitation:

    Article Title: A shotgun antisense approach to the identification of novel essential genes in Pseudomonas aeruginosa
    Article Snippet: .. Following ethanol precipitation, fragmented DNA was treated with nuclease BAL-31 and Klenow (New England Biolabs) for 10 min at 30°C to obtain blunt ends. .. After enzyme inactivation with 1 mM EDTA, DNA was dialyzed against 20 mM Tris–HCl (pH 8.0). pVI533EH and pHERD20T were digested with Sma I (New England Biolabs) and dephosphorylated using shrimp alkaline phosphatase (Roche).

    Staining:

    Article Title: Effects of Vinylphosphonate Internucleotide Linkages on the Cleavage Specificity of Exonuclease III and on the Activity of DNA Polymerase I †
    Article Snippet: The purity of the commercially available enzymes, exonuclease III, mung bean nuclease, DNA pol I, and Klenow, was assessed by SDS–PAGE (data not shown). .. Exonuclease III enzymes from Hybaid-AGS, New England Biolabs, and Amersham Pharmacia Biotech as well as Klenow and DNA polymerase I from New England Biolabs appeared to be very pure, as only single bands corresponding to approximately 28 kDa for exonuclease III, 68 kDa for Klenow, and 103 kDa for DNA polymerase I were visible after Coomassie blue staining. .. No protein bands could be detected for mung bean nuclease enzymes obtained from New England Biolabs and Amersham Pharmacia Biotech, presumably because the concentrations were very low and could not be detected by SDS–PAGE.

    Modification:

    Article Title: Hot Start PCR with heat-activatable primers: a novel approach for improved PCR performance
    Article Snippet: .. Primer extension with Klenow fragment of DNA polymerase Primer extension experiments using large fragment (Klenow) of DNA polymerase I (New England Biolabs) were performed at 25°C using the HIV-1 tat reverse primer (5′-AATACTATGGTCCACACAACTATTGCT-3′) that was unmodified or contained a single OXP modification. ..

    DNA Synthesis:

    Article Title: 5?CAG and 5?CTG Repeats Create Differential Impediment to the Progression of a Minimal Reconstituted T4 Replisome Depending on the Concentration of dNTPs
    Article Snippet: In addition, in the presence of gp43, gp41, and gp59, three intermediate DNA synthesis products (indicated by a backward arrow in ) near the end of the parental DNA duplex transiently accumulated to a significant extent; they might correspond to pause sites for the minimal reconstituted replisome from where DNA synthesis successfully resumed. .. Similarly, the DNA synthesis pattern was examined in the presence of Klenow fragment. .. Klenow fragment has weak strand displacement DNA synthesis activity that allowed it to synthesize through the duplex part of the minifork ( , lanes 2 and 5).

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    New England Biolabs t7 endonuclease i
    Deletion of MCM10 through CRISPR/Cas9 technology. Notes:  ( A ) Validation of CRISPR/Cas9-mediated knockout efficiency using a mCherry/GFP reporter construct. EC109 cells were transfected with the Cas9, sgRNAs, and reporter constructs, and mCherry/GFP fluorescence was examined 48 h after transfection. (a) Bright field image of cells. (b) Some cells displayed GFP fluorescence, indicating the presence of CRISPR/Cas9-mediated removal of target sequence. (c) EC109 cells that were transfected with reporter construct showed mCherry fluorescence. (d) Merged image of green and red fluorescence yielded yellow fluorescence. Scale bar = 100 µm. ( B ) T7 endonuclease assay. Different clones derived from EC109 cells transfected with Cas9 and sgRNAs were subjected to PCR amplification of genomic DNA containing sgRNA-1 target site. The size of T7 endonuclease I-digested DNA fragments is indicated on the right. Control, negative control. ( C ) Upper; RT-PCR analysis of MCM10 mRNA expression in different EC109 sublines. Lower; Western blot analysis of MCM10 protein levels. ( D ) Depletion of MCM10 hampers the migration of ESCC cells. In vitro wound-healing assay was performed to assess cell migration capacity. Top; one representative experiment. The percentage of wound closure was determined from three independent experiments. * P
    T7 Endonuclease I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs dna library
    Reverse-genetics system for epidemic strain of ZIKV. (A) Maximum-likelihood phylogenetic tree with bootstrap values for the Paraiba_01/2015 strain (highlighted with a black box) and 60 representative ZIKV isolates. Color coding emphasizes the geographic origins of the strains. ZIKV strains associated with human microcephaly cases (Natal RGN, ZKV2015, and BeH823339) are highlighted with red stars. Strain FSS13025 is highlighted with a blue star. (B) Schematic map of ZIKV- ICD plasmid <t>DNA.</t> NCR, noncoding region; RBZ, antigenomic ribozyme of HDV; TERM, poly(A) <t>signal/RNA-</t> polII terminator. (C) Growth kinetics of ZIKV- ICD and ZIKV- 1 after plasmid DNA transfection into Vero cells. The dashed line indicates the limit of virus detection (0.7 log 10 PFU/ml). (D) Plaque morphology of ZIKV- ICD and ZIKV- 1 in Vero cells at 4 days postinfection (dpi).
    Dna Library, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Deletion of MCM10 through CRISPR/Cas9 technology. Notes:  ( A ) Validation of CRISPR/Cas9-mediated knockout efficiency using a mCherry/GFP reporter construct. EC109 cells were transfected with the Cas9, sgRNAs, and reporter constructs, and mCherry/GFP fluorescence was examined 48 h after transfection. (a) Bright field image of cells. (b) Some cells displayed GFP fluorescence, indicating the presence of CRISPR/Cas9-mediated removal of target sequence. (c) EC109 cells that were transfected with reporter construct showed mCherry fluorescence. (d) Merged image of green and red fluorescence yielded yellow fluorescence. Scale bar = 100 µm. ( B ) T7 endonuclease assay. Different clones derived from EC109 cells transfected with Cas9 and sgRNAs were subjected to PCR amplification of genomic DNA containing sgRNA-1 target site. The size of T7 endonuclease I-digested DNA fragments is indicated on the right. Control, negative control. ( C ) Upper; RT-PCR analysis of MCM10 mRNA expression in different EC109 sublines. Lower; Western blot analysis of MCM10 protein levels. ( D ) Depletion of MCM10 hampers the migration of ESCC cells. In vitro wound-healing assay was performed to assess cell migration capacity. Top; one representative experiment. The percentage of wound closure was determined from three independent experiments. * P

    Journal: OncoTargets and therapy

    Article Title: Ablation of MCM10 using CRISPR/Cas9 restrains the growth and migration of esophageal squamous cell carcinoma cells through inhibition of Akt signaling

    doi: 10.2147/OTT.S157025

    Figure Lengend Snippet: Deletion of MCM10 through CRISPR/Cas9 technology. Notes: ( A ) Validation of CRISPR/Cas9-mediated knockout efficiency using a mCherry/GFP reporter construct. EC109 cells were transfected with the Cas9, sgRNAs, and reporter constructs, and mCherry/GFP fluorescence was examined 48 h after transfection. (a) Bright field image of cells. (b) Some cells displayed GFP fluorescence, indicating the presence of CRISPR/Cas9-mediated removal of target sequence. (c) EC109 cells that were transfected with reporter construct showed mCherry fluorescence. (d) Merged image of green and red fluorescence yielded yellow fluorescence. Scale bar = 100 µm. ( B ) T7 endonuclease assay. Different clones derived from EC109 cells transfected with Cas9 and sgRNAs were subjected to PCR amplification of genomic DNA containing sgRNA-1 target site. The size of T7 endonuclease I-digested DNA fragments is indicated on the right. Control, negative control. ( C ) Upper; RT-PCR analysis of MCM10 mRNA expression in different EC109 sublines. Lower; Western blot analysis of MCM10 protein levels. ( D ) Depletion of MCM10 hampers the migration of ESCC cells. In vitro wound-healing assay was performed to assess cell migration capacity. Top; one representative experiment. The percentage of wound closure was determined from three independent experiments. * P

    Article Snippet: After treatment with T7 endonuclease I (New England Biolabs, Ipswich, MA, USA) at 37°C for 2 h, the resulting fragments were subjected to 1% agarose gel electrophoresis and stained with ethidium bromide.

    Techniques: CRISPR, Knock-Out, Construct, Transfection, Fluorescence, Sequencing, Clone Assay, Derivative Assay, Polymerase Chain Reaction, Amplification, Negative Control, Reverse Transcription Polymerase Chain Reaction, Expressing, Western Blot, Migration, In Vitro, Wound Healing Assay

    Reverse-genetics system for epidemic strain of ZIKV. (A) Maximum-likelihood phylogenetic tree with bootstrap values for the Paraiba_01/2015 strain (highlighted with a black box) and 60 representative ZIKV isolates. Color coding emphasizes the geographic origins of the strains. ZIKV strains associated with human microcephaly cases (Natal RGN, ZKV2015, and BeH823339) are highlighted with red stars. Strain FSS13025 is highlighted with a blue star. (B) Schematic map of ZIKV- ICD plasmid DNA. NCR, noncoding region; RBZ, antigenomic ribozyme of HDV; TERM, poly(A) signal/RNA- polII terminator. (C) Growth kinetics of ZIKV- ICD and ZIKV- 1 after plasmid DNA transfection into Vero cells. The dashed line indicates the limit of virus detection (0.7 log 10 PFU/ml). (D) Plaque morphology of ZIKV- ICD and ZIKV- 1 in Vero cells at 4 days postinfection (dpi).

    Journal: mBio

    Article Title: A Full-Length Infectious cDNA Clone of Zika Virus from the 2015 Epidemic in Brazil as a Genetic Platform for Studies of Virus-Host Interactions and Vaccine Development

    doi: 10.1128/mBio.01114-16

    Figure Lengend Snippet: Reverse-genetics system for epidemic strain of ZIKV. (A) Maximum-likelihood phylogenetic tree with bootstrap values for the Paraiba_01/2015 strain (highlighted with a black box) and 60 representative ZIKV isolates. Color coding emphasizes the geographic origins of the strains. ZIKV strains associated with human microcephaly cases (Natal RGN, ZKV2015, and BeH823339) are highlighted with red stars. Strain FSS13025 is highlighted with a blue star. (B) Schematic map of ZIKV- ICD plasmid DNA. NCR, noncoding region; RBZ, antigenomic ribozyme of HDV; TERM, poly(A) signal/RNA- polII terminator. (C) Growth kinetics of ZIKV- ICD and ZIKV- 1 after plasmid DNA transfection into Vero cells. The dashed line indicates the limit of virus detection (0.7 log 10 PFU/ml). (D) Plaque morphology of ZIKV- ICD and ZIKV- 1 in Vero cells at 4 days postinfection (dpi).

    Article Snippet: To prepare the DNA library from the RNA fragments, the NEBNext mRNA library prep master mix set for Illumina (New England Biolabs) was used according to the manufacturer’s protocol.

    Techniques: Plasmid Preparation, Transfection

    PFGE and hybridization analysis of I-CeuI and MluI double-digested DNA of the bacitracin resistant C. perfringens strain c1261_A. PFGE analysis of C. perfringens strain c1261_A total DNA (A). Southern blot of C. perfringens isolate c1261_A total DNA probed with rrn (B) and with bcrB (C). Sizes (in kilobases) are indicated on the left.

    Journal: PLoS ONE

    Article Title: Characterization of Genes Encoding for Acquired Bacitracin Resistance in Clostridium perfringens

    doi: 10.1371/journal.pone.0044449

    Figure Lengend Snippet: PFGE and hybridization analysis of I-CeuI and MluI double-digested DNA of the bacitracin resistant C. perfringens strain c1261_A. PFGE analysis of C. perfringens strain c1261_A total DNA (A). Southern blot of C. perfringens isolate c1261_A total DNA probed with rrn (B) and with bcrB (C). Sizes (in kilobases) are indicated on the left.

    Article Snippet: DNA plugs were double-digested with 40 U of I-CeuI (New England Biolabs) and 80 U of MluI (New England Biolabs) for 1 h at 37°C.

    Techniques: Hybridization, Southern Blot

    Phylogenetic tree showing the evolutionary relationship between Ts K1 DNA polymerase and other Thermus DNA polymerases based on maximum likelihood analysis. The tree with the highest likelihood (7699.30) is shown, and the bootstrap value (1000 replicates) for each clade is shown next to each branch. The final dataset contained 824 positions. All positions containing gaps or missing data were eliminated (complete deletion option). Bar indicates 0.05 substitutions per amino acid position. Evolutionary analyses were conducted using MEGA X

    Journal: MicrobiologyOpen

    Article Title: Characteristics of DNA polymerase I from an extreme thermophile, Thermus scotoductus strain K1

    doi: 10.1002/mbo3.1149

    Figure Lengend Snippet: Phylogenetic tree showing the evolutionary relationship between Ts K1 DNA polymerase and other Thermus DNA polymerases based on maximum likelihood analysis. The tree with the highest likelihood (7699.30) is shown, and the bootstrap value (1000 replicates) for each clade is shown next to each branch. The final dataset contained 824 positions. All positions containing gaps or missing data were eliminated (complete deletion option). Bar indicates 0.05 substitutions per amino acid position. Evolutionary analyses were conducted using MEGA X

    Article Snippet: 3.5 PCR by Ts K1 DNA polymerase The electrophoretogram of the PCR products amplified by using the Ts K1 DNA polymerase is shown in Figure .

    Techniques:

    Properties of Ts K1 DNA polymerase. (a) Effect of temperature on Ts K1 DNA polymerase activity; (b) effect of pH on Ts K1 DNA polymerase activity in MOPS‐NaOH (■), Tris‐HCl (▲), and glycine‐NaOH (●) buffers; (c) effect of KCl concentration on Ts K1 DNA polymerase activity; and (d) effect of the divalent cations Mg 2+ (■) and Mn 2+ (●) on Ts K1 DNA polymerase activity. Each point represents the average of 3 measured values, and error bars represent the standard deviation between these 3 values

    Journal: MicrobiologyOpen

    Article Title: Characteristics of DNA polymerase I from an extreme thermophile, Thermus scotoductus strain K1

    doi: 10.1002/mbo3.1149

    Figure Lengend Snippet: Properties of Ts K1 DNA polymerase. (a) Effect of temperature on Ts K1 DNA polymerase activity; (b) effect of pH on Ts K1 DNA polymerase activity in MOPS‐NaOH (■), Tris‐HCl (▲), and glycine‐NaOH (●) buffers; (c) effect of KCl concentration on Ts K1 DNA polymerase activity; and (d) effect of the divalent cations Mg 2+ (■) and Mn 2+ (●) on Ts K1 DNA polymerase activity. Each point represents the average of 3 measured values, and error bars represent the standard deviation between these 3 values

    Article Snippet: 3.5 PCR by Ts K1 DNA polymerase The electrophoretogram of the PCR products amplified by using the Ts K1 DNA polymerase is shown in Figure .

    Techniques: Activity Assay, Concentration Assay, Standard Deviation

    Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of Ts K1 DNA polymerase purification: (1) noninduced culture, (2) induced culture, (3) sonicated extract from host cells, (4) supernatant after heat treatment, 5) purified protein, M1—Full Range Rainbow molecular‐mass marker (Amersham)

    Journal: MicrobiologyOpen

    Article Title: Characteristics of DNA polymerase I from an extreme thermophile, Thermus scotoductus strain K1

    doi: 10.1002/mbo3.1149

    Figure Lengend Snippet: Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of Ts K1 DNA polymerase purification: (1) noninduced culture, (2) induced culture, (3) sonicated extract from host cells, (4) supernatant after heat treatment, 5) purified protein, M1—Full Range Rainbow molecular‐mass marker (Amersham)

    Article Snippet: 3.5 PCR by Ts K1 DNA polymerase The electrophoretogram of the PCR products amplified by using the Ts K1 DNA polymerase is shown in Figure .

    Techniques: Polyacrylamide Gel Electrophoresis, Purification, Sonication, Marker

    Polymerase chain reaction products amplified using Ts K1 DNA polymerase. Lane 1, 265 bp; lane 2, 500 bp; lane 3, 1500 bp; lane 4, 1920 bp; lane 5, 2.5 kb; M, GeneRuler 1 kb Plus DNA ladder (New England BioLabs)

    Journal: MicrobiologyOpen

    Article Title: Characteristics of DNA polymerase I from an extreme thermophile, Thermus scotoductus strain K1

    doi: 10.1002/mbo3.1149

    Figure Lengend Snippet: Polymerase chain reaction products amplified using Ts K1 DNA polymerase. Lane 1, 265 bp; lane 2, 500 bp; lane 3, 1500 bp; lane 4, 1920 bp; lane 5, 2.5 kb; M, GeneRuler 1 kb Plus DNA ladder (New England BioLabs)

    Article Snippet: 3.5 PCR by Ts K1 DNA polymerase The electrophoretogram of the PCR products amplified by using the Ts K1 DNA polymerase is shown in Figure .

    Techniques: Polymerase Chain Reaction, Amplification

    Ts K1 DNA polymerase thermostability. ×Represents 75°C, ▲ represents 80°C, ● represents 88°C, ♦ represents 95°C. Data are represented on a logarithmic scale. Each point represents the average of 3 measured values, and error bars represent the standard deviation between these 3 values

    Journal: MicrobiologyOpen

    Article Title: Characteristics of DNA polymerase I from an extreme thermophile, Thermus scotoductus strain K1

    doi: 10.1002/mbo3.1149

    Figure Lengend Snippet: Ts K1 DNA polymerase thermostability. ×Represents 75°C, ▲ represents 80°C, ● represents 88°C, ♦ represents 95°C. Data are represented on a logarithmic scale. Each point represents the average of 3 measured values, and error bars represent the standard deviation between these 3 values

    Article Snippet: 3.5 PCR by Ts K1 DNA polymerase The electrophoretogram of the PCR products amplified by using the Ts K1 DNA polymerase is shown in Figure .

    Techniques: Standard Deviation