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TaKaRa klenow dna polymerase
Klenow Dna Polymerase, supplied by TaKaRa, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 6 article reviews
Price from $9.99 to $1999.99
klenow dna polymerase - by Bioz Stars, 2020-07
92/100 stars

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Expressing:

Article Title: Endonuclease III and endonuclease VIII conditionally targeted into mitochondria enhance mitochondrial DNA repair and cell survival following oxidative stress
Article Snippet: .. EcoRI fragments containing either MTS–HA–EndoIII–HA or MTS–HA–EndoVIII–HA sequences were filled in with Klenow DNA polymerase and ligated into the PvuII restriction site of the pTRE2hyg expression vector (Clontech). .. The final constructs were sequenced to verify the integrity of the reading frames and fidelity of the sequences.

Plasmid Preparation:

Article Title: Endonuclease III and endonuclease VIII conditionally targeted into mitochondria enhance mitochondrial DNA repair and cell survival following oxidative stress
Article Snippet: .. EcoRI fragments containing either MTS–HA–EndoIII–HA or MTS–HA–EndoVIII–HA sequences were filled in with Klenow DNA polymerase and ligated into the PvuII restriction site of the pTRE2hyg expression vector (Clontech). .. The final constructs were sequenced to verify the integrity of the reading frames and fidelity of the sequences.

Synthesized:

Article Title: An easy operating pathogen microarray (EOPM) platform for rapid screening of vertebrate pathogens
Article Snippet: .. The first strand cDNA was then synthesized to double-stranded DNA using the same primer and Klenow DNA polymerase (Takara, Dalian, China). .. Double stranded cDNA from both patients and normal controls was PCR amplified using the heel primer.

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  • 88
    TaKaRa pyex bx
    Western blot analysis of yeast extracts. Strains W303 <t>pYEX-BX</t> (empty vector), and W303 pYEX-BX 2.1vhs (2.1vhs) were grown to an OD 600 of 2 to 3 in YNBG and then induced with 0.15 mM CuSO 4 for 5 h at 30°C. Whole-cell extracts were prepared, and the <t>vhs</t> protein in the extracts was detected by Western blot analysis using a monoclonal antibody directed against the HA epitope. A lysate of Vero cells infected for 12 h with HSV-1 Pvhs N138-HA (lane Pvhs N138-HA) at an MOI of 10 was included as a positive control.
    Pyex Bx, supplied by TaKaRa, used in various techniques. Bioz Stars score: 88/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pyex bx/product/TaKaRa
    Average 88 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
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    99
    TaKaRa klenow fragment
    The effect of transiently expressed nuclear <t>MxA</t> proteins. ( A ) The effect of nuclear MxA proteins in Swiss3T3 cells. The cells were transfected with pHMP1-vNS-Luc (0.2 µg), pSEAP2-control (0.1 µg), plasmids encoding three RNA polymerase subunits and NP (0.05 µg of each plasmid) and either parental vector, pVP16-MxA or pHMG-TMxA (0.3 µg each). Luciferase activity was determined and shown as described in Materials and Methods. Error bars represent standard deviation (n = 3). ( B ) Dose-dependent effect of wild-type MxA and VP16-MxA. The same procedure for (A) was carried out in the presence of increasing amounts of wild-type MxA or VP16-MxA. Error bars represent standard deviation (n = 3). ( C ) The effect of C-terminal (MxAΔC) and internal (MxAΔM) deletion VP16-MxA mutant proteins on reporter gene expression. The same procedure for (A) was carried out with mutant MxA proteins. To generate a VP16-MxA deletion mutant (MxAΔC) for expression of MxA lacking its C-terminal region (362–662), we amplified a fragment by PCR with specific primers, 5′-GGCATCCATATGGTTGTTTCCGAAGTGGACATCGCA-3′ and 5′-CGCGGATCCTTAACCATACTTTTGTAGCTCCTCTGT-3′ and pVP16-MxA as template. To generate a VP16-MxA deletion mutant (MxAΔM) lacking its internal region (362–573), a fragment was amplified by PCR with primers, 5′-GGCATCCATATGGTTGTTTCCGAAGTGGACATC GCA-3′ and 5′-CGCGGATCCTTAACCGGGGAACTGGGCAAGCCGGCG-3′ and pCHA-MxAΔM plasmid as a template. pCHA-MxAΔM was derived from previously constructed plasmid, pCHA-MxA by removal of an internal part of MxA by digestion with SalI (TOYOBO) and NcoI (TOYOBO) restriction enzymes. The main part of the plasmid was blunted with <t>Klenow</t> fragment and self-ligated. MxA fragments thus prepared were digested with NdeI, blunted with Klenow fragment and then digested with BamHI. These fragments were cloned into pVP16 plasmid digested with EcoRI followed by Klenow treatment and subsequent digestion with BamHI. Error bars represent standard deviation (n = 3).
    Klenow Fragment, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/klenow fragment/product/TaKaRa
    Average 99 stars, based on 44 article reviews
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    95
    TaKaRa dna polymerase i
    Amplification of the ORFV <t>DNA</t> polymerase gene by PCR. Lane M, DNA marker DL-2000; lane 1, DNA <t>polymerase</t> I PCR product (888 bp); lane 2, DNA polymerase II PCR product (1001 bp); lane 3, polymerase III PCR product (1752 bp)
    Dna Polymerase I, supplied by TaKaRa, used in various techniques. Bioz Stars score: 95/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Western blot analysis of yeast extracts. Strains W303 pYEX-BX (empty vector), and W303 pYEX-BX 2.1vhs (2.1vhs) were grown to an OD 600 of 2 to 3 in YNBG and then induced with 0.15 mM CuSO 4 for 5 h at 30°C. Whole-cell extracts were prepared, and the vhs protein in the extracts was detected by Western blot analysis using a monoclonal antibody directed against the HA epitope. A lysate of Vero cells infected for 12 h with HSV-1 Pvhs N138-HA (lane Pvhs N138-HA) at an MOI of 10 was included as a positive control.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus Virion Host Shutoff Protein Requires a Mammalian Factor for Efficient In Vitro Endoribonuclease Activity

    doi: 10.1128/JVI.75.3.1172-1185.2001

    Figure Lengend Snippet: Western blot analysis of yeast extracts. Strains W303 pYEX-BX (empty vector), and W303 pYEX-BX 2.1vhs (2.1vhs) were grown to an OD 600 of 2 to 3 in YNBG and then induced with 0.15 mM CuSO 4 for 5 h at 30°C. Whole-cell extracts were prepared, and the vhs protein in the extracts was detected by Western blot analysis using a monoclonal antibody directed against the HA epitope. A lysate of Vero cells infected for 12 h with HSV-1 Pvhs N138-HA (lane Pvhs N138-HA) at an MOI of 10 was included as a positive control.

    Article Snippet: The Nco I- Hin dIII fragment of pYGAL vhs bearing the vhs ORF and 3′ flanking sequences was cloned between the Bam HI- Sal I sites of pYEX-BX (after making all four ends flush with the Klenow fragment of DNA polymerase I), generating pYEX-BX vhs. pYEX-BX vhs1 was generated in the same way, using the Nco I- Hin dIII fragment of pYGAL vhs1.

    Techniques: Western Blot, Plasmid Preparation, Infection, Positive Control

    Levels of expression of 2.1vhs and 2.1vhs1 proteins. Strains W303 pYEX-BX (empty vector), W303 pYEX-BX 2.1vhs (2.1vhs), and W303 pYEX-BX 2.1vhs1 (2.1vhs1) were grown to saturation in YNBG, and the cultures were then split into two portions. One culture was induced with 0.5 mM CuSO 4 for 5 h at 30°C (lanes I), while the other was left untreated (lanes U). Cell extracts were then analyzed for vhs expression by Western blot analysis using a monoclonal antibody directed against the HA epitope. A lysate of Vero cells infected for 12 h with HSV-1 Pvhs N138-HA (lane Pvhs N138-HA) at a multiplicity of infection (MOI) of 10 was included as a positive control.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus Virion Host Shutoff Protein Requires a Mammalian Factor for Efficient In Vitro Endoribonuclease Activity

    doi: 10.1128/JVI.75.3.1172-1185.2001

    Figure Lengend Snippet: Levels of expression of 2.1vhs and 2.1vhs1 proteins. Strains W303 pYEX-BX (empty vector), W303 pYEX-BX 2.1vhs (2.1vhs), and W303 pYEX-BX 2.1vhs1 (2.1vhs1) were grown to saturation in YNBG, and the cultures were then split into two portions. One culture was induced with 0.5 mM CuSO 4 for 5 h at 30°C (lanes I), while the other was left untreated (lanes U). Cell extracts were then analyzed for vhs expression by Western blot analysis using a monoclonal antibody directed against the HA epitope. A lysate of Vero cells infected for 12 h with HSV-1 Pvhs N138-HA (lane Pvhs N138-HA) at a multiplicity of infection (MOI) of 10 was included as a positive control.

    Article Snippet: The Nco I- Hin dIII fragment of pYGAL vhs bearing the vhs ORF and 3′ flanking sequences was cloned between the Bam HI- Sal I sites of pYEX-BX (after making all four ends flush with the Klenow fragment of DNA polymerase I), generating pYEX-BX vhs. pYEX-BX vhs1 was generated in the same way, using the Nco I- Hin dIII fragment of pYGAL vhs1.

    Techniques: Expressing, Plasmid Preparation, Western Blot, Infection, Positive Control

    Expression of vhs from the inducible CUP1 promoter inhibits colony formation. Strains W303 pYEX-BX (vector), W303 pYEX-BX vhs (vhs), and W303 pYEX-BX vhs1 (vhs1) were grown to saturation in YNBD, and then equal amounts of cells from each strain were spotted and streaked onto YNBD (glucose), YNBG (galactose), YNBR (raffinose), and YNBM (maltose) plates containing (+) or lacking (−) 0.5 mM copper sulfate (Cu). The plates were incubated at 30°C for 5 days.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus Virion Host Shutoff Protein Requires a Mammalian Factor for Efficient In Vitro Endoribonuclease Activity

    doi: 10.1128/JVI.75.3.1172-1185.2001

    Figure Lengend Snippet: Expression of vhs from the inducible CUP1 promoter inhibits colony formation. Strains W303 pYEX-BX (vector), W303 pYEX-BX vhs (vhs), and W303 pYEX-BX vhs1 (vhs1) were grown to saturation in YNBD, and then equal amounts of cells from each strain were spotted and streaked onto YNBD (glucose), YNBG (galactose), YNBR (raffinose), and YNBM (maltose) plates containing (+) or lacking (−) 0.5 mM copper sulfate (Cu). The plates were incubated at 30°C for 5 days.

    Article Snippet: The Nco I- Hin dIII fragment of pYGAL vhs bearing the vhs ORF and 3′ flanking sequences was cloned between the Bam HI- Sal I sites of pYEX-BX (after making all four ends flush with the Klenow fragment of DNA polymerase I), generating pYEX-BX vhs. pYEX-BX vhs1 was generated in the same way, using the Nco I- Hin dIII fragment of pYGAL vhs1.

    Techniques: Expressing, Plasmid Preparation, Incubation

    Carbon source-dependent variation in the vhs-induced phenotype in liquid cultures. Strains W303 pYEX-BX (vector), W303 pYEX-BX vhs (vhs), and W303 pYEX-BX vhs1 (vhs1) growing in YNBD (glucose) were pelleted, washed in water, and resuspended in YNB containing the indicated carbon sources, in the presence or absence of 0.5 mM CuSO 4 . The OD 600 of the cultures was then monitored over time. Closed symbols, not induced; open symbols, induced. Circles, empty vector; squares, vhs expression vector; triangles, vhs1 expression vector.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus Virion Host Shutoff Protein Requires a Mammalian Factor for Efficient In Vitro Endoribonuclease Activity

    doi: 10.1128/JVI.75.3.1172-1185.2001

    Figure Lengend Snippet: Carbon source-dependent variation in the vhs-induced phenotype in liquid cultures. Strains W303 pYEX-BX (vector), W303 pYEX-BX vhs (vhs), and W303 pYEX-BX vhs1 (vhs1) growing in YNBD (glucose) were pelleted, washed in water, and resuspended in YNB containing the indicated carbon sources, in the presence or absence of 0.5 mM CuSO 4 . The OD 600 of the cultures was then monitored over time. Closed symbols, not induced; open symbols, induced. Circles, empty vector; squares, vhs expression vector; triangles, vhs1 expression vector.

    Article Snippet: The Nco I- Hin dIII fragment of pYGAL vhs bearing the vhs ORF and 3′ flanking sequences was cloned between the Bam HI- Sal I sites of pYEX-BX (after making all four ends flush with the Klenow fragment of DNA polymerase I), generating pYEX-BX vhs. pYEX-BX vhs1 was generated in the same way, using the Nco I- Hin dIII fragment of pYGAL vhs1.

    Techniques: Plasmid Preparation, Expressing

    Effect of vhs expression on the in vivo stability of PDA1 mRNA. Strains W303 pYEX-BX (empty vector) and W303 pYEX-BX vhs (vhs) were grown to an OD 600 of 0.6 in YNBD, and a 10-ml aliquot was withdrawn for RNA extraction (solid arrow). The remainder of the culture was induced with the addition of 0.5 mM CuSO 4 for 30 min. Another aliquot was then removed for RNA extraction (open arrow), and transcription was inhibited in the remainder of the culture with 100 μg of phenanthroline per ml. Aliquots were then removed every 30 min over a 3-h time course. Total RNA was analyzed for PDA1 mRNA levels by Northern blot hybridization. Lane 1, RNA extracted just before induction with CuSO 4 ; lane 2, RNA extracted just before addition of phenanthroline; lanes 3, 4, 5, 6, 7, and 8, RNA extracted at 30, 60, 90, 120, 180, and 210 min after addition of phenanthroline, respectively.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus Virion Host Shutoff Protein Requires a Mammalian Factor for Efficient In Vitro Endoribonuclease Activity

    doi: 10.1128/JVI.75.3.1172-1185.2001

    Figure Lengend Snippet: Effect of vhs expression on the in vivo stability of PDA1 mRNA. Strains W303 pYEX-BX (empty vector) and W303 pYEX-BX vhs (vhs) were grown to an OD 600 of 0.6 in YNBD, and a 10-ml aliquot was withdrawn for RNA extraction (solid arrow). The remainder of the culture was induced with the addition of 0.5 mM CuSO 4 for 30 min. Another aliquot was then removed for RNA extraction (open arrow), and transcription was inhibited in the remainder of the culture with 100 μg of phenanthroline per ml. Aliquots were then removed every 30 min over a 3-h time course. Total RNA was analyzed for PDA1 mRNA levels by Northern blot hybridization. Lane 1, RNA extracted just before induction with CuSO 4 ; lane 2, RNA extracted just before addition of phenanthroline; lanes 3, 4, 5, 6, 7, and 8, RNA extracted at 30, 60, 90, 120, 180, and 210 min after addition of phenanthroline, respectively.

    Article Snippet: The Nco I- Hin dIII fragment of pYGAL vhs bearing the vhs ORF and 3′ flanking sequences was cloned between the Bam HI- Sal I sites of pYEX-BX (after making all four ends flush with the Klenow fragment of DNA polymerase I), generating pYEX-BX vhs. pYEX-BX vhs1 was generated in the same way, using the Nco I- Hin dIII fragment of pYGAL vhs1.

    Techniques: Expressing, In Vivo, Plasmid Preparation, RNA Extraction, Northern Blot, Hybridization

    Expression of epitope-tagged vhs inhibits colony formation. Strains W303 pYEX-BX (vector), W303 pYEX-BX 2.1vhs (2.1vhs), and W303 pYEX-BX 2.1vhs1 (2.1vhs1) were grown to saturation in YNBD, and then equal amounts of cells from each strain were spotted and streaked onto YNBD (glucose), YNBG (galactose), YNBR (raffinose), and YNBM (maltose) plates containing (+) or lacking (−) 0.5 mM copper sulfate (Cu). The plates were incubated at 30°C for 5 days.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus Virion Host Shutoff Protein Requires a Mammalian Factor for Efficient In Vitro Endoribonuclease Activity

    doi: 10.1128/JVI.75.3.1172-1185.2001

    Figure Lengend Snippet: Expression of epitope-tagged vhs inhibits colony formation. Strains W303 pYEX-BX (vector), W303 pYEX-BX 2.1vhs (2.1vhs), and W303 pYEX-BX 2.1vhs1 (2.1vhs1) were grown to saturation in YNBD, and then equal amounts of cells from each strain were spotted and streaked onto YNBD (glucose), YNBG (galactose), YNBR (raffinose), and YNBM (maltose) plates containing (+) or lacking (−) 0.5 mM copper sulfate (Cu). The plates were incubated at 30°C for 5 days.

    Article Snippet: The Nco I- Hin dIII fragment of pYGAL vhs bearing the vhs ORF and 3′ flanking sequences was cloned between the Bam HI- Sal I sites of pYEX-BX (after making all four ends flush with the Klenow fragment of DNA polymerase I), generating pYEX-BX vhs. pYEX-BX vhs1 was generated in the same way, using the Nco I- Hin dIII fragment of pYGAL vhs1.

    Techniques: Expressing, Plasmid Preparation, Incubation

    The effect of transiently expressed nuclear MxA proteins. ( A ) The effect of nuclear MxA proteins in Swiss3T3 cells. The cells were transfected with pHMP1-vNS-Luc (0.2 µg), pSEAP2-control (0.1 µg), plasmids encoding three RNA polymerase subunits and NP (0.05 µg of each plasmid) and either parental vector, pVP16-MxA or pHMG-TMxA (0.3 µg each). Luciferase activity was determined and shown as described in Materials and Methods. Error bars represent standard deviation (n = 3). ( B ) Dose-dependent effect of wild-type MxA and VP16-MxA. The same procedure for (A) was carried out in the presence of increasing amounts of wild-type MxA or VP16-MxA. Error bars represent standard deviation (n = 3). ( C ) The effect of C-terminal (MxAΔC) and internal (MxAΔM) deletion VP16-MxA mutant proteins on reporter gene expression. The same procedure for (A) was carried out with mutant MxA proteins. To generate a VP16-MxA deletion mutant (MxAΔC) for expression of MxA lacking its C-terminal region (362–662), we amplified a fragment by PCR with specific primers, 5′-GGCATCCATATGGTTGTTTCCGAAGTGGACATCGCA-3′ and 5′-CGCGGATCCTTAACCATACTTTTGTAGCTCCTCTGT-3′ and pVP16-MxA as template. To generate a VP16-MxA deletion mutant (MxAΔM) lacking its internal region (362–573), a fragment was amplified by PCR with primers, 5′-GGCATCCATATGGTTGTTTCCGAAGTGGACATC GCA-3′ and 5′-CGCGGATCCTTAACCGGGGAACTGGGCAAGCCGGCG-3′ and pCHA-MxAΔM plasmid as a template. pCHA-MxAΔM was derived from previously constructed plasmid, pCHA-MxA by removal of an internal part of MxA by digestion with SalI (TOYOBO) and NcoI (TOYOBO) restriction enzymes. The main part of the plasmid was blunted with Klenow fragment and self-ligated. MxA fragments thus prepared were digested with NdeI, blunted with Klenow fragment and then digested with BamHI. These fragments were cloned into pVP16 plasmid digested with EcoRI followed by Klenow treatment and subsequent digestion with BamHI. Error bars represent standard deviation (n = 3).

    Journal: Nucleic Acids Research

    Article Title: Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome

    doi: 10.1093/nar/gkh192

    Figure Lengend Snippet: The effect of transiently expressed nuclear MxA proteins. ( A ) The effect of nuclear MxA proteins in Swiss3T3 cells. The cells were transfected with pHMP1-vNS-Luc (0.2 µg), pSEAP2-control (0.1 µg), plasmids encoding three RNA polymerase subunits and NP (0.05 µg of each plasmid) and either parental vector, pVP16-MxA or pHMG-TMxA (0.3 µg each). Luciferase activity was determined and shown as described in Materials and Methods. Error bars represent standard deviation (n = 3). ( B ) Dose-dependent effect of wild-type MxA and VP16-MxA. The same procedure for (A) was carried out in the presence of increasing amounts of wild-type MxA or VP16-MxA. Error bars represent standard deviation (n = 3). ( C ) The effect of C-terminal (MxAΔC) and internal (MxAΔM) deletion VP16-MxA mutant proteins on reporter gene expression. The same procedure for (A) was carried out with mutant MxA proteins. To generate a VP16-MxA deletion mutant (MxAΔC) for expression of MxA lacking its C-terminal region (362–662), we amplified a fragment by PCR with specific primers, 5′-GGCATCCATATGGTTGTTTCCGAAGTGGACATCGCA-3′ and 5′-CGCGGATCCTTAACCATACTTTTGTAGCTCCTCTGT-3′ and pVP16-MxA as template. To generate a VP16-MxA deletion mutant (MxAΔM) lacking its internal region (362–573), a fragment was amplified by PCR with primers, 5′-GGCATCCATATGGTTGTTTCCGAAGTGGACATC GCA-3′ and 5′-CGCGGATCCTTAACCGGGGAACTGGGCAAGCCGGCG-3′ and pCHA-MxAΔM plasmid as a template. pCHA-MxAΔM was derived from previously constructed plasmid, pCHA-MxA by removal of an internal part of MxA by digestion with SalI (TOYOBO) and NcoI (TOYOBO) restriction enzymes. The main part of the plasmid was blunted with Klenow fragment and self-ligated. MxA fragments thus prepared were digested with NdeI, blunted with Klenow fragment and then digested with BamHI. These fragments were cloned into pVP16 plasmid digested with EcoRI followed by Klenow treatment and subsequent digestion with BamHI. Error bars represent standard deviation (n = 3).

    Article Snippet: A fragment containing MxA gene was prepared from pET14b-MxA by digestion with NdeI followed by treatment with Klenow fragment and digestion with BamHI.

    Techniques: Transfection, Plasmid Preparation, Luciferase, Activity Assay, Standard Deviation, Mutagenesis, Expressing, Amplification, Polymerase Chain Reaction, Derivative Assay, Construct, Clone Assay

    Amplification of the ORFV DNA polymerase gene by PCR. Lane M, DNA marker DL-2000; lane 1, DNA polymerase I PCR product (888 bp); lane 2, DNA polymerase II PCR product (1001 bp); lane 3, polymerase III PCR product (1752 bp)

    Journal: Archives of Virology

    Article Title: In vitro RNA interference targeting the DNA polymerase gene inhibits orf virus replication in primary ovine fetal turbinate cells

    doi: 10.1007/s00705-013-1896-z

    Figure Lengend Snippet: Amplification of the ORFV DNA polymerase gene by PCR. Lane M, DNA marker DL-2000; lane 1, DNA polymerase I PCR product (888 bp); lane 2, DNA polymerase II PCR product (1001 bp); lane 3, polymerase III PCR product (1752 bp)

    Article Snippet: Cloning and DNA sequencing The PCR products of the DNA polymerase I, II, and III fragments were cloned into the pMD-18T vector (Takara, Dalian, China) and used to transform E. coli DH5a.

    Techniques: Amplification, Polymerase Chain Reaction, Marker