dntps Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Thermo Fisher dntp
    Dntp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 30875 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Thermo Fisher
    Average 90 stars, based on 30875 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    90
    TaKaRa dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by TaKaRa, used in various techniques. Bioz Stars score: 90/100, based on 9852 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/TaKaRa
    Average 90 stars, based on 9852 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    90
    Bio-Rad dntp mix
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp Mix, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 219 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp mix/product/Bio-Rad
    Average 90 stars, based on 219 article reviews
    Price from $9.99 to $1999.99
    dntp mix - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    93
    5 PRIME dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by 5 PRIME, used in various techniques. Bioz Stars score: 93/100, based on 366 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/5 PRIME
    Average 93 stars, based on 366 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    93/100 stars
      Buy from Supplier

    95
    Amresco dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Amresco, used in various techniques. Bioz Stars score: 95/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Amresco
    Average 95 stars, based on 52 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    95
    Applichem dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by Applichem, used in various techniques. Bioz Stars score: 95/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Applichem
    Average 95 stars, based on 59 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    96
    Bangalore Genei dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by Bangalore Genei, used in various techniques. Bioz Stars score: 96/100, based on 446 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Bangalore Genei
    Average 96 stars, based on 446 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    96/100 stars
      Buy from Supplier

    93
    Bio Basic Canada dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Bio Basic Canada, used in various techniques. Bioz Stars score: 93/100, based on 111 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Bio Basic Canada
    Average 93 stars, based on 111 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    93/100 stars
      Buy from Supplier

    91
    Bioneer Corporation dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by Bioneer Corporation, used in various techniques. Bioz Stars score: 91/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Bioneer Corporation
    Average 91 stars, based on 128 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    95
    Biozym dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by Biozym, used in various techniques. Bioz Stars score: 95/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Biozym
    Average 95 stars, based on 46 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    92
    Boehringer Mannheim dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 756 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Boehringer Mannheim
    Average 92 stars, based on 756 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    92/100 stars
      Buy from Supplier

    95
    Enzymatics dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by Enzymatics, used in various techniques. Bioz Stars score: 95/100, based on 105 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Enzymatics
    Average 95 stars, based on 105 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    91
    Epicentre Biotechnologies dntps
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntps, supplied by Epicentre Biotechnologies, used in various techniques. Bioz Stars score: 91/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Epicentre Biotechnologies
    Average 91 stars, based on 46 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    95
    Eppendorf AG dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 95/100, based on 502 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Eppendorf AG
    Average 95 stars, based on 502 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    91
    Eurobio dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Eurobio, used in various techniques. Bioz Stars score: 91/100, based on 168 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Eurobio
    Average 91 stars, based on 168 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    91
    Euromedex dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Euromedex, used in various techniques. Bioz Stars score: 91/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Euromedex
    Average 91 stars, based on 37 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    dntp  (Feldan)
    91
    Feldan dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Feldan, used in various techniques. Bioz Stars score: 91/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Feldan
    Average 91 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    93
    Fisher Scientific dntp
    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of <t>dNTPs.</t> ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM <t>NaCl,</t> 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.
    Dntp, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 163 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Fisher Scientific
    Average 93 stars, based on 163 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    93/100 stars
      Buy from Supplier

    94
    GE Healthcare dntp
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntp, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 1823 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/GE Healthcare
    Average 94 stars, based on 1823 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    94/100 stars
      Buy from Supplier

    91
    GenBiotech dntp
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntp, supplied by GenBiotech, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/GenBiotech
    Average 91 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    94
    Genecraft dntp
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntp, supplied by Genecraft, used in various techniques. Bioz Stars score: 94/100, based on 153 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Genecraft
    Average 94 stars, based on 153 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    94/100 stars
      Buy from Supplier

    93
    GenScript dntps
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntps, supplied by GenScript, used in various techniques. Bioz Stars score: 93/100, based on 157 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/GenScript
    Average 93 stars, based on 157 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    93/100 stars
      Buy from Supplier

    dntp  (HyTest)
    91
    HyTest dntp
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntp, supplied by HyTest, used in various techniques. Bioz Stars score: 91/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/HyTest
    Average 91 stars, based on 46 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    91/100 stars
      Buy from Supplier

    95
    iNtRON Biotechnology dntp
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntp, supplied by iNtRON Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 173 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/iNtRON Biotechnology
    Average 95 stars, based on 173 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    95
    Kaneka Corp dntp
    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate <t>ATP/ATPγS</t> in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of <t>dNTPs</t> (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004
    Dntp, supplied by Kaneka Corp, used in various techniques. Bioz Stars score: 95/100, based on 387 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Kaneka Corp
    Average 95 stars, based on 387 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    95
    Kapa Biosystems dntp
    Pathogenic Homozygous Recessive Variants in MCM9 Were Identified in Two Consanguineous Kurdish Families from Turkey (A and B) The MCM9 genotype is provided below each individual. WT denotes the wild-type allele. MT (for mutation) indicates either (A) MCM9 c.1732+2T > C or (B) MCM9 c. 394C > T. PCR amplification was completed with the <t>KAPA</t> HiFi HotStart PCR Kit with <t>dNTPs</t> (Kapa Biosystems) according to the manufacturer’s instructions (primers for A are 5′-TCTAGGAGGTCCCGAGATGG-3′ and 5′-CAAAGGCAGAGTGATTGCCG-3′; primers for B are 5′-GCCTGAGAGGCAAGTGAATTTAG-3′ and 5′-TACCTAAAACCAAGGATGTGGGA-3′). PCR products were sequenced at Beckman Coulter Genomics. Results were analyzed with Sequencher (Gene Codes Corporation). Sample chromatograms are shown (5′ to 3′ direction in A; 3′ to 5′ direction in B). Arrows point to the nucleotide peak of interest. Samples utilized for whole-exome sequencing (WES) are indicated by an asterisk. (C) MCM9 is encoded on chr6: 119,252,903–119,134,612 (UCSC Genome Browser hg19). The MCM9 c.1732+2T > C splice variant lies in the splice donor site of exon 9 (red arrow). The c.394C > T mutation lies near the 5′ end of exon 2 (blue arrow). Exons are indicated as full boxes (black). Alternative splice forms of MCM9 either include or exclude exon 11 (white). Introns are indicated as lines. (D) MCM9 consists of an N-terminal DNA binding domain and AAA + core domain. The c.1732+2T > C mutation is predicted to disrupt normal splicing after amino acid 577. The c.394C > T mutation causes insertion of a stop codon in the place of an arginine at position 132 (p.Arg132 ∗ ). This most likely results in a truncated protein if one is formed. The yellow box represents the arginine finger domain (RF), the pink box represents the Walker A motif (WA), and the deep green box represents the Walker B motif (WB).
    Dntp, supplied by Kapa Biosystems, used in various techniques. Bioz Stars score: 95/100, based on 411 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Kapa Biosystems
    Average 95 stars, based on 411 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    96
    Meridian Life Science dntp
    Pathogenic Homozygous Recessive Variants in MCM9 Were Identified in Two Consanguineous Kurdish Families from Turkey (A and B) The MCM9 genotype is provided below each individual. WT denotes the wild-type allele. MT (for mutation) indicates either (A) MCM9 c.1732+2T > C or (B) MCM9 c. 394C > T. PCR amplification was completed with the <t>KAPA</t> HiFi HotStart PCR Kit with <t>dNTPs</t> (Kapa Biosystems) according to the manufacturer’s instructions (primers for A are 5′-TCTAGGAGGTCCCGAGATGG-3′ and 5′-CAAAGGCAGAGTGATTGCCG-3′; primers for B are 5′-GCCTGAGAGGCAAGTGAATTTAG-3′ and 5′-TACCTAAAACCAAGGATGTGGGA-3′). PCR products were sequenced at Beckman Coulter Genomics. Results were analyzed with Sequencher (Gene Codes Corporation). Sample chromatograms are shown (5′ to 3′ direction in A; 3′ to 5′ direction in B). Arrows point to the nucleotide peak of interest. Samples utilized for whole-exome sequencing (WES) are indicated by an asterisk. (C) MCM9 is encoded on chr6: 119,252,903–119,134,612 (UCSC Genome Browser hg19). The MCM9 c.1732+2T > C splice variant lies in the splice donor site of exon 9 (red arrow). The c.394C > T mutation lies near the 5′ end of exon 2 (blue arrow). Exons are indicated as full boxes (black). Alternative splice forms of MCM9 either include or exclude exon 11 (white). Introns are indicated as lines. (D) MCM9 consists of an N-terminal DNA binding domain and AAA + core domain. The c.1732+2T > C mutation is predicted to disrupt normal splicing after amino acid 577. The c.394C > T mutation causes insertion of a stop codon in the place of an arginine at position 132 (p.Arg132 ∗ ). This most likely results in a truncated protein if one is formed. The yellow box represents the arginine finger domain (RF), the pink box represents the Walker A motif (WA), and the deep green box represents the Walker B motif (WB).
    Dntp, supplied by Meridian Life Science, used in various techniques. Bioz Stars score: 96/100, based on 2045 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Meridian Life Science
    Average 96 stars, based on 2045 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    96/100 stars
      Buy from Supplier

    95
    Metabion International AG dntps
    Pathogenic Homozygous Recessive Variants in MCM9 Were Identified in Two Consanguineous Kurdish Families from Turkey (A and B) The MCM9 genotype is provided below each individual. WT denotes the wild-type allele. MT (for mutation) indicates either (A) MCM9 c.1732+2T > C or (B) MCM9 c. 394C > T. PCR amplification was completed with the <t>KAPA</t> HiFi HotStart PCR Kit with <t>dNTPs</t> (Kapa Biosystems) according to the manufacturer’s instructions (primers for A are 5′-TCTAGGAGGTCCCGAGATGG-3′ and 5′-CAAAGGCAGAGTGATTGCCG-3′; primers for B are 5′-GCCTGAGAGGCAAGTGAATTTAG-3′ and 5′-TACCTAAAACCAAGGATGTGGGA-3′). PCR products were sequenced at Beckman Coulter Genomics. Results were analyzed with Sequencher (Gene Codes Corporation). Sample chromatograms are shown (5′ to 3′ direction in A; 3′ to 5′ direction in B). Arrows point to the nucleotide peak of interest. Samples utilized for whole-exome sequencing (WES) are indicated by an asterisk. (C) MCM9 is encoded on chr6: 119,252,903–119,134,612 (UCSC Genome Browser hg19). The MCM9 c.1732+2T > C splice variant lies in the splice donor site of exon 9 (red arrow). The c.394C > T mutation lies near the 5′ end of exon 2 (blue arrow). Exons are indicated as full boxes (black). Alternative splice forms of MCM9 either include or exclude exon 11 (white). Introns are indicated as lines. (D) MCM9 consists of an N-terminal DNA binding domain and AAA + core domain. The c.1732+2T > C mutation is predicted to disrupt normal splicing after amino acid 577. The c.394C > T mutation causes insertion of a stop codon in the place of an arginine at position 132 (p.Arg132 ∗ ). This most likely results in a truncated protein if one is formed. The yellow box represents the arginine finger domain (RF), the pink box represents the Walker A motif (WA), and the deep green box represents the Walker B motif (WB).
    Dntps, supplied by Metabion International AG, used in various techniques. Bioz Stars score: 95/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/Metabion International AG
    Average 95 stars, based on 24 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-02
    95/100 stars
      Buy from Supplier

    96
    Millipore dntp
    Evaluation of direct cell lysis protocols on RT-qPCR . (A) The RT-qPCR yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike using 17 lysis conditions. Five nanograms of purified RNA was used in all RT reactions. Relative RT yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage relative to the water control for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Lysis conditions with Cq-values below that of the water control are RT enhancing agents, while conditions with higher Cq-values are inhibitory. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are shown in Table S4 in Supplementary Material. (B) Mean RT yield for Gapdh , Vim , Dll , and Jag1 . The relative transcript yield of each transcript was averaged and compared to the optimal RT-qPCR condition (RT mix). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM <t>oligo-dT,</t> and 1 mM <t>dNTP.</t>
    Dntp, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 2634 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/Millipore
    Average 96 stars, based on 2634 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    96/100 stars
      Buy from Supplier

    dntp  (PEQLAB)
    93
    PEQLAB dntp
    Evaluation of direct cell lysis protocols on RT-qPCR . (A) The RT-qPCR yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike using 17 lysis conditions. Five nanograms of purified RNA was used in all RT reactions. Relative RT yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage relative to the water control for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Lysis conditions with Cq-values below that of the water control are RT enhancing agents, while conditions with higher Cq-values are inhibitory. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are shown in Table S4 in Supplementary Material. (B) Mean RT yield for Gapdh , Vim , Dll , and Jag1 . The relative transcript yield of each transcript was averaged and compared to the optimal RT-qPCR condition (RT mix). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM <t>oligo-dT,</t> and 1 mM <t>dNTP.</t>
    Dntp, supplied by PEQLAB, used in various techniques. Bioz Stars score: 93/100, based on 130 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/PEQLAB
    Average 93 stars, based on 130 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    93/100 stars
      Buy from Supplier

    96
    PerkinElmer dntp
    Evaluation of direct cell lysis protocols on RT-qPCR . (A) The RT-qPCR yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike using 17 lysis conditions. Five nanograms of purified RNA was used in all RT reactions. Relative RT yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage relative to the water control for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Lysis conditions with Cq-values below that of the water control are RT enhancing agents, while conditions with higher Cq-values are inhibitory. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are shown in Table S4 in Supplementary Material. (B) Mean RT yield for Gapdh , Vim , Dll , and Jag1 . The relative transcript yield of each transcript was averaged and compared to the optimal RT-qPCR condition (RT mix). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM <t>oligo-dT,</t> and 1 mM <t>dNTP.</t>
    Dntp, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 96/100, based on 2063 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntp/product/PerkinElmer
    Average 96 stars, based on 2063 article reviews
    Price from $9.99 to $1999.99
    dntp - by Bioz Stars, 2020-02
    96/100 stars
      Buy from Supplier

    Image Search Results


    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of dNTPs. ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM NaCl, 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.

    Journal: Molecules

    Article Title: Chemical Incorporation of Chain-Terminating Nucleoside Analogs as 3′-Blocking DNA Damage and Their Removal by Human ERCC1-XPF Endonuclease

    doi: 10.3390/molecules21060766

    Figure Lengend Snippet: Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of dNTPs. ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM NaCl, 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.

    Article Snippet: Resumption of DNA Synthesis by DNA Polymerase after the Removal of CTNAs The hybridized oligonucleotides (400 fmol) were first treated with ERCC1-XPF (230 fmol) in 10 µL of 50 mM Tris-HCl buffer (pH 8.0), containing 2 mM MgCl2 , 0.5 mM DTT and 0.1 mg·mL−1 BSA, at 25 °C for 16 h. To the reaction mixture was added 5 µL of 30 mM Tris-HCl buffer (pH 7.9), containing 150 mM NaCl, 30 mM MgCl2 , 30 mM DTT, 300 µM dNTPs and the Klenow fragment of Escherichia coli DNA polymerase I, lacking the 3′–5′ exonuclease activity (KF− , 0.1 unit, Takara Bio).

    Techniques: Activity Assay, Labeling, Incubation

    Repair of the CTNA-containing oligonucleotides by human ERCC1-XPF endonuclease and DNA polymerase. Panels A and B represent the reaction scheme and the results, respectively. First, the 32 P-labeled substrates (400 fmol) were incubated at 25 °C for 16 h, in the absence (lanes 1, 2, 5, 6, 9, 10, 13, 14, 17, 18, 21 and 22) or presence (the other lanes) of ERCC1-XPF (230 fmol), in 10 µL of 50 mM Tris-HCl buffer (pH 8.0) containing 2 mM MgCl 2 , 0.5 mM DTT and 0.1 mg·mL −1 BSA. Then, a polymerase reaction mixture (5 µL, containing 30 mM Tris-HCl, (pH 7.9), 150 mM NaCl, 30 mM MgCl 2 , 30 mM DTT, 300 µM dNTPs and 0.1 unit of KF − for even lanes) or 5 mM EDTA (5 µL for odd lanes) was added to the reaction mixture, and the total reaction mixtures (15 µL) were incubated at 37 °C for 10 min. The cleavage sites observed with ERCC1-XPF are indicated by black triangles. The fully extended products were quantified, and the values are shown.

    Journal: Molecules

    Article Title: Chemical Incorporation of Chain-Terminating Nucleoside Analogs as 3′-Blocking DNA Damage and Their Removal by Human ERCC1-XPF Endonuclease

    doi: 10.3390/molecules21060766

    Figure Lengend Snippet: Repair of the CTNA-containing oligonucleotides by human ERCC1-XPF endonuclease and DNA polymerase. Panels A and B represent the reaction scheme and the results, respectively. First, the 32 P-labeled substrates (400 fmol) were incubated at 25 °C for 16 h, in the absence (lanes 1, 2, 5, 6, 9, 10, 13, 14, 17, 18, 21 and 22) or presence (the other lanes) of ERCC1-XPF (230 fmol), in 10 µL of 50 mM Tris-HCl buffer (pH 8.0) containing 2 mM MgCl 2 , 0.5 mM DTT and 0.1 mg·mL −1 BSA. Then, a polymerase reaction mixture (5 µL, containing 30 mM Tris-HCl, (pH 7.9), 150 mM NaCl, 30 mM MgCl 2 , 30 mM DTT, 300 µM dNTPs and 0.1 unit of KF − for even lanes) or 5 mM EDTA (5 µL for odd lanes) was added to the reaction mixture, and the total reaction mixtures (15 µL) were incubated at 37 °C for 10 min. The cleavage sites observed with ERCC1-XPF are indicated by black triangles. The fully extended products were quantified, and the values are shown.

    Article Snippet: Resumption of DNA Synthesis by DNA Polymerase after the Removal of CTNAs The hybridized oligonucleotides (400 fmol) were first treated with ERCC1-XPF (230 fmol) in 10 µL of 50 mM Tris-HCl buffer (pH 8.0), containing 2 mM MgCl2 , 0.5 mM DTT and 0.1 mg·mL−1 BSA, at 25 °C for 16 h. To the reaction mixture was added 5 µL of 30 mM Tris-HCl buffer (pH 7.9), containing 150 mM NaCl, 30 mM MgCl2 , 30 mM DTT, 300 µM dNTPs and the Klenow fragment of Escherichia coli DNA polymerase I, lacking the 3′–5′ exonuclease activity (KF− , 0.1 unit, Takara Bio).

    Techniques: Labeling, Incubation

    Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate ATP/ATPγS in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of dNTPs (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004

    Journal: eLife

    Article Title: DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase

    doi: 10.7554/eLife.02384

    Figure Lengend Snippet: Pol V Mut is not activated by GTP, ADP, or dTTP and does not incorporate ATP/ATPγS in to DNA during synthesis. Pol V Mut WT, pol V Mut E38K/K72R, and pol V Mut E38K/ΔC17 were assembled according to the protocol in Figure 1A . ( A ) ATP, dATP, GTP, ADP, dTTP or ATPγS (500 μM) were used to activate pol V Mut for DNA synthesis and activity was checked in the presence of dNTPs (500 μM) and 3 nt oh HP (50 nM). ( B ) A HP containing TTT as its 3 nt oh was employed to determine if the various pol V Muts insert ATP or ATPγS during DNA synthesis. DNA extension is only observed in reactions where dATP is included. Other dNTPs are not present in any of the reactions. DOI: http://dx.doi.org/10.7554/eLife.02384.004

    Article Snippet: Pol V Mut (400 nM) was added to a 10-μl reaction mixture containing annealed template DNA (50 nM), ATP, ATPγS, dATP, GTP, dTTP, or ADP (500 μM, unless stated otherwise) and dNTPs (Amersham-Pharmacia) (500 μM each).

    Techniques: DNA Synthesis, Activity Assay

    Pol V Mut WT activity on DNA containing an abasic site. Pol V Mut (400 nM) activity was detected on 5′- 32 P-labeled 12 nt oh HP (100 nM), containing an abasic site 3 nts upstream from the 3′-OH, in the presence or absence of ATP/ATPγS and dNTPs. Lesion bypass is only observed when ATPγS is present. DOI: http://dx.doi.org/10.7554/eLife.02384.005

    Journal: eLife

    Article Title: DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase

    doi: 10.7554/eLife.02384

    Figure Lengend Snippet: Pol V Mut WT activity on DNA containing an abasic site. Pol V Mut (400 nM) activity was detected on 5′- 32 P-labeled 12 nt oh HP (100 nM), containing an abasic site 3 nts upstream from the 3′-OH, in the presence or absence of ATP/ATPγS and dNTPs. Lesion bypass is only observed when ATPγS is present. DOI: http://dx.doi.org/10.7554/eLife.02384.005

    Article Snippet: Pol V Mut (400 nM) was added to a 10-μl reaction mixture containing annealed template DNA (50 nM), ATP, ATPγS, dATP, GTP, dTTP, or ADP (500 μM, unless stated otherwise) and dNTPs (Amersham-Pharmacia) (500 μM each).

    Techniques: Activity Assay, Labeling

    Pathogenic Homozygous Recessive Variants in MCM9 Were Identified in Two Consanguineous Kurdish Families from Turkey (A and B) The MCM9 genotype is provided below each individual. WT denotes the wild-type allele. MT (for mutation) indicates either (A) MCM9 c.1732+2T > C or (B) MCM9 c. 394C > T. PCR amplification was completed with the KAPA HiFi HotStart PCR Kit with dNTPs (Kapa Biosystems) according to the manufacturer’s instructions (primers for A are 5′-TCTAGGAGGTCCCGAGATGG-3′ and 5′-CAAAGGCAGAGTGATTGCCG-3′; primers for B are 5′-GCCTGAGAGGCAAGTGAATTTAG-3′ and 5′-TACCTAAAACCAAGGATGTGGGA-3′). PCR products were sequenced at Beckman Coulter Genomics. Results were analyzed with Sequencher (Gene Codes Corporation). Sample chromatograms are shown (5′ to 3′ direction in A; 3′ to 5′ direction in B). Arrows point to the nucleotide peak of interest. Samples utilized for whole-exome sequencing (WES) are indicated by an asterisk. (C) MCM9 is encoded on chr6: 119,252,903–119,134,612 (UCSC Genome Browser hg19). The MCM9 c.1732+2T > C splice variant lies in the splice donor site of exon 9 (red arrow). The c.394C > T mutation lies near the 5′ end of exon 2 (blue arrow). Exons are indicated as full boxes (black). Alternative splice forms of MCM9 either include or exclude exon 11 (white). Introns are indicated as lines. (D) MCM9 consists of an N-terminal DNA binding domain and AAA + core domain. The c.1732+2T > C mutation is predicted to disrupt normal splicing after amino acid 577. The c.394C > T mutation causes insertion of a stop codon in the place of an arginine at position 132 (p.Arg132 ∗ ). This most likely results in a truncated protein if one is formed. The yellow box represents the arginine finger domain (RF), the pink box represents the Walker A motif (WA), and the deep green box represents the Walker B motif (WB).

    Journal: American Journal of Human Genetics

    Article Title: MCM9 Mutations Are Associated with Ovarian Failure, Short Stature, and Chromosomal Instability

    doi: 10.1016/j.ajhg.2014.11.002

    Figure Lengend Snippet: Pathogenic Homozygous Recessive Variants in MCM9 Were Identified in Two Consanguineous Kurdish Families from Turkey (A and B) The MCM9 genotype is provided below each individual. WT denotes the wild-type allele. MT (for mutation) indicates either (A) MCM9 c.1732+2T > C or (B) MCM9 c. 394C > T. PCR amplification was completed with the KAPA HiFi HotStart PCR Kit with dNTPs (Kapa Biosystems) according to the manufacturer’s instructions (primers for A are 5′-TCTAGGAGGTCCCGAGATGG-3′ and 5′-CAAAGGCAGAGTGATTGCCG-3′; primers for B are 5′-GCCTGAGAGGCAAGTGAATTTAG-3′ and 5′-TACCTAAAACCAAGGATGTGGGA-3′). PCR products were sequenced at Beckman Coulter Genomics. Results were analyzed with Sequencher (Gene Codes Corporation). Sample chromatograms are shown (5′ to 3′ direction in A; 3′ to 5′ direction in B). Arrows point to the nucleotide peak of interest. Samples utilized for whole-exome sequencing (WES) are indicated by an asterisk. (C) MCM9 is encoded on chr6: 119,252,903–119,134,612 (UCSC Genome Browser hg19). The MCM9 c.1732+2T > C splice variant lies in the splice donor site of exon 9 (red arrow). The c.394C > T mutation lies near the 5′ end of exon 2 (blue arrow). Exons are indicated as full boxes (black). Alternative splice forms of MCM9 either include or exclude exon 11 (white). Introns are indicated as lines. (D) MCM9 consists of an N-terminal DNA binding domain and AAA + core domain. The c.1732+2T > C mutation is predicted to disrupt normal splicing after amino acid 577. The c.394C > T mutation causes insertion of a stop codon in the place of an arginine at position 132 (p.Arg132 ∗ ). This most likely results in a truncated protein if one is formed. The yellow box represents the arginine finger domain (RF), the pink box represents the Walker A motif (WA), and the deep green box represents the Walker B motif (WB).

    Article Snippet: Using the KAPA HiFi HotStart PCR Kit with dNTPs (Kapa Biosystems) and primers to amplify exons 7–12 (c.1151_1996), we expected to observe two previously reported wild-type products: an 846 bp product and a 700 bp product resulting from exon 11 skipping ( A; B, S3C, and A).

    Techniques: Mutagenesis, Polymerase Chain Reaction, Amplification, Sequencing, Variant Assay, Binding Assay, Western Blot

    Evaluation of direct cell lysis protocols on RT-qPCR . (A) The RT-qPCR yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike using 17 lysis conditions. Five nanograms of purified RNA was used in all RT reactions. Relative RT yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage relative to the water control for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Lysis conditions with Cq-values below that of the water control are RT enhancing agents, while conditions with higher Cq-values are inhibitory. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are shown in Table S4 in Supplementary Material. (B) Mean RT yield for Gapdh , Vim , Dll , and Jag1 . The relative transcript yield of each transcript was averaged and compared to the optimal RT-qPCR condition (RT mix). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM oligo-dT, and 1 mM dNTP.

    Journal: Frontiers in Oncology

    Article Title: Direct Cell Lysis for Single-Cell Gene Expression Profiling

    doi: 10.3389/fonc.2013.00274

    Figure Lengend Snippet: Evaluation of direct cell lysis protocols on RT-qPCR . (A) The RT-qPCR yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike using 17 lysis conditions. Five nanograms of purified RNA was used in all RT reactions. Relative RT yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage relative to the water control for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Lysis conditions with Cq-values below that of the water control are RT enhancing agents, while conditions with higher Cq-values are inhibitory. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are shown in Table S4 in Supplementary Material. (B) Mean RT yield for Gapdh , Vim , Dll , and Jag1 . The relative transcript yield of each transcript was averaged and compared to the optimal RT-qPCR condition (RT mix). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM oligo-dT, and 1 mM dNTP.

    Article Snippet: Directly lysed cells were incubated in 0.5 mM dNTP (Sigma-Aldrich), 2.5 μM oligo-dT (Metabion), and 2.5 μM random hexamers (Metabion) at 65°C for 5 min and then chilled on ice.

    Techniques: Lysis, Quantitative RT-PCR, Purification, Polymerase Chain Reaction

    Evaluation of direct cell lysis protocols . (A) The lysis yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike compared at 17 lysis conditions. Thirty-two astrocytes were sorted for each condition. Relative cDNA yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage compared to the optimal lysis condition for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are listed in Table S3 in Supplementary Material. (B) Mean cDNA yield of the transcripts. Expressions of Gapdh , Vim , Dll , and Jag1 were averaged and are compared to the overall optimal lysis condition (1 mg/ml BSA). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM oligo-dT, and 1 mM dNTP.

    Journal: Frontiers in Oncology

    Article Title: Direct Cell Lysis for Single-Cell Gene Expression Profiling

    doi: 10.3389/fonc.2013.00274

    Figure Lengend Snippet: Evaluation of direct cell lysis protocols . (A) The lysis yields of Gapdh , Vim , Dll1 , Jag1 , DNA, and RNA spike compared at 17 lysis conditions. Thirty-two astrocytes were sorted for each condition. Relative cDNA yields are presented as Cq-values on the left y -axis and relative transcript numbers on the right y -axis. The relative transcript number is expressed in percentage compared to the optimal lysis condition for each gene, assuming 100% RT efficiency and 100% PCR efficiency. Data are shown as mean ± SD ( n = 4). Missing data were excluded and are listed in Table S3 in Supplementary Material. (B) Mean cDNA yield of the transcripts. Expressions of Gapdh , Vim , Dll , and Jag1 were averaged and are compared to the overall optimal lysis condition (1 mg/ml BSA). Data are shown as mean ± SD ( n = 4). 7-deaz GTP, 7-deaza-2′ deoxyguanosine 5′ triphosphate lithium salt; GTC, guanidine thiocyanate; LPA, linear polyacrylamide; polyI, polyinosinic acid potassium salt; 2× RT buffer, 2× reverse transcription buffer; RT mix, 2× RT buffer, 5 μM random hexamers, 5 μM oligo-dT, and 1 mM dNTP.

    Article Snippet: Directly lysed cells were incubated in 0.5 mM dNTP (Sigma-Aldrich), 2.5 μM oligo-dT (Metabion), and 2.5 μM random hexamers (Metabion) at 65°C for 5 min and then chilled on ice.

    Techniques: Lysis, Polymerase Chain Reaction

    Incorporation of 8-oxodGMP and 2-OH-dAMP in TNR sequences. ( A and B ) Incorporation of dGMP and 8-oxodGMP opposite cytosine. ( A ) The primer/template sequence and representative gels are shown. Primer/template substrate (160 nM) (S1/T1) was incubated with POL β and increasing concentration of 8-oxodGTP or dGTP at 37°C for 1 h (0–30 μM and 0–3 μM, respectively). M is the DNA substrate without enzyme. Reaction products were separated by 20% denaturing PAGE at 500 V for 2.5 h. Bands were visualized by fluorescence emission by Typhoon scanner and the analysis of the band intensities was performed by ImageJ software. ( B ) Percentage of incorporated dNMP plotted as a function of added dNTPs. Data were fitted by Kaleidagraph software to evaluate kinetics parameters. ( C and D ) Incorporation of 8-oxodGMP and dTMP opposite adenine. Primer/template sequences is S2/T1 (Supplementary Table S1). Experimental conditions and analyses were as described above. The concentration range of 8-oxodGTP and dTTP was 0–2 μM and 0–1 μM, respectively. ( E – F ) Incorporation of 2-OH-dAMP and dAMP in CAG/CTG repeat sequence. ( E ) Primer/template sequence is S3/T2 (Supplementary Table S1); ( F ) Primer/template duplex (160 nM) was incubated with POL β (0.1U) in 10 μl reaction buffer in the absence of dNTP (lane 1), after addition of 2-OH-dATP (lane 2), dGTP and 2-OH-dATP (lane 3); 2-OH-dATP, dGTP and dCTP (lane 4), dATP (lane 5); dATP and dGTP (lane 6), dATP, dGTP and dCTP (lane 7). All nucleotide triphosphates were at 10 μM final concentration. Reaction products were separated by 15% denaturing PAGE and image acquisition and analysis was performed as described before.

    Journal: Nucleic Acids Research

    Article Title: Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability

    doi: 10.1093/nar/gkw170

    Figure Lengend Snippet: Incorporation of 8-oxodGMP and 2-OH-dAMP in TNR sequences. ( A and B ) Incorporation of dGMP and 8-oxodGMP opposite cytosine. ( A ) The primer/template sequence and representative gels are shown. Primer/template substrate (160 nM) (S1/T1) was incubated with POL β and increasing concentration of 8-oxodGTP or dGTP at 37°C for 1 h (0–30 μM and 0–3 μM, respectively). M is the DNA substrate without enzyme. Reaction products were separated by 20% denaturing PAGE at 500 V for 2.5 h. Bands were visualized by fluorescence emission by Typhoon scanner and the analysis of the band intensities was performed by ImageJ software. ( B ) Percentage of incorporated dNMP plotted as a function of added dNTPs. Data were fitted by Kaleidagraph software to evaluate kinetics parameters. ( C and D ) Incorporation of 8-oxodGMP and dTMP opposite adenine. Primer/template sequences is S2/T1 (Supplementary Table S1). Experimental conditions and analyses were as described above. The concentration range of 8-oxodGTP and dTTP was 0–2 μM and 0–1 μM, respectively. ( E – F ) Incorporation of 2-OH-dAMP and dAMP in CAG/CTG repeat sequence. ( E ) Primer/template sequence is S3/T2 (Supplementary Table S1); ( F ) Primer/template duplex (160 nM) was incubated with POL β (0.1U) in 10 μl reaction buffer in the absence of dNTP (lane 1), after addition of 2-OH-dATP (lane 2), dGTP and 2-OH-dATP (lane 3); 2-OH-dATP, dGTP and dCTP (lane 4), dATP (lane 5); dATP and dGTP (lane 6), dATP, dGTP and dCTP (lane 7). All nucleotide triphosphates were at 10 μM final concentration. Reaction products were separated by 15% denaturing PAGE and image acquisition and analysis was performed as described before.

    Article Snippet: Reagents 8-oxodGTP was obtained from TriLink (TriLink BioTechnologies, San Diego, CA 92121, USA), dNTPs were from Sigma (Sigma-Aldrich, Corporate Offices St. Louis, MO 63103, USA) and 2-OH-dATP was purchased from Jena (Jena Bioscience GmbH 07749 Jena, DE).

    Techniques: Sequencing, Incubation, Concentration Assay, Polyacrylamide Gel Electrophoresis, Fluorescence, Software, CTG Assay

    Incorporation and extension of 8-oxodGMP by POL β. Primer/template (160 nM) (Supplementary Table S1, S3/T2 panel A; S1/T1 panel B) were used. Both substrates were incubated with POL β (0.1 U) and 8-oxodGTP or dGTP and others dNTPs (50 μM final concentration each). ( A ) Lane 1, primer; lane 2, 8-oxodGTP; lane 3, as lane 2 plus dCTP; lane 4, as lane 3 plus dATP; lane 5, as lane 4 plus dTTP; lane 6, primer plus dGTP; lane 7, as lane 6 plus dCTP; lane 8 as lane 7 plus dATP; lane 9, as lane 8 plus dTTP. ( B ) Lane 1, primer; lane 2, primer plus 8- oxodGTP; lane 3, as lane 2 plus dCTP; lane 4 as lane 3 plus dTTP; lane 5, as lane 4 plus dATP; lane 6, primer plus dGTP; lane 7, as lane 6 plus dCTP; lane 8 as lane 6 plus dTTP and dATP. ( C ) The DNA substrate (160 nM) was built by annealing three oligomers of 22, 77 and 100 bases respectively indicated as S1, S4 and T1 in Supplementary Table S1, in order to produce a preformed nicked duplex containing CTG/CAG repeats. Incorporation of dGTP and 8-oxodGTP (lanes 1 and 4) and elongation (lanes 2 and 5) was obtained by incubating the substrate (lane 3) with POL β (0.1 U) at 37°C for 1 h.

    Journal: Nucleic Acids Research

    Article Title: Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability

    doi: 10.1093/nar/gkw170

    Figure Lengend Snippet: Incorporation and extension of 8-oxodGMP by POL β. Primer/template (160 nM) (Supplementary Table S1, S3/T2 panel A; S1/T1 panel B) were used. Both substrates were incubated with POL β (0.1 U) and 8-oxodGTP or dGTP and others dNTPs (50 μM final concentration each). ( A ) Lane 1, primer; lane 2, 8-oxodGTP; lane 3, as lane 2 plus dCTP; lane 4, as lane 3 plus dATP; lane 5, as lane 4 plus dTTP; lane 6, primer plus dGTP; lane 7, as lane 6 plus dCTP; lane 8 as lane 7 plus dATP; lane 9, as lane 8 plus dTTP. ( B ) Lane 1, primer; lane 2, primer plus 8- oxodGTP; lane 3, as lane 2 plus dCTP; lane 4 as lane 3 plus dTTP; lane 5, as lane 4 plus dATP; lane 6, primer plus dGTP; lane 7, as lane 6 plus dCTP; lane 8 as lane 6 plus dTTP and dATP. ( C ) The DNA substrate (160 nM) was built by annealing three oligomers of 22, 77 and 100 bases respectively indicated as S1, S4 and T1 in Supplementary Table S1, in order to produce a preformed nicked duplex containing CTG/CAG repeats. Incorporation of dGTP and 8-oxodGTP (lanes 1 and 4) and elongation (lanes 2 and 5) was obtained by incubating the substrate (lane 3) with POL β (0.1 U) at 37°C for 1 h.

    Article Snippet: Reagents 8-oxodGTP was obtained from TriLink (TriLink BioTechnologies, San Diego, CA 92121, USA), dNTPs were from Sigma (Sigma-Aldrich, Corporate Offices St. Louis, MO 63103, USA) and 2-OH-dATP was purchased from Jena (Jena Bioscience GmbH 07749 Jena, DE).

    Techniques: Incubation, Concentration Assay, CTG Assay

    Novel contributors in TNR expansion process. Following an initial incision event mediated by OGG1 and APE1 at an 8-oxodG site in the top strand (red, step 1), POL drives repair synthesis by LP BER. Long flaps might eventually fold in stable secondary structures (step 2). A faulty removal by FEN1 depending on flap conformations might leave hairpins with unligatable dRP ends (step 3). Removal of dRP by POL β allows ligation by LIG1 (step 4). If 8-oxodGTP is present in the dNTPs pool, 8-oxodGMP can be incorporated opposite A in the complementary strand creating a substrate for MUTYH (step 5). MUTYH activity on the bottom strand (blue) allows the initiation of a new repair event, as well as an elongation process on this side (step 6). Realignements of the strands will result in TNR expansion (step 7). Newly synthesized tracts are represented by full rectangles. The proposed model has been modified from refs. ( 12 , 16 , 40 ).

    Journal: Nucleic Acids Research

    Article Title: Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability

    doi: 10.1093/nar/gkw170

    Figure Lengend Snippet: Novel contributors in TNR expansion process. Following an initial incision event mediated by OGG1 and APE1 at an 8-oxodG site in the top strand (red, step 1), POL drives repair synthesis by LP BER. Long flaps might eventually fold in stable secondary structures (step 2). A faulty removal by FEN1 depending on flap conformations might leave hairpins with unligatable dRP ends (step 3). Removal of dRP by POL β allows ligation by LIG1 (step 4). If 8-oxodGTP is present in the dNTPs pool, 8-oxodGMP can be incorporated opposite A in the complementary strand creating a substrate for MUTYH (step 5). MUTYH activity on the bottom strand (blue) allows the initiation of a new repair event, as well as an elongation process on this side (step 6). Realignements of the strands will result in TNR expansion (step 7). Newly synthesized tracts are represented by full rectangles. The proposed model has been modified from refs. ( 12 , 16 , 40 ).

    Article Snippet: Reagents 8-oxodGTP was obtained from TriLink (TriLink BioTechnologies, San Diego, CA 92121, USA), dNTPs were from Sigma (Sigma-Aldrich, Corporate Offices St. Louis, MO 63103, USA) and 2-OH-dATP was purchased from Jena (Jena Bioscience GmbH 07749 Jena, DE).

    Techniques: Ligation, Activity Assay, Synthesized, Modification

    Effects of increasing the dNTP concentration on primase-coupled polymerase activity. Assays contained primase-helicase, polymerase (UL30-UL42), 3′-d(T 20 GTCCT 36 )-5′, and either [α- 32 P]NTPs or NTPs and [α- 32 P]dNTPs to measure primase activity and primase-coupled polymerase activity, respectively. Coupled activity was measured in terms of pmol of dATP incorporated. The fraction of primers elongated was determined as described under “Experimental Procedures.”

    Journal: The Journal of Biological Chemistry

    Article Title: Initiation of New DNA Strands by the Herpes Simplex Virus-1 Primase-Helicase Complex and Either Herpes DNA Polymerase or Human DNA Polymerase ? *

    doi: 10.1074/jbc.M805476200

    Figure Lengend Snippet: Effects of increasing the dNTP concentration on primase-coupled polymerase activity. Assays contained primase-helicase, polymerase (UL30-UL42), 3′-d(T 20 GTCCT 36 )-5′, and either [α- 32 P]NTPs or NTPs and [α- 32 P]dNTPs to measure primase activity and primase-coupled polymerase activity, respectively. Coupled activity was measured in terms of pmol of dATP incorporated. The fraction of primers elongated was determined as described under “Experimental Procedures.”

    Article Snippet: Unlabeled NTPs and dNTPs were from Sigma, and radiolabeled NTPs and dNTPs were from PerkinElmer Life Sciences.

    Techniques: Concentration Assay, Activity Assay