Dntp solutions

Manufactured by New England Biolabs

DNTP solutions are a set of four nucleotide triphosphates (dATP, dCTP, dGTP, and dTTP) that serve as building blocks for DNA synthesis. These solutions are designed to provide a convenient and reliable source of the necessary components for various DNA-based applications, such as PCR, DNA sequencing, and other molecular biology techniques.

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Lab products found in correlation

T4 dna ligase, by New England Biolabs (3 mentions) Pcr purification kit, by Qiagen (3 mentions) Restriction endonuclease, by New England Biolabs (3 mentions) Peptide calibration standard 2 for maldi tof ms, by Bruker (3 mentions) Phusion high fidelity dna polymerase, by New England Biolabs (3 mentions) Protein calibration standard 1, by Bruker (3 mentions) Taq ligase, by New England Biolabs (3 mentions) Oligonucleotide primers, by Integrated DNA Technologies (3 mentions) Endoproteinases glu c, by Roche (2 mentions) Electrocompetent e coli dh5α cells, by New England Biolabs (2 mentions) Gel extraction, by Qiagen (2 mentions) Lys c, by Roche (2 mentions) Pbad hisa vector, by Thermo Fisher Scientific (2 mentions) γ 32p atp, by PerkinElmer (1 mentions) Q5 dna polymerase, by New England Biolabs (1 mentions) Gradient gel, by Bio-Rad (1 mentions) Cyanine5 amine, by Lumiprobe (1 mentions) Bovine serum albumin (bsa), by New England Biolabs (1 mentions)

Spelling variants of this product

DNTPs (205 citations) Deoxynucleotide (dNTP) solution mix (11 citations) DNTP Solution Mix (4 citations) Deoxynucleotide solution mixture (dNTPs) (3 citations) Ultrapure equimolar deoxynucleotide triphosphate (dNTP) sodium salt solution (2 citations)

5 protocols using dntp solutions

Recombinant Protein Expression in E. coli

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All chemicals used were purchased from Sigma Aldrich or Fisher Scientific unless noted otherwise. Endoproteinases Glu-C and Lys-C were purchased from Roche Applied Science. Oligonucleotide primers used for molecular cloning were purchased from Integrated DNA Technologies. The pBAD/HisA vector was purchased from Invitrogen. Electrocompetent E. coli DH5α cells, Phusion High-Fidelity DNA polymerase, Taq ligase, dNTP solutions, T4 DNA ligase and all restriction endonucleases were purchased from New England Biolabs. Gel extraction, plasmid miniprep, and PCR purification kits were purchased from QIAGEN. Protein Calibration Standard I and Peptide Calibration Standard II for MALDI-TOF MS were purchased from Bruker. E. coli DH5α was used as host for cloning and plasmid propagation, and E. coli BL21 (DE3) was used as a host for overexpression.

Yang X., Lennard K.R., He C., Walker M.C., Ball A.T., Doigneaux C., Tavassoli A, & van der Donk W.A. (2018). A lanthipeptide library used to identify a protein–protein interaction inhibitor. Nature chemical biology, 14(4), 375-380.

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Recombinant Protein Expression in E. coli

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Eukaryotic Translesion Synthesis Enzymes

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Yeast pol ζ, human pol κ, and
Rev1 were obtained from Enzymax (Lexington, KY). The dNTP solutions
(100 mM) were from New England Biolabs (Ipswich, MA) or GE Healthcare
(Piscataway, NJ). [γ-³²P]ATP was obtained from PerkinElmer
(Waltham, MA). dG-N²-IQ modified oligonucleotides
were synthesized according to a literature procedure.^{40 (link)} Unmodified oligonucleotides were from Midland Certified
Reagents (Midland, TX).

Bose A., Millsap A.D., DeLeon A., Rizzo C.J, & Basu A.K. (2016). Translesion Synthesis of the N2-2′-Deoxyguanosine Adduct of the Dietary Mutagen IQ in Human Cells: Error-Free Replication by DNA Polymerase κ and Mutagenic Bypass by DNA Polymerases η, ζ, and Rev1. Chemical Research in Toxicology, 29(9), 1549-1559.

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Deglycosylation and Purification of Lantipeptide

Cited 1 time

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All chemicals and enzymes used were purchased from Sigma-Aldrich or Fisher Scientific unless noted otherwise. Endoproteinase Glu-C was purchased from Worthington Biosciences. UDP-xylose was obtained from Complex Carbohydrate Research Center. Oligonucleotide primers used for molecular cloning were purchased from Integrated DNA Technologies. Phusion High-Fidelity DNA polymerase, Q5 DNA polymerase, Taq ligase, dNTP solutions, T4 DNA ligase, and all restriction endonucleases were purchased from New England BioLabs. Gel extraction, plasmid miniprep, and PCR purification kits were purchased from QIAGEN. Protein Calibration Standard I and Peptide Calibration Standard II for MALDI–TOF MS were purchased from Bruker. E. coli NEB Turbo was used as host for cloning and plasmid propagation, and E. coli BL21(DE3) SHuffle was used as a host for expression of deglycosublancin.^{19 (link)} Nickel resin used for gravity-based purification of His-tagged peptides or proteins was purchased from Takara Biosciences. Gradient gels used for checking protein expression were purchased from Biorad Inc. Plasmids pHCMC04 and pJOE8999 for molecular cloning in B. subtilis Δspβ were purchased from the Bacillus Genetics Stock Center (BGSC). B. subtilis Δ6 and plasmids encoding fluorescent proteins in Bacillus were also purchased from BGSC. Cyanine-5-amine was purchased from Lumiprobe.

Biswas S., Wu C, & van der Donk W.A. (2021). The antimicrobial activity of the glycocin sublancin is dependent on an active phosphoenolpyruvate-sugar phosphotransferase system. ACS infectious diseases, 7(8), 2402-2412.

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Kinetics of T7 DNA Polymerase

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All dNTP solutions and BSA were purchased from New England Biolabs. All chemicals used in the reaction buffer were purchased from Fisher Scientific or Sigma-Aldrich. The exonuclease-deficient D5A E7A variant of T7 gene product 5 was used in all experiments and enzymatic synthesis reactions in this paper to prevent exonuclease degradation of the DNA. Wildtype and E514Cou T7 DNA polymerase as well as thioredoxin were expressed and purified as described (21 (link)). All reactions were carried out in T7 Reaction Buffer at 4 °C to better resolve the individual rate constants in the pathway. In some experiments the enzyme–DNA complex was preincubated without Mg²⁺ and Mg²⁺-dNTP was added to start the reaction. In other experiments, both reactant mixtures were preincubated in the presence of Mg²⁺ before mixing with dNTP to start the reaction. In both cases, the final total MgCl₂ concentration after mixing was 12.5 mM and there was no observed difference in the kinetics between the two experimental protocols. All concentrations given are those after mixing.

Dangerfield T.L, & Johnson K.A. (2020). Conformational dynamics during high-fidelity DNA replication and translocation defined using a DNA polymerase with a fluorescent artificial amino acid. The Journal of Biological Chemistry, 296, 100143.

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