Log In Sign up
The largest database of trusted experimental protocols

E coli uracil dna glycosylase udg

Manufactured by New England Biolabs
Visit Supplier
Sourced in United Kingdom

E. coli uracil DNA glycosylase (UDG) is an enzyme that selectively removes uracil residues from DNA. It is involved in the base excision repair pathway, which is responsible for correcting DNA damage caused by the spontaneous deamination of cytosine to uracil.

Automatically generated - may contain errors

Lab products found in correlation

γ 32p atp, by PerkinElmer (3 mentions) Human ap endonuclease 1 ape1, by New England Biolabs (1 mentions) Acrylamide bis acrylamide solution, by Bio-Rad (1 mentions) Human pol β, by Bio-Techne (1 mentions) Biospin columns, by Bio-Rad (1 mentions) T4 polynucleotide kinase t4 pnk, by New England Biolabs (1 mentions) Unlabeled nucleotides, by GE Healthcare (1 mentions)

Spelling variants of this product

Uracil DNA glycosylase (74 citations) E. coli UDG (4 citations) E. coli uracil DNA glycosylase (2 citations)

5 protocols using e coli uracil dna glycosylase udg

1

Enzymatic DNA Damage Repair Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
E. coli uracil DNA glycosylase (UDG, ca# M0280S), human AP endonuclease 1 (APE1, ca# M0282S), and human single-strand selective monofunctional uracil DNA glycosylase (hSMUG1, ca# M0336S) were purchased from New England Biolabs (NEB).
Sowers M.L., Conrad J.W., Chang-Gu B., Cherryhomes E., Hackfeld L.C, & Sowers L.C. (2023). DNA Base Excision Repair Intermediates Influence Duplex–Quadruplex Equilibrium. Molecules, 28(3), 970.
+ Open protocol
+ Expand
2

Recombinant Human Polymerases for Gel Electrophoresis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Full-length recombinant human polymerase κ (hPol κ) used for gel electrophoresis experiments was purchased from Enzymax (Lexington, KY). Human Pol β was obtained from Trevigen (Gaithersburg, MD). Recombinant human DNA polymerases hPol η (amino acids 1–437), hPol ι (amino acids 1–420), and hPol κ (amino acids 19–526) (active core enzymes) were expressed and purified according to previously published procedures.44 (link)–46 (link) T4 polynucleotide kinase (T4-PNK) and E. coli uracil DNA glycosylase (UDG) were purchased from New England Biolabs (Beverly, MA). [γ-32P]ATP was purchased from Perkin-Elmer Life Sciences (Boston, MA). Acrylamide/bis-acrylamide solution (40% 19:1, w/w) and Bio-spin columns were obtained from Bio-Rad laboratories (Hercules, CA). All other chemicals were purchased either from Sigma-Aldrich or Fisher Scientific.
Kotapati S., Wickramaratne S., Esades A., Boldry E.J., Dorr D.Q., Pence M.G., Guengerich F.P, & Tretyakova N.Y. (2015). Polymerase Bypass of N6-Deoxyadenosine Adducts Derived from Epoxide Metabolites of 1,3-Butadiene. Chemical research in toxicology, 28(7), 1496-1507.
+ Open protocol
+ Expand
3

Thermal Stability of DNA Glycosylase TvoOgg

Check if the same lab product or an alternative is used in the 5 most similar protocols
The preparation of double-stranded DNA containing AP sites was essentially according to the method of Horst and Fritz [23 (link)]. Ten pmol of double-stranded DNA containing a U/C mismatch was incubated with 1.25 U of E. coli uracil DNA glycosylase (UDG, New England BioLabs, UK), in the reaction buffer for UDG, for 30 min at 37°C. The AP/C substrate was incubated with 1 pmol of TvoOgg, in the same reaction buffer used for the glycosylase activity assay described above, for 30 min at 37°C, 50°C, 60°C, 70°C, 80°C, or 90°C without subsequent alkaline treatment. The reaction products were suspended in 10 μL of gel loading buffer at 94°C for 3 min and then analyzed on 15% polyacrylamide-7 M urea gels.
Fujii M., Hata C., Ukita M., Fukushima C., Matsuura C., Kawashima-Ohya Y., Tomobe K, & Kawashima T. (2016). Characterization of a Thermostable 8-Oxoguanine DNA Glycosylase Specific for GO/N Mismatches from the Thermoacidophilic Archaeon Thermoplasma volcanium. Archaea, 2016, 8734894.
+ Open protocol
+ Expand
4

Radiolabeling Substrates for DNA Repair Assays

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
Unlabeled nucleotides were purchased from GE Healthcare. [α32P]-Cordycepin (3′-dATP) and [γ32P]-ATP were obtained from Perkin Elmer Life Sciences. Substrates were radiolabeled at the 3′ end with [α32P]-Cordycepin and terminal deoxynucleotidyl transferase (TdT) or at the 5′ end with [γ32P]-ATP and T4 polynucleotide kinase (T4PNK). TdT, T4PNK, human AP endonuclease I (hAPE1), E. coli Uracil DNA Glycosylase (UDG) and E. coli EndoIII, were from New England Biolabs. Thrombin was obtained from Novagen. BsuLigD was purified as described (19 (link)).
de Ory A., Nagler K., Carrasco B., Raguse M., Zafra O., Moeller R, & de Vega M. (2016). Identification of a conserved 5′-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair. Nucleic Acids Research, 44(4), 1833-1844.
+ Open protocol
+ Expand
5

Purification and Characterization of Pol β Mutants

Check if the same lab product or an alternative is used in the 5 most similar protocols
Oligodeoxyribonucleotides (oligos) were from Integrated DNA Technologies (IDT) and all were individually PAGE purified. Each oligonucleotide was resuspended in DNase-, RNase-, protease-free water and the concentration was determined from the UV absorbance at 260 nm. Human WT and mutant (K35A,K68A,K72A) Pol β were expressed in Escherichia coli (E. coli) and purified as previously described (33 (link),36 (link)). Total enzyme concentrations were determined by the Bradford assay and are indicated within the plots or figure legends. E. coli uracil DNA glycosylase (UDG) was from New England Biolabs. All radiolabels (γ-32P-ATP and 3′-α-32P-dATP [cordicypin]) were from Perkin Elmer.
Rodriguez Y., Howard M.J., Cuneo M.J., Prasad R, & Wilson S.H. (2017). Unencumbered Pol β lyase activity in nucleosome core particles. Nucleic Acids Research, 45(15), 8901-8915.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!