MutS Protein (Thermus aquaticus)
The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases.
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Description
Endonuclease VIII from E. coli acts as both an N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site). The AP-lyase activity cleaves 3´ and 5´ to the AP site leaving a 5´ phosphate and a 3´ phosphate. Damaged bases recognized and removed by Endonuclease VIII include urea, 5, 6- dihydroxythymine, thymine glycol, 5-hydroxy-5- methylhydantoin, uracil glycol, 6-hydroxy-5, 6-dihydrothymine and methyltartronylurea. While Endonuclease VIII is similar to Endonuclease III, Endonuclease VIII has β and δ lyase activity while Endonuclease III has only β lyase activity.
Applications
Single cell gel electrophoresis (Comet assay)
Alkaline elution
Alkaline unwinding
Source
An E. coli strain which carries the cloned nei gene.
Purity
> 95 % as determined by SDS-PAGE
1X Endonuclease VIII Reaction Buffer
10 mM Tris-HCl, 75 mM NaCl, 1 mM EDTA, pH 8 @ 25°C
Storage Buffer
10 mM Tris-HCl, 250 mM NaCl, 0.1 mM EDTA, 50% Glycerol, 200mg/ml BSA, pH 8 @ 25°C
Heat Inactivation
75°C for 10 min
Storage
-20℃ Avoid repeated freeze-thaw cycles.
Unit Definition
One unit is defined as the amount of enzyme required to cleave 1 pmol of a 34 mer oligonucleotide duplex containing a single AP site* in a total reaction volume of 10 µl in 1 hour at 37°C in 1X Endonuclease VIII Reaction Buffer containing 10 pmol of fluorescently labeled oligonucleotide duplex.
* An AP site is created by treating 10 pmol of a 34 mer oligonucleotide duplex containing a single uracil residue with 1 unit of Uracil-DNA Glycosylase (UDG) for 2 minutes at 37°C.
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The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases.
Endonuclease V, (Endo V) is a 3'-endonuclease involved in DNA repair, which initiates removal of deaminated bases from damaged DNA, including uracil, hypoxanthine, and xanthine.
Human Recombinant Alkyl Adenine DNA Glycosylase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).
Endonuclease III (Nth) protein from E. coli acts as both N-glycosylase and a AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating a basic (AP site).
Endonuclease VIII from E. coli acts as both an N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site).
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