- Bifunctional DNA glycosylase with DNA N-glycosylase and AP lyase activities
- The N-glycosylase activity releases damaged pyrimidines, including thymine glycol and uracil glycol. The AP lyase activity cleaves DNA phosphodiester backbone at AP sites via β and δ-elimination, creating a 1 nucleotide DNA gap with 5' and 3' phosphate termini
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 (1,2). While Endonuclease VIII is similar to Endonuclease III, Endonuclease VIII has β and δ lyase activity while Endonuclease III has only β lyase activity.
Product SourceAn E. coli strain which carries the cloned nei gene.
The following reagents are supplied with this product:
Store at (°C) Concentration Endonuclease VIII Reaction Buffer 10 X
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