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APE 1, also known as HAP 1 or Ref-1, acts as an AP lyase by hydrolyzing the phosphodiester backbone at the 5′ end of an apurinic (AP) site, generating a 1 base gap in the DNA duplex and leaving 3′-hydroxyl and 5′-deoxyribose phosphate termini.
A class II apurinic/apyrimidic (AP) enzyme that cleaves 5’ to an AP site by hydrolysis leaving a hydroxyl group at the 3´ terminus and a deoxyribose 5´-phosphate at the 5´ terminus
The enzyme has DNA glycosylase and apurinic/apyrimidinic lyase (AP lyase) activity.
Modified Enzyme. Ideal for cleaving DNA heteroduplexes on one strand.
Topoisomerase I, derived from Vaccinia virus, is a type I eukaryotic topoisomerase that removes both positive and negative superhelical turns (also called right- and left-handed supercoils) from covalently closed DNA. The product of the reaction is a covalently closed, circular DNA with fewer positive or negative superhelical turns. DNA Topoisomerase I does not absolutely require Mg2+ to function, although low concentrations of Mg2+ may increase activity. Ideal for relax positively and negatively supercoiled DNA in presence of EDTA.
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