- Apurinic/apyrimidinic Endonuclease 1
- DNA AP endonuclease that catalyzes the cleavage of DNA phosphodiester backbone at AP sites via hydrolysis leaving a 1 nucleotide gap with 3'-hydroxyl and 5' deoxyribose phosphate (dRP) termini
- APE 1 has also been reported to have DNA 3'-diesterase, 3' to 5' exonuclease, and RNase H activities
- Also known as HAP1 or Ref-1
Human apurinic/apyrimidinic (AP) endonuclease, APE 1, also known as HAP 1 or Ref-1, shares homology with Escherichia coli exonuclease III protein. APE 1 cleaves the phosphodiester backbone immediately 5´ to an AP site, via hydrolytic mechanism, to generate a single-strand DNA break leaving a 3´-hydroxyl and 5´-deoxyribose phosphate terminus. Besides AP endonuclease activity, APE 1 has also been reported to have weak DNA 3´ -diesterase, 3´ to 5´ exonuclease and RNase H activities (3-5).
In addition to DNA repair activity, APE 1 is also capable of regulating the DNA binding activity of many transcription factors in vitro by a redox mechanism (Ref-1). As part of this process, APE 1 has been shown to stimulate the DNA binding activity of Fos-Jun heterodimers, Jun-Jun homodimers and Hela cell AP-1 proteins as well as that of several other transcription factors including NF-kB, Myb and members of the ATF/CREB family (7-9).
Product SourceAn E. coli strain which carries the cloned human APE 1 gene.
The following reagents are supplied with this product:
Store at (°C) Concentration NEBuffer™ 4 -20 10 X
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