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 Source
An E. coli strain which carries the cloned human APE 1 gene.
This product is related to the following categories:
DNA Repair Enzymes and Structure-specific Endonucleases Products
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