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DNA replication, repair, and recombination requires the excision of nucleotides from the DNA 3′ termini. Many 3′ to 5′ exonucleases have been identified which catalyze the excision of monophosphates from the 3′ termini of DNA. TREX1 and TREX2 are 3′ to 5′ exonucleases that contain three conserved exonuclease active site motifs (EASM) that may produce exonuclease activity. TREX1 and TREX2 are most closely related to the proofreading exonucleases of the bacterial replicative DNA polymerases and the RNase T enzymes. Recombinant expression of TREX1 and TREX2 demonstrates that they have exonuclease activity when oligonucleotide is present. TREX1 shows the greatest exonuclease activity with partial duplex DNA, and no activity with single-stranded RNA or an RNA-DNA partial duplex. In addition, reconstitution of TREX1 with DNA polymerase β and DNA ligase III-XRCC1 facilitates accurate rejoining of a 3′ mismatched base residue at a single-strand break. Thus, TREX1 and TREX2 are 3′ to 5′ exonucleases that may be important for excision of nucleotides during DNA replication, repair, and recombination.Host Species: MouseClone: 29Isotype: IgG1Species Reactivity [for Features Main]: HumanImmunogen: Mouse TRE1 aa. 82-179Immunofluorescence, Western Blotting
