Oxoguanine Glycosylase 1 (OGG1), a prominent member of the BER enzyme family, is an essential DNA repair enzyme. OGG1 is highly conserved across eukaryotic organisms and is expressed in various cell types. Its activity is regulated by several factors, including cellular redox status, DNA damage, and cell cycle progression. In addition to its role in repairing oxidative DNA damage, OGG1 has also been implicated in other cellular processes, such as transcription, replication, and apoptosis. In addition, the combination of OGG1 and NEIL1 can contribute to improve the repair efficiency of oxidative DNA damage, maintain genomic stability, and reduce the risk of cell mutation. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human OGG1 and recombinant human NEIL1. Briefly, biotin-linked OGG1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to NEIL1-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37℃. Finally, add 50 μl stop solution to the wells and read at 450 nm immediately. The binding activity of recombinant human OGG1 and recombinant human NEIL1 was shown in Figure 1, the EC50?for this effect is 0.33 ug/mL.