Ogg1 Recombinant Rabbit mAb (S-6056)

OGG1 (8-oxoguanine DNA glycosylase 1) is a bifunctional DNA repair enzyme that initiates the base excision repair (BER) pathway by recognizing and excising 7,8-dihydro-8-oxoguanine (8-oxoG), the most abundant oxidative DNA lesion generated by reactive oxygen species (ROS). The enzyme exhibits a strong preference for 8-oxoG paired with cytosine and catalyzes two successive reactions: hydrolysis of the N-glycosidic bond (glycosylase activity) followed by β-elimination at the 3'-side of the resulting apurinic/apyrimidinic (AP) site (lyase activity). Beyond its canonical repair role, OGG1 functions as an epigenetic reader that binds 8-oxoG lesions enriched in gene regulatory elements, particularly guanine-rich promoters, to facilitate the DNA binding of transcription factors such as NF-κB, thereby modulating inflammatory gene expression. OGG1 deficiency in mice leads to 8-oxoG accumulation in the genome and is associated with increased susceptibility to asbestos-induced pulmonary fibrosis, exacerbated doxorubicin-induced cardiac dysfunction, and altered brain development involving both DNA damage and epigenetic dysregulation. In the context of infection and inflammation, OGG1 bound to oxidative lesions promotes innate immune responses, and pharmacological inhibition of OGG1 substrate binding has emerged as a potential therapeutic strategy for pulmonary diseases and viral infections.