8-oxoguanine DNA glycosylase (OGG1) is found in many species and catalyzes the excision of 8-oxoguanine from DNA. This modified base byproduct occurs as a result of exposure to reactive oxygen species. Alternative splicing of the C-terminal region of the OGG1 gene in humans results in two major groups of variants: type 1 and type 2. Both groups share a common N-terminal region that contains a mitochondrial targeting sequence required for OGG1 localization in mitochondria. Although knockout mice lacking the OGG1 gene were observed to have a normal lifespan, the precise role of OGG1 in mutagenesis and cancer remains controversial. OGG1 is also known as 8-hydroxyguanine DNA glycosylase, DNA-apurinic or apyrimidinic site lyase, AP lyase, N-glycosylase/DNA lyase, HMMH, MMH, MUTM, OGH1, and HOGG1.
This product is an affinity-purified IgG antibody that recognizes human OGG1 protein. The antibody was raised in mouse using recombinant OGG1 and can be used for Western blot (WB) detection of human OGG1 protein.