|Flow Cytometry (Flow)||Assay-Dependent|
|Immunohistochemistry (Frozen) (IHC (F))||1:25-1:100|
|Immunohistochemistry (Paraffin) (IHC (P))||1:1000|
|Tested Species reactivity||Human, Mouse, Non-human primate, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A peptide derived from the human Ogg1 (within amino acids 1-100).|
|Purification||Antigen affinity chromatography|
|Contains||0.05% sodium azide|
|Storage conditions||-20° C, Avoid Freeze/Thaw Cycles|
Suggested positive control: Jurkat whole cell extracts.
8-hydroxyguanine, a form of oxidative DNA damage induced by free radicals, causes G:C to T:A transversion. In E. Coli, three DNA repair enzymes exist to prevent the mutagenic effects of 8-hydroxyguanine. One of these enzymes, MutM, was found to have a functional yeast (yOgg1) and human (hOgg1) homologue. hOgg1 proteins efficiently released the 8-hydroxyguanine opposite the pyrimidine from DNA and cleaved the AP site in a manner similar to bacterial and yeast enzymes. Genetic backgrounds in control of the repair of damaged DNA are involved in the susceptibility to cancer development. The hOgg1 gene has been mapped to region 3p26.2, a region showing loss of heterozygosity (LOH) in a variety of cancers. In particular, 3p25-p26 is a common LOH region in lung cancer.
Protein Aliases: 8-hydroxyguanine DNA glycosylase; 8-oxoguanine DNA-glycosylase 1; 8-oxoguanine-DNA-glycosylase; AP lyase; DNA-apurinic or apyrimidinic site lyase; HMMH; HOGG1; MUTM; N-glycosylase/DNA lyase; OGG1 type 1f; OGH1
Gene Aliases: HMMH; HOGG1; MMH; MUTM; OGG1; OGH1