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|Tested species reactivity||Human, Mouse, 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|
|Tested Applications||Dilution *|
|Flow Cytometry (Flow)||Assay-Dependent|
|Immunohistochemistry (Frozen) (IHC (F))||1:25-1:100|
|Immunohistochemistry (Paraffin) (IHC (P))||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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
HMMH; HOGG1; MMH; MUTM; OGG1; OGH1