Anti-Ogg1 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The Ogg1 protein also known as 8-oxoguanine DNA glycosylase or Oggone is an important repair enzyme responsible for the removal of oxidatively damaged guanine bases from DNA. This protein has a molecular mass of approximately 39 kDa and is expressed in various tissues including the brain liver and lungs. Ogg1 is significant in maintaining genome integrity by excising 8-oxoguanine lesions which can otherwise lead to mutations if left unrepaired.

Biological function summary

Within cellular processes Ogg1 functions primarily to maintain DNA stability by participating in the base excision repair pathway. This protein operates as part of a complex that identifies and excises damaged bases subsequently facilitating the refilling and ligation of the resulting single-strand DNA breaks. The removal of oxidized guanine by Ogg1 is important in preventing mutagenesis apoptosis and tumorigenesis.

Pathways

The involvement of Ogg1 can be predominantly seen in the DNA repair and oxidative stress response pathways. Within these pathways Ogg1 is closely related to other proteins such as MutYH and APE1 which work collaboratively to ensure DNA integrity. Coordinating with other repair enzymes Ogg1 therefore helps to counteract the effects of reactive oxygen species-induced damage on the genetic material.

Associated diseases and disorders

Studies link abnormal Ogg1 activity to increased risk for cancer and neurodegenerative diseases. Mutations or deficiencies in the Ogg1 protein can result in an accumulation of 8-oxoguanine promoting genomic instability and potentially facilitating cancer development. Additionally the accumulation of oxidative DNA damage is associated with Alzheimer's disease where Ogg1 interaction with proteins like APE1 can influence disease progression by affecting the efficiency of DNA repair mechanisms.