DNA in human cells is subjected to high rates of oxidative damage by reactive oxygen species. Oxidative DNA damage is deleterious as it can directly modify the genetic information of DNA. The 7,8-dihydro-8-oxoguanine (8-oxoG) adduct is the most common mutagenic lesion that can lead to G:C to T:A transversions; these damages are normally processed by the Base Excision Repair pathway. Single-stranded binding (SSB) proteins from the oligonucleotide domain family are involved in DNA repair processes, such as the detection of DNA damage and recruitment of repair proteins. Using immunofluorescence and ChIP experiments we show that hSSB1 (a new human SSB) levels increase in response to oxidative damage (H₂0₂) and that hSSB1 is localised at chromatin. Cells depleted of hSSB1 using siRNA are hypersensitive to oxidative damage. We show that hSSB1 forms a stable tetramer under oxidative conditions and has a stronger affinity for 8-oxo-G damaged ssDNA than non-damaged ssDNA. These data indicate that hSSB1 is required in the repair of oxidative DNA damage. As oxidative stress is associated with aging, cancer and Alzheimer’s disease, understanding the molecular mechanism of how cells repair oxidative DNA damage will be crucial in the development of potential therapeutic treatments.