NEIL3 polyclonal, anti-human, mouse

Background:
DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5- OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair.

Other Names:
NEIL3; Endonuclease 8-like 3; DNA glycosylase FPG2; DNA glycosylase/AP lyase Neil3; Endonuclease VIII-like 3; Nei-like protein 3

Antigen Type: synthetic peptide

Antigen Type: NEIL3
Gene ID: 55247
Primary Accession: Q8TAT5