NEIL1
NEIL1 (nei like DNA glycosylase 1, also known as endonuclease 8-like 1, hFPG1, NEI1 and FPG1) is a bifunctional DNA glycosylase and AP lyase. It initiates base excision repair by removing oxidised pyrimidines from damaged DNA. Browse Assay Genie's current range of NEIL1 research reagents below, or read on for the biology behind the target.
NEIL1 is involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. It acts as a DNA glycosylase that recognises and removes damaged bases, with a preference for oxidised pyrimidines such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Activity towards 8-oxoguanine is marginal. The enzyme also has AP (apurinic/apyrimidinic) lyase activity: it cleaves the DNA backbone by beta-delta elimination, leaving a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
NEIL1 also shows glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. It binds 5-hydroxymethylcytosine (5hmC) specifically, which suggests it acts as a reader of this modified base. UniProt records the protein in the nucleus, on chromosomes and at the centrosome. Researchers studying the NEIL1 gene and protein can therefore look at repair activity in several cellular compartments.
NEIL1 belongs to the FPG family and is a member of the Nei endonuclease VIII-like gene family, which encodes DNA glycosylases. HGNC places it in the groups of DNA glycosylases and DNA-(apurinic or apyrimidinic site) lyases, and its previous name was nei endonuclease VIII-like 1 (E. coli). Multiple transcript variants encoding different isoforms have been reported. The mouse ortholog is Neil1.
NEIL1 starts base excision repair by removing damaged bases, mainly oxidised pyrimidines, making it a core target for studying this DNA repair pathway.
The enzyme recognises lesions such as thymine glycol, Fapy and 5-hydroxyuracil, which makes it relevant to work on DNA damaged by oxidation or mutagenic agents.
NEIL1 specifically binds 5-hydroxymethylcytosine, suggesting a role as a 5hmC reader and linking DNA repair enzymes to modified-cytosine biology.
NEIL1 has glycosylase/lyase activity towards mismatched uracil and thymine, particularly U:C and T:C mismatches, supporting research into non-canonical substrates.
NEIL1 is a DNA glycosylase that recognises and removes damaged bases, preferring oxidised pyrimidines such as thymine glycol, Fapy and 5-hydroxyuracil. Its AP lyase activity then nicks the DNA by beta-delta elimination, leaving a single-strand break with 3'- and 5'-phosphates.
NEIL1 is also called endonuclease 8-like 1, FLJ22402, hFPG1, NEI1 and FPG1. Its previous HGNC name was nei endonuclease VIII-like 1 (E. coli). Multiple transcript variants encoding different isoforms have been described, so check the datasheet of any product for its validated reactivity.
NEIL1 belongs to the FPG family and to the Nei endonuclease VIII-like gene family of DNA glycosylases, which also includes NEIL3. A mouse ortholog, Neil1, exists. Check the datasheet of any product for its validated reactivity.
Other members of the Nei endonuclease VIII-like family and related DNA repair targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q96FI4; product specifications from Assay Genie datasheets.