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Human NEIL1 Protein expressed in Escherichia coli (E. coli) - ABIN667641
Dou, Mitra, Hazra: Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. in The Journal of biological chemistry 2003
Show all 2 references for ABIN667641
The abnormal expressions of NEIL1, NEIL2 (show NEIL2 Proteins), and NEIL3 (show NEIL3 Proteins) are involved in cancer through their association with the somatic mutation load.
NEIL1 and NEIL2 (show NEIL2 Proteins) cooperate with TDG (show TDG Proteins) during base excision: TDG (show TDG Proteins) occupies the abasic site and is displaced by NEILs, which further process the baseless sugar, thereby stimulating TDG (show TDG Proteins)-substrate turnover.
Findings suggesting that DNA glycosylase NEIL1 c.C844T is a defective allele.
NEIL1 forms a multiprotein complex with DNA replication proteins via its C-terminal domain, allowing recruitment at the replication fork.
Results show that YB-1 (show YBX1 Proteins) interferes negatively with the AP site DNA cleavage activity of both APE1 (show APEX1 Proteins) and NEIL1 for ssDNA and bubble structures.
Rad9 (show RAD9A Proteins) regulates base excision repair by controlling NEIL1 transcription.
genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase
The NEIL1 rs4462560 SNP may serve as a predictor of acute RIET and RP risk but not of overall survival.
one role for Neil3 (show NEIL3 Proteins) and NEIL1 is to repair DNA base damages in telomeres in vivo and that Neil3 (show NEIL3 Proteins) and Neil1 may function in quadruplex-mediated cellular events, such as gene regulation via removal of damaged bases from quadruplex DNA.
Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins.
Rad9 (show RAD9A Proteins) regulates base excision repair by controlling Neil1 protein stability in mouse embryonic stem cells.
Hypersensitivity to H2O2 caused by NEIL1 knockdown was more significant in S phase than in G1 phase, suggesting that NEIL1 has an important role during S phase.
Data indicate that maternal folate depletion during pregnancy and high-fat feeding from weaning altered gene expression of Ogg1 (show OGG1 Proteins), Neil1, Mutyh (show MUTYH Proteins) and Xrcc1 (show XRCC1 Proteins) in the brain of adult offspring.
binds to the BRCT domain of PARP-1 (show PARP1 Proteins)
Neil1 contributes to germline and somatic Huntington's disease CAG repeat (show CELF3 Proteins) expansion.
Endonuclease VIII-like 1 (NEIL1) promotes short-term spatial memory retention and protects from ischemic stroke-induced brain dysfunction and death in mice.
NEIL1 deficiency results in an increased susceptibility to obesity and related complications potentially by lowering the threshold for tolerance of cellular oxidative stress in neil1(-/-) mice.
NEIL1 is involved in nucleotide excision repair of(5'R)- and (5'S)-8,5'-cyclo-2'-deoxyadenosines, in addition to its function as a DNA glycosylase in base excision repair.
NEIL1 is a back-up glycosylase for NTH1 with unique substrate specificity and tissue-specific expression.
This gene is a member of the Nei endonuclease VIII-like gene family which encodes DNA glycosylases. The encoded enzyme participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines. Multiple transcript variants encoding different isoforms have been found for this gene.
endonuclease VIII-like 1
, DNA glycosylase/AP lyase Neil1
, DNA-(apurinic or apyrimidinic site) lyase Neil1
, endonuclease 8-like 1
, endonuclease VIII
, nei homolog 1
, nei-like protein 1