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anti-Rat (Rattus) NEIL3 Antibodies:
anti-Human NEIL3 Antibodies:
anti-Mouse (Murine) NEIL3 Antibodies:
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This study identifies the NEIL3 promoter possessing a G-rich element that can adopt a G4 fold, and when 8-oxo-7,8-dihydroguanine is incorporated, the sequence can lock into a more stable G4 fold via recruitment of the fifth track of Gs.
Results suggest a novel role for the DNA glycosylase Neil3 in atherogenesis in balancing lipid metabolism and macrophage function, potentially independently of genome-wide canonical base excision repair of oxidative DNA damage.
NEIL3 protects genome stability through targeted repair of oxidative damage in telomeres during S/G2 phase.
NEIL3-dependent modulation of DNA methylation regulates cardiac fibroblast proliferation and thereby affects extracellular matrix modulation after myocardial infarction.
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.
These findings demonstrate that deficiency in NEIL3 is associated with increased lymphocyte apoptosis, autoantibodies, and predisposition to autoimmunity.
SNPs in NEIL3 are associated with impulsivity in Native American sample.
Single nucleotide polymorphism (SNP) rs142310826 near the NEIL3 gene showed a genome-wide significant interaction with caffeine consumption .There was no gender difference for this interaction (P = 0.64 for heterogeneity). NEIL3, a gene belonging to the base excision DNA repair pathway, encodes a DNA glycosylase that recognizes and removes lesions produced by oxidative stress.
The abnormal expressions of NEIL1, NEIL2, and NEIL3 are involved in cancer through their association with the somatic mutation load.
NEIL3 rs12645561 SNP TT genotype was associated with increased risk of myocardial infarction.
Polymorphisms within FLT3, EGFR, NEIL3, and ALOX5 may contribute to the occurrence of GBM.
Results show that the base excision and strand incision activities of NEIL3 exhibited a non-concerted action, indicating that NEIL3 mainly operates as a monofunctional DNA glycosylase.
one role for Neil3 and NEIL1 is to repair DNA base damages in telomeres in vivo and that Neil3 and Neil1 may function in quadruplex-mediated cellular events, such as gene regulation via removal of damaged bases from quadruplex DNA.
Here we report the construction of bicistronic expression vectors for expressing in Escherichia coli the full-length mouse Neil3 (MmuNeil3), its glycosylase domain (MmuNeil3Delta324), as well as the glycosylase domain of human Neil3 (NEIL3Delta324).
both the transcription and protein levels of hNEIL3 fluctuated during the cell cycle
NEIL3 partially rescues an E. coli nth nei mutant from hydrogen peroxide sensitivity. Taken together, repair of certain base damage including base loss in ssDNA may be mediated by NEIL3.
hFPG1 and hFPG2 repair 8-oxoguanine and other DNA oxidation products. (hFPG1 and hFPG2)
Data suggest that neurogenesis induced by Neil3 repair of oxidative DNA damage protects against prion disease during the clinical phase.
Structural insight into the substrate specificity and marked preference of Neil3 for ssDNA.
Our data support the involvement of Neil3 in removal of replication blocks in proliferating cells.
Neil3-dependent repair of oxidative DNA damage in neural stem/progenitor cells is required for maintenance of adult neurogenesis to counteract the age-associated deterioration of cognitive performance.
Neil3 exercises a highly specialized function through accurate molecular repair of DNA in rapidly proliferating cells
Neil3 plays a role in repairing 2,6-diamino-4-hydroxy-5-formamidopyrimidine in vivo.
NEIL3 is localized in the nuclei; Neil3 mRNA was selectively expressed in thymus, spleen and bone marrow
NEIL3 is specifically expressed in brain areas where neurogenesis takes place during development and that its expression is tightly regulated both temporally and spatially. NEIL3 seems to be upregulated in tumor tissues compared to normal tissues.
NEIL3 belongs to a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction (Bandaru et al., 2002
endonuclease VIII-like 3
, nei like 3
, nei endonuclease VIII-like 3 (E. coli)
, nei endonuclease VIII-like 3
, DNA glycosylase FPG2
, DNA glycosylase hFPG2
, DNA glycosylase/AP lyase Neil3
, endonuclease 8-like 3
, nei-like protein 3