TargetMol

NEIL1 Protein, Human, Recombinant (His)

Product Code:
 
TAR-TMPY-02798
Product Group:
 
Recombinant Proteins
Supplier:
 
TargetMol
Regulatory Status:
 
RUO
Shipping:
 
cool pack
Storage:
 
-20°C
1 / 1
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TAR-TMPY-02798-50ug50ugEnquire
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  • Further Information
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Further Information

Bioactivity:
NEIL1 is a member of DNA glycosylases. DNA glycosylases are a family homologous to the bacterial Fpg/Nei family. They play a role in base excision repair which is the mechanism by which damaged bases in DNA are removed and replaced. The first step of this process is catalyzed by DNA glycosylases. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. NEIL1 functions in base excision repair of DNA damaged by oxidation or by mutagenic agents. It acts as a DNA glycosylase that recognizes and removes damaged bases. NEIL1 prefers to oxidized pyrimidines, such as thymine glycol, Formamidopyrimidine (Fapy), and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. It has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand and cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Molecular Weight:
45 kDa (predicted)
Purity:
98%

References

1.Zhang QM,et al. (2005) DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. DNA Repair. 4 (1): 71-9. 2.Mokkapati SK,et al. (2004) Stimulation of DNA glycosylase activity of OGG1 by NEIL1: functional collaboration between two human DNA glycosylases. Biochemistry. 43 (36): 11596-604. 3.Shinmura K,et al. (2005) Inactivating mutations of the human base excision repair gene NEIL1 in gastric cancer. Carcinogenesis. 25 (12): 2311-7. 4.Doublie S,et al. (2004) The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity. Proc Natl Acad. 101 (28): 10284-9.