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Human NEIL1 Protein (His Tag)

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Human NEIL1 Protein Product Information
Synonym:FPG1, NEI1, hFPG1
Protein Construction:A DNA sequence encoding the human NEIL1 (AAH10876.1) (Met 1-Ser 390) was fused with a polyhistidine tag at the C-terminus and an initial Met at the N-terminus.
Expressed Host:E. coli
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Human NEIL1 Protein QC Testing
Purity:> 84 % as determined by SDS-PAGE
Endotoxin:Please contact us for more information.
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Met 1
Molecule Mass:The recombinant human NEIL1 comprises 400 amino acids and migrates as an approximately 45 kDa band as predicted in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile 50mM Tris, 150mM NaCl, pH 8.0
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Human NEIL1 Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Human NEIL1 Protein SDS-PAGE
Human NEIL1 Protein (His Tag) SDS-PAGE
Other NEIL1 Recombinant Protein Products
NEIL1 Background

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 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.

Human NEIL1 References
  • 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.
  • 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.
  • Shinmura K, et al. (2005) Inactivating mutations of the human base excision repair gene NEIL1 in gastric cancer. Carcinogenesis. 25 (12): 2311-7.
  • 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.
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    Catalog: 12695-H08E-20
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