Technical Data
NTH1 (E. coli Endonuclease III Homologue)
Oxygen radicals damage chromosonal DNA causing cell death and inducing mutations. Although a major focus of oxidatively damaged DNA has centered on the repair of 8-oxo-G, a number of other damaged DNA sites are created by free-radical attack on DNA. The human NTH1 repair protein is one enzyme that has been shown to act on a large number of these other oxidatively damaged DNA sites. A homologue of E. coli Endonuclease III, NTH is a DNA glycosylase with apurinic/apyrimidinic lyase activity. The NTH protein has broad substrate specificity, including numerous ring saturation and fragmentation products of pyrimidines. Research indicates NTH plays a crucial role in removal of oxidative base lesions in mitochondrial DNA.

Positive control: K562 cell extracts , Hela cell extracts.
PabIgGAffinity Purified
200ul-20CBlue IceHumanRabbit
Not determined
A peptide derived from the human NTH1.
Purified by affinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.05% sodium azide.
Specific for NTH1. Species crossreactivity: Reacts with human NTH1. There is sequence homology to mouse.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Aspinwall, R., Cloning and Characterization of a functional human homologue of Escherichia coli Endonuclease III. Proc. Natl. Acad. Sci. U.S.A., 94: 109-114, 1997. 2. Takao, M., Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage. Nucleic Acids Research, 26: 2917-2922, 1998.