Search Thermo Fisher Scientific
Search Thermo Fisher Scientific
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.
bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase; Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase; DNA glycoslyase/AP lyase; DNA glycosylase/AP lyase; Endonuclease III-like protein 1; FAP3; hNTH1; nth (endonuclease III)-like 1 (E.coli); nth endonuclease III-like 1; Nth1; NTHL 1; Nthl1; nth-like DNA glycosylase 1; OCTS 3; OCTS3; thymine glycol DNA glycosylase/AP lyase
100 µL
150 µL
100 µL
150 µL
100 µL
200 µL
100 µL
100 µg
100 µL
200 µL
200 µL
200 µL
200 µL
200 µL
200 µL
Searching for an antibody we don't offer? We make custom antibodies for specific targets, species and applications.
More than 18,000 custom antibodies created so far.
Talk to a specialist nowIf an Invitrogen™ antibody doesn't perform as described on our website or datasheet,we'll replace the product at no cost to you, or provide you with a credit for a future purchase.*
Learn moreGet expert recommendations for common problems or connect directly with an on staff expert for technical assistance related to applications, equipment and general product use.
Contact tech support