Description:
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. |
| Type | Isotype | Clone | Grade |
| Pab | IgG | | Affinity Purified |
|
| Size | | Storage | Shipping | Source | Host |
| 200ul | | -20°C | Blue Ice | Human | Rabbit |
|
| Concentration: |
| As reported |
| Immunogen: |
| A peptide derived from the human NTH1. |
| Purity: |
| Purified by affinity chromatography. |
| Form |
| Supplied as a liquid in PBS, pH 7.2, 0.05% sodium azide. |
| Specificity: |
| 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. |
|