| Product Name |
Human 8-oxoguanine DNA Glycosylase (hOGG1) |
| Overview |
Human 8-oxoguanine DNA glycosylase (hOGG1) is a key DNA repair enzyme that initiates the base excision repair (BER) pathway by recognizing and excising 8-oxoguanine (8-oxoG), a major mutagenic lesion resulting from oxidative DNA damage. hOGG1 specifically removes 8-oxoG paired with cytosine, preventing G:C to T:A transversions and maintaining genomic stability. In addition to its glycosylase activity, hOGG1 also possesses AP lyase activity, cleaving the DNA backbone at the abasic site generated after base removal.
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| Gene/Protein Names |
- Gene: OGG1
- UniProt: O15527
- Other Names: hOGG1, 8-oxoguanine DNA glycosylase, OGG1 DNA glycosylase
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| Molecular Weight |
~38 kDa (monomer) |
| Key Features |
- Recognizes and excises 8-oxoguanine lesions from DNA
- Initiates base excision repair (BER) pathway
- Exhibits both glycosylase and AP lyase activities
- Prevents mutagenic G:C to T:A transversions
- Essential for cellular defense against oxidative DNA damage
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| Applications |
- In vitro DNA repair assays
- Oxidative DNA damage and repair studies
- Genotoxicity and mutagenesis research
- Functional studies of the base excision repair pathway
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| Source |
Recombinant protein expressed in E. coli |
| Quality Control |
- Purity >95% by SDS-PAGE
- Validated for 8-oxoG excision and AP lyase activities
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| Formulation |
20 mM Tris-HCl, 100 mM NaCl, 1 mM DTT, 10% glycerol, pH 7.5 |
| Storage |
-80 °C (long-term); avoid repeated freeze-thaw cycles |
| References |
- Bruner, S.D., et al. "Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA." Nature. 2000; 403(6772): 859-866.
- Boiteux, S., Radicella, J.P. "The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis." Arch Biochem Biophys. 2000; 377(1): 1-8.
- UniProt: O15527
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