Analytical Data
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Gene name
OGG1
- Application
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Alternative Names
Including the following 2 domains: 8-oxoguanine DNA glycosylase (EC:3.2.2.-) DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.18) Short name: AP lyase
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15527
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Expression Region
1-345aa
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Molecular Weight
42.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. 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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
OGG1 (8-oxoguanine DNA glycosylase 1) is a crucial enzyme involved in the base excision repair pathway, responsible for the recognition and removal of 8-oxo-7,8-dihydroguanine (8-oxoG), a common oxidative DNA lesion resulting from various stressors, including oxidative stress and radiation. The accumulation of 8-oxoG is a significant contributor to mutagenesis and genomic instability, associated with various diseases, including cancer. Research on OGG1 has garnered attention due to its role in maintaining genomic integrity and its potential implications in disease mechanisms and aging. Mutations or dysregulation of OGG1 can lead to impaired repair of oxidative DNA damage, increasing susceptibility to tumor development. Furthermore, understanding the structural and functional dynamics of OGG1, including its binding and catalytic mechanisms, can provide insights into developing targeted therapeutic strategies for cancers characterized by DNA repair deficiencies. Recent studies have delved into the biochemical properties of OGG1, exploring its interactions with other proteins and how post-translational modifications influence its activity. The ongoing investigation into the OGG1 enzyme not only advances our understanding of DNA repair processes but also holds promise for novel interventions in diseases linked to oxidative DNA damage.
