Analytical Data
-
Gene name
OGG1
- Application
-
Alternative Names
OGG1;MMH;MUTM;OGH1;N-glycosylase/DNA lyase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O15527
-
Expression Region
1-345aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHTGSMPARALLPRRMGHRTLASTPALWASIP CPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTV YRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKF QGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVT YHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQ LRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQR DYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQCR HAQEPPAKRRKGSKGPEG
-
Molecular Weight
41 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
OGG1 (8-oxoguanine DNA glycosylase 1) is a critical enzyme involved in the base excision repair pathway, playing a pivotal role in maintaining genomic stability by recognizing and excising 8-oxo-7,8-dihydroguanine (8-oxoguanine), a common oxidative DNA lesion. The accumulation of such oxidative damage is associated with various pathological conditions, including cancer, neurodegenerative diseases, and aging. Understanding OGG1 function and regulation has garnered significant attention in recent years, as it serves as a key player in protecting cells from the deleterious effects of reactive oxygen species. Research has shown that polymorphisms in the OGG1 gene can influence an individual's susceptibility to oxidative stress-related diseases, making it a crucial focus for genetic and epidemiological studies. Additionally, the exploration of OGG1's interactions with other repair proteins and its potential post-translational modifications is essential for elucidating the broader mechanisms of DNA repair and cellular response to oxidative damage. Thus, ongoing investigations into OGG1 not only enhance our comprehension of cellular defense mechanisms but also hold promise for therapeutic interventions aimed at modulating its activity in disease contexts.
