Glycerol inhibits binding affinity to Ni-NTA beads in immunoprecipitation.
>90%, by SDS-PAGE
Use in In vitro assay reported in scientific literature (PMID 24489103)
41.2 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Read Publications using NBP1-45318 in the following applications:
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
20 mM Tris-HCl Buffer (pH 8.0) Containing 100 mM NaCl, 40% Glycerol
>90%, by SDS-PAGE
Alternate Names for Recombinant Human OGG1 Protein
8-hydroxyguanine DNA glycosylase
8-oxoguanine DNA glycosylase
DNA-apurinic or apyrimidinic site lyase
OGG1, also known as 8-oxoguanine glycosylase, is a DNA glycosylase enzyme involved in base excision repair. This protein is the primary enzyme responsible for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which occurs as a result of exposure to reactive oxygen species (ROS). It has a beta lyase activity that nicks DNA 3' to the lesion. Recombinant human OGG1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.
You down with Ogg? Yeah, you know me 8-hydroxyguanine is a form of oxidative DNA damage where free radicals cause G:C to T:A transversions within the backbone. In E. coli, three DNA repair enzymes exist to prevent the mutagenic effects of 8-hydroxyguanine mutations. One of these enzymes,... Read full blog post.
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