Fpg (also known as Formamidopyrimidine DNA glycosylase, Mut M, FAPY DNA Glycosylase, and 8-oxoguanine DNA glycosylase) participates in the base-excision (BER) pathway of DNA repair enzymes and acts both as a N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged purines from double stranded DNA, generating an apurinic/apyrimidinic (AP site). The AP-lyase activity cleaves both the 3′ and 5′ phosphodiester bonds at the AP site, producing a 1 base gap in the DNA and 3′ and 5′ phosphate termini. Bases recognized and removed by Fpg include 7, 8-dihydro-8-oxoguanine (8-oxoguanine), 8-oxoadenine, fapy-guanine, methy-fapy-guanine, fapy-adenine, aflatoxin B1-fapy-guanine, 5-hydroxy-cytosine and 5-hydroxy-uracil (1,2).
Source of ProteinA recombinant E. coli strain carrying the cloned fpg gene.
Supplied in20 mM Tris-HCl50 mM NaCl1.0 mM DTT0.1 mM EDTA50% glycerolpH 8.0 @ 25°C
Supplied WithB0130 (10X Yellow Buffer)10X Yellow Buffer (B0130):100 mM Bis-Tris-Propane100 mM MgCl210 mM DTTpH 7.0 @ 25°C
Unit DefinitionOne unit is defined as the amount of enzyme required to cleave 1 pmol of a 34mer oligo-nucleotide duplex containing an 8-oxoguanine base paired with a cysteine in 1 hour at 37°C in a total reaction volume of 10µl in reaction buffer.
