Fpg, E. coli

Description

Description:
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).

Applications:

• DNA Nicking
• DNA Repair
• Nick Translation

Source:
A recombinant E. coli strain carrying the cloned fpg gene

Specific Activity: 20,513 U/mg

Supplied With:
10X Fpg Buffer
Incubate at 37°C

10X Fpg Buffer:
100 mM Bis-Tris-Propane
100 mM MgCl₂
10 mM DTT
1 mg/ml BSA
pH 7.0 @ 25°C

Supplied in:
20 mM Tris-HCl
50 mM NaCl
1.0 mM DTT
0.1 mM EDTA
50% glycerol
pH 8.0 @ 25°C

Unit Definition:
One 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 cytosine in 1 hour at 37°C in a total reaction volume of 10µl in reaction buffer.

Recommended Storage Condition: -20°C

References:
1. Tchou, J. et al. (1994) Substrate specificity of Fpg protein. J. Biol. Chem., 269, 15318-15324.
2. Hatahet, Z. et al. (1994) New substrates for old enzymes. J. Biol. Chem., 269, 18814-18820.

Additional information

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