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F3174

Fpg Protein from Escherichia coli

≥90% (SDS-PAGE), buffered aqueous glycerol solution, >20,000 units/mg protein, suitable for genomic analysis

Synonym(s):

DNA-(apurinic or apyrimidinic site)lyase MutM (APlyase MutM), Fapy-DNAglycosylase, Formamidopyrimidine-DNA glycosylase, Fpg Protein from Escherichia coli, Recombinant, Fapy DNA glycosylase, Formamidopyrimidine DNA glycosylase, MutM

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About This Item

CAS Number:
EC Number:
UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
Form:
buffered aqueous glycerol solution
Assay:
≥90% (SDS-PAGE)
Biological source:
Escherichia coli
Recombinant:
expressed in E. coli
Mol wt:
30.2 kDa (269 amino acids, predicted from the nucleotide sequence)
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biological source

Escherichia coli

Quality Segment

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

>20,000 units/mg protein

mol wt

30.2 kDa (269 amino acids, predicted from the nucleotide sequence)

composition

protein, 0.1- 0.3 mg/mL Bradford

storage condition

(Tightly closed)

technique(s)

nucleic acid detection: suitable

UniProt accession no.

application(s)

genomic analysis

shipped in

wet ice

storage temp.

−20°C

Gene Information

Escherichia coli CFT073 ... mutM(1038243)
Escherichia coli K12 ... mutM(946765)

General description

Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme found in Escherichia coli, which contains one zinc atom. Proximal to its C-terminal, it contains a zinc-finger motif of CC/CC type.[1]
Fpg contains two domains separated by a flexible hinge.

Research area: Cell signaling

Application

Fpg Protein from Escherichia coli has been used for the assessment of DNA oxidative damage using comet assay.[2][3]

Biochem/physiol Actions

Formamidopyrimidine-DNA glycosylase (Fpg) cleaves double-stranded DNA containing the damaged base 8-oxo-7,8-dihydroguanine. It functions as an N-glycosylase and apurinic/apyrimidinic lyase.[1]
Fpg is a key enzyme in the DNA base excision repair pathway (BER). It catalyses the excision of a broad spectrum of modified purines. Fpg has both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose leaving both 5′- and 3′-phosphorylated ends in the DNA. The zinc finger motif at its C-terminus is responsible for the DNA binding and AP-lyase activity. In addition, its N-terminal proline acts as a nucleophile to produce a Schiff base intermediate that is essential for enzyme action.
Fpg specifically acts on 3′- and 5′-phosphodiester bonds.

Physical form

Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl.

Other Notes

One unit will cleave 50% of 0.5 pmol of double-stranded DNA oligomer substrate (8-oxoguanine−mutated) in 10 min at 25 °C.

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This Item
N9284T0910HPA006531
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

biological source

Escherichia coli

biological source

-

biological source

Escherichia coli

biological source

rabbit

technique(s)

nucleic acid detection: suitable

technique(s)

-

technique(s)

activity assay: suitable

technique(s)

immunoblotting: 0.04-0.4 μg/mL, immunofluorescence: 0.25-2 μg/mL, immunohistochemistry: 1:50-1:200

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

-

form

buffered aqueous glycerol solution

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

buffered aqueous glycerol solution

mol wt

30.2 kDa (269 amino acids, predicted from the nucleotide sequence)

mol wt

monomer 24000

mol wt

11.7 kDa

mol wt

-


Storage Class

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)



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