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Merck

F3174

Fpg Protein from Escherichia coli

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

Sinónimos:

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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Número CAS:
78783-53-6
Número CE:
3.2.2.23 (BRENDA, IUBMB)
UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
MFCD02264758

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Nombre del producto

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

biological source

Escherichia coli

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.

P05523

application(s)

genomic analysis

shipped in

wet ice

storage temp.

−20°C

Quality Level

200

Gene Information

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

Application

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

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.
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.

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.
Fpg contains two domains separated by a flexible hinge.

Research area: Cell signaling

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.

Physical form

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

Clase de almacenamiento

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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Certificados de análisis (COA)

Lot/Batch Number
0000198140
0000198140
11190439
099M4153V
11161014

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Alwin B Mbene et al.
Journal of photochemistry and photobiology. B, Biology, 94(2), 131-137 (2008-12-23)
Phototherapy or biomodulation is a remarkable therapy that has become more popular and widely used in the treatment of a variety of medical conditions, such as slow to heal wounds, pain, soft tissue injuries and skin trauma. It has been
Derrik M Leach et al.
Mutagenesis, 28(5), 507-513 (2013-06-25)
Previously, we have reported the use of a recombinant adenovirus (Ad)-based host cell reactivation (HCR) assay to examine nucleotide excision repair (NER) of UVC-induced DNA lesions in several mammalian cell types. The recombinant non-replicating Ad expresses the Escherichia coli β-galactosidase
Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8
Sugahara M, et al.
The Embo Journal, 19(15), 3857-3869 (2000)
J Kain et al.
Mutagenesis, 27(4), 491-500 (2012-03-27)
Reliable methods for evaluation of toxicity from particles, such as manufactured nanoparticles, are needed. One promising tool is the comet assay, often used to measure DNA breaks (strand breaks and alkali-labile sites) as well as oxidatively damaged DNA, the latter
J Tchou et al.
The Journal of biological chemistry, 268(35), 26738-26744 (1993-12-15)
Fpg protein of Escherichia coli cleaves duplex DNA containing the oxidatively damaged base 8-oxo-7,8-dihydroguanine (Tchou, J., Kasai, H., Shibutani, S., Chung, M.-H., Laval, J., Grollman, A. P., and Nishimura, S. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4690-4694). This DNA
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