F3174
Fpg Protein from Escherichia coli
≥90% (SDS-PAGE), buffered aqueous glycerol solution, >20,000 units/mg protein, suitable for genomic analysis
동의어(들):
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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크기 선택
제품정보 (DICE 배송 시 비용 별도)
CAS 번호:
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)
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.
application(s)
genomic analysis
shipped in
wet ice
storage temp.
−20°C
Quality Level
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.
Fpg contains two domains separated by a flexible hinge.
Research area: Cell signaling
Research area: Cell signaling
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.
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.
저장 등급
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)
Therese Bergström et al.
Mutagenesis, 27(4), 511-517 (2012-04-03)
Vitamins with antioxidant properties have the ability to act as pro-oxidants, inducing oxidative damage and oxidative stress as opposed to preventing it. While vitamin supplements are commonly consumed, the scientific evidence for their health beneficial effects is inconclusive. In fact
Kim Jantzen et al.
Mutagenesis, 27(6), 693-701 (2012-08-08)
Studies in mono-culture of cells have shown that diesel exhaust particles (DEPs) increase the production of reactive oxygen species (ROS) and oxidative stress-related damage to DNA. However, the level of particle-generated genotoxicity may depend on interplay between different cell types
Lotte Frigaard Mandsberg et al.
FEMS microbiology letters, 324(1), 28-37 (2011-11-19)
Prevention and correction of oxidative DNA lesions in Pseudomonas aeruginosa is ensured by the DNA oxidative repair system (GO). Single inactivation of mutT, mutY and mutM involved in GO led to elevated mutation rates (MRs) that correlated to increased development
Yan Qi et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(4), 1086-1091 (2012-01-06)
Base excision repair of genotoxic nucleobase lesions in the genome is critically dependent upon the ability of DNA glycosylases to locate rare sites of damage embedded in a vast excess of undamaged DNA, using only thermal energy to fuel the
Lykke Forchhammer et al.
Mutagenesis, 27(6), 665-672 (2012-07-31)
There are substantial inter-laboratory variations in the levels of DNA damage measured by the comet assay. The aim of this study was to investigate whether adherence to a standard comet assay protocol would reduce inter-laboratory variation in reported values of
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