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化学文摘社编号:
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
Quality Level
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
Fpg contains two domains separated by a flexible hinge.
Research area: Cell signaling
Research area: Cell signaling
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.
Application
Fpg Protein from Escherichia coli has been used for the assessment of DNA oxidative damage using comet assay.
Biochem/physiol Actions
Fpg specifically acts on 3′- and 5′-phosphodiester bonds.
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.
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.
存储类别
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)
法规信息
常规特殊物品
此项目有
Kim Jantzen et al.
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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
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
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)
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