F3174
Fpg Protein from Escherichia coli
≥90% (SDS-PAGE), buffered aqueous glycerol solution, >20,000 units/mg protein, suitable for genomic analysis
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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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生物来源
Escherichia coli
质量水平
重组
expressed in E. coli
检测方案
≥90% (SDS-PAGE)
形式
buffered aqueous glycerol solution
比活
>20,000 units/mg protein
分子量
30.2 kDa (269 amino acids, predicted from the nucleotide sequence)
组成
protein, 0.1- 0.3 mg/mL Bradford
储存条件
(Tightly closed)
技术
nucleic acid detection: suitable
UniProt登记号
应用
genomic analysis
运输
wet ice
储存温度
−20°C
基因信息
Escherichia coli CFT073 ... mutM(1038243)
Escherichia coli K12 ... mutM(946765)
一般描述
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
应用
Fpg Protein from Escherichia coli has been used for the assessment of DNA oxidative damage using comet assay.
生化/生理作用
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.
单位定义
One unit will cleave 50% of 0.5 pmol of double-stranded DNA oligomer substrate (8-oxoguanine−mutated) in 10 min at 25 °C.
外形
Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl.
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
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
The Embo Journal, 19(15), 3857-3869 (2000)
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
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
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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