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Merck

F3174

Sigma-Aldrich

Fpg Protein from Escherichia coli

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

别名:

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号:
MDL號碼:
分類程式碼代碼:
12352202
NACRES:
NA.32

生物源

Escherichia coli

品質等級

重組細胞

expressed in E. coli

化驗

≥90% (SDS-PAGE)

形狀

buffered aqueous glycerol solution

比活性

>20,000 units/mg protein

分子量

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

成份

protein, 0.1- 0.3 mg/mL Bradford

儲存條件

(Tightly closed)

技術

nucleic acid detection: suitable

UniProt登錄號

應用

genomic analysis

運輸包裝

wet ice

儲存溫度

−20°C

基因資訊

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

一般說明

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

應用

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.

單位定義

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

外觀

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

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 2

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

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


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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
Richard Meitern et al.
The Journal of experimental biology, 216(Pt 14), 2713-2721 (2013-04-13)
Oxidative stress (OS) is widely believed to be responsible for the generation of trade-offs in evolutionary ecology by means of constraining investment into a number of components of fitness. Yet, progress in understanding the true role of OS in ecology
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
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
Nikita A Kuznetsov et al.
Nucleic acids research, 40(15), 7384-7392 (2012-05-16)
Formamidopyrimidine-DNA glycosylase, Fpg protein from Escherichia coli, initiates base excision repair in DNA by removing a wide variety of oxidized lesions. In this study, we perform thermodynamic analysis of the multi-stage interaction of Fpg with specific DNA-substrates containing 7,8-dihydro-8-oxoguanosine (oxoG)

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