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F3174

Fpg Protein from Escherichia coli

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

Synonym(e):

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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10 μG

€ 884,00

€ 884,00


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Über diesen Artikel

CAS-Nummer:
EG-Nummer:
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)

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Unterstützung erhalten

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)

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Dieser Artikel
T0910N9284HPA006531
biological source

Escherichia coli

biological source

Escherichia coli

biological source

-

biological source

rabbit

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

-

technique(s)

nucleic acid detection: suitable

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

immunoblotting: 0.04-0.4 μg/mL, immunofluorescence: 0.25-2 μg/mL, immunohistochemistry: 1:50-1:200

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

form

buffered aqueous glycerol solution

form

essentially salt-free, lyophilized powder

form

lyophilized powder

form

buffered aqueous glycerol solution

mol wt

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

mol wt

11.7 kDa

mol wt

monomer 24000

mol wt

-

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.[1]
Fpg contains two domains separated by a flexible hinge.

Research area: Cell signaling

Application

Fpg Protein from Escherichia coli has been used for the assessment of DNA oxidative damage using comet assay.[2][3]

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.[1]
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.

Lagerklasse

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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Die Dokumentenbibliothek aufrufen

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
Marlies Wallner et al.
Cancer prevention research (Philadelphia, Pa.), 6(10), 1056-1063 (2013-08-29)
The bile pigment bilirubin is a known antioxidant and is associated with protection from cancer and cardiovascular disease (CVD) when present in too strong concentrations. Unconjugated bilirubin (UCB) might also possess anti-genotoxic potential by preventing oxidative damage to DNA. Moderately
E Seeberg et al.
Trends in biochemical sciences, 20(10), 391-397 (1995-10-01)
The base excision repair pathway has evolved to protect cells from the deleterious effects of endogenous DNA damage induced by hydrolysis, reactive oxygen species and other intracellular metabolites that modify DNA base structure. However, base excision repair is also important
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
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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