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UNG Protein

This UNG protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN1068292

Quick Overview for UNG Protein (ABIN1068292)

Target

See all UNG Proteins
UNG (Uracil-DNA Glycosylase (UNG))

Biological Activity

Active

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E. coli

Source

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Escherichia coli (E. coli)
  • Characteristics

    10x UNG Reaction Buffer: 200mM Tris-HCl (pH 8.0 at 25°C), 10mM DTT and 10mM EDTA.

    Sterility

    Sterile filtered

    Unit Definition

    1 Unit of the enzyme catalyzes the release of 1 nanomole of uracil-containing DNA template in 60 min at 37°C.
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  • Comment

    Specific Activity: The Specific Activity was found to be 5U/μl.
    Reaction Conditions: 1X UNG Reaction Buffer, incubate at 37°C.UNG is active over a broad pH rabge with an optimum at pH-8.0, doesn't require divalent cation, and is inhibited by high ionic strength (>200mM). The abasic sites formed in DNA by UNG may be cleaved by heat, alkali-treatment or endonucleases that cleave specifically at abasic sites.
    Inhibition and Inactivation: Inactivated by heating at 95°C for 10min. Enzye activity is partially restored at temperatures lower than 55°C.

    Restrictions

    For Research Use only
  • Buffer

    UNG solution(5U/ul)in 10mM Tris-Hcl (pH-7.4 at 25°C), 50mM KCl, 1mM DTT, 0.1mM EDTA, 0.1 mg/ml BSA and 50% glycerol.

    Storage Comment

    Uracil DNA Glycosilase although stable at 15°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
  • Target

    UNG (Uracil-DNA Glycosylase (UNG))

    Alternative Name

    Uracil DNA Glycosylase

    Target Type

    Viral Protein

    Background

    E.Coli Uracil DNA Glycosilase (UNG) catalyses the release of free Uracil from Uracil-containing DNA. UNG efficiently hydrolyzes uracil from signle-stranded or double-stranded DNA, but not from oligomers (6 fewer bases).

    Pathways

    DNA Damage Repair, Production of Molecular Mediator of Immune Response
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