Human OGG1, His Tag, E. coli

Catalog Number

LDG169PHE

Datasheet

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• Specifications

  • Species of Origin

    Human

    Expression System

    Escherichia coli

  • Affinity Tag

    His Tag (C-term)

    Storage Buffer

    Lyophilized from a 0.2 µm filtered solution of PBS, pH 7.4.

  • Purity

    >98% as determined by SDS-PAGE analysis.

    Molecular weight

    The protein has a calculated MW of 39.61 kDa.
    The protein migrates as 40 kDa under reducing condition (SDS-PAGE analysis).

  • Endotoxin Level

    <0.1 EU per 1 μg of the protein by the LAL method.

    Form

    Lyophilized

• Background

  • Background

    8-oxoguanine DNA glycosylase-1 (OGG1) is a major DNA glycosylase that plays a critical role in n base-excision repair (BER) of oxidative DNA damage to nuclear and mitochondrial DNA (mtDNA) to remove 7,8-dihydro-8-oxo-2′-deoxyguanosine (8-OH-dG). OGG1 is a 38.8 kDa protein containing 52 amino acid it found in bacterial, archaeal and eukaryotic species. OGG1 in DNA causes G:C to T:A transversions and, therefore, it could be responsible for mutations that lead to carcinogenesis.

    Synonyms

    8-oxoguanine DNA glycosylase

  • Uniprot ID

    # O15527 2

    Sequence Note

    Met1-Gly345

• Instruction

  • Reconstitution

    It is recommended to reconstitute the lyophilized protein in sterile H₂O to a concentration not less than 200 μg/mL and incubate the stock solution for at least 20 min to ensure sufficient re-dissolved.

    Shipping

    The product is shipped with polar packs. Upon receipt, store it immediately at -20°C or lower for long term storage.

  • Stability & Storage

    This product is stable after storage at:

    • -20°C for 12 months in lyophilized state from date of receipt.
    • -20°C or -80°C for 1 month under sterile conditions after reconstitution.

    Avoid repeated freeze/thaw cycles.

• Image

  

  SDS-PAGE analysis of recombinant human OGG1.

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• Datasheet & Documents

  Datasheet

  MSDS

  Manual

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Disclaimer：For Research Use or Further Manufacturing Only.