Cat: PA1000-3417

Recombinant E.coli ung Protein,His

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Analytical Data

  • Gene name

    ung

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ung;DGU;Uracil-DNA glycosylase

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P12295

  • Expression Region

    1-229aa

  • AA Sequence

    MGSSHHHHHH SSGLVPRGSH MGSMANELTW HDVLAEEKQQ PYFLNTLQTV ASERQSGVTI YPPQKDVFNA FRFTELGDVK VVILGQDPYH GPGQAHGLAF SVRPGIAIPP SLLNMYKELE NTIPGFTRPN HGYLESWARQ GVLLLNTVLT VRAGQAHSHA SLGWETFTDK VISLINQHRE GVVFLLWGSH AQKKGAIIDK QRHHVLKAPH PSPLSAHRGF FGCNHFVLAN QWLEQRGETP IDWMPVLPAE SE

  • Molecular Weight

    28 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

UNG (Uracil N-glycosylase) is a critical enzyme involved in the base excision repair pathway, recognizing and removing uracil residues from DNA. The presence of uracil in DNA can arise from the deamination of cytosine or misincorporation during DNA replication, leading to mutations if left unrepaired. Research on UNG has gained significance due to its implications in maintaining genomic stability and preventing various diseases, including cancer. In addition, UNG plays a pivotal role in the immune system by modulating somatic hypermutation and class switch recombination in B lymphocytes, processes essential for generating diverse antibodies. The recombinant form of UNG has been extensively studied for its enzymatic properties, and its structural analysis helps in understanding its catalytic mechanism and interactions with DNA substrates. Moreover, recombinant UNG is being explored for therapeutic applications, including the development of targeted cancer treatments and novel diagnostic tools for detecting uracil misincorporation in DNA, thus representing an essential area of molecular biology research with significant clinical implications.

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