Cat: IPD-X37354

Recombinant Human PARP2 Protein (Baculovirus),His

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Analytical Data

  • Gene name

    PARP2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Poly [ADP-ribose] polymerase 2; ADP-ribosyltransferase diphtheria toxin-like 2; DNA ADP-ribosyltransferase PARP2; NAD(+) ADP-ribosyltransferase 2; ADPRT-2; pADPRT-2; EC:2.4.2.30; ADPRT2; ADPRTL2

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    N-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UGN5

  • Expression Region

    M1-W583

  • Protein Length

    Full Length

  • Molecular Weight

    71.6 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.

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Protein Description

PARP2 (Poly(ADP-ribose) polymerase 2) is a member of the PARP family of enzymes, which play a crucial role in cellular responses to DNA damage and stress, particularly through the post-translational modification of proteins via poly(ADP-ribosyl)ation. Unlike its closely related counterpart PARP1, PARP2 exhibits distinct functions and regulatory mechanisms that contribute to genomic stability and cellular survival. The study of PARP2 has gained significant attention due to its implications in cancer biology; aberrations in its expression or activity can affect tumor progression and response to therapies. Additionally, PARP2 is implicated in various physiological processes, including DNA repair, regulation of gene expression, and modulation of apoptosis. Given the therapeutic potential of targeting PARP enzymes in cancer treatment, the development of detailed structural and functional insights into PARP2 is paramount. Recombinant protein studies of PARP2 allow researchers to elucidate its enzymatic activity, interaction with DNA, and role in the PARP pathway, thus providing valuable information for potential drug development and understanding its contribution to disease mechanisms. These investigations enhance our understanding of PARP2's biological functions and pave the way for novel therapeutic strategies that exploit its activities in cancer and other diseases characterized by DNA repair deficiencies.

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