Cat: IPD-X41789

Recombinant Human PARP12 Protein ,His & Myc

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Analytical Data

  • Gene name

    PARP12

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (ADP-ribosyltransferase diphtheria toxin-like 12)(ARTD12)(Poly [ADP-ribose] polymerase 12)(PARP-12)(Zinc finger CCCH domain-containing protein 1)

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9H0J9

  • Expression Region

    1-701aa

  • Molecular Weight

    86.5 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

PARP12, a member of the poly(ADP-ribose) polymerase (PARP) family, has garnered significant interest in recent years due to its emerging roles in various cellular processes, including DNA damage response, immune regulation, and viral infection. Unlike its better-known relatives, such as PARP1, which is predominantly involved in the repair of single-strand DNA breaks, PARP12 exhibits distinct functions linked to post-translational modifications. Recent studies have revealed its capacity to modulate the immune system by regulating the activity of key signaling molecules and influencing inflammatory responses. Additionally, PARP12 has been implicated in the antiviral repertoire of host cells, suggesting that this protein could play a critical role in the defense against viral pathogens by facilitating the degradation of viral proteins. The functional diversity of PARP12 raises questions about its potential as a therapeutic target for diseases involving dysregulated immune responses or viral infections. This has sparked a growing interest in developing recombinant PARP12 proteins for comprehensive functional studies, which could unravel the mechanistic insights underpinning its activity and pave the way for novel drug development strategies. Understanding the precise molecular mechanisms by which PARP12 contributes to cellular homeostasis and immune surveillance is crucial for leveraging its potential in biomedical applications.

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