Cat: IPD-X31568

Recombinant Human DPP9 Protein (Baculovirus)

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Analytical Data

  • Gene name

    DPP9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DPRP2

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q86TI2-1

  • Expression Region

    M1-L863

  • Protein Length

    Full Length of Isoform-1

  • Molecular Weight

    98.3 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

Dipeptidyl peptidase 9 (DPP9) is a member of the prolyl oligopeptidase family, which plays a crucial role in various biological processes by regulating peptide substrates and modulating cellular signaling pathways. Recent studies have shown that DPP9 is involved in important physiological functions such as immune response, inflammation, and cell proliferation. Its dysregulation has been implicated in several diseases, including autoimmune disorders and cancer, making it a target of interest for therapeutic interventions. Additionally, DPP9 acts as an inhibitor of the activation of some immune pathways, and its unique substrate specificity offers insights into the regulatory mechanisms of cellular functions. The recombinant protein of DPP9 is utilized in various research applications, including biochemical assays, structural biology studies, and drug discovery efforts aimed at modulating its activity. Understanding the structure and function of DPP9 can provide valuable insights into its role in health and disease, offering potential avenues for novel therapeutic strategies. Given the increasing relevance of DPP9 in the context of disease pathology and treatment, the development and characterization of recombinant DPP9 proteins remains a critical area of research, enabling scientists to decipher its complex biological roles and establish its potential as a drug target.

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