Cat: IPD-X16747

Recombinant Cynomolgus uPAR Protein(HEK293) , hFc

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Analytical Data

  • Gene name

    uPAR

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    U-PAR; uPAR; CD87; PLAUR; MO3; UPAR

  • Species

    Cynomolgus

  • Source

    HEK293

  • Tag

    C-hFc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9GK78

  • Expression Region

    L23-R303

  • Molecular Weight

    65-95 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

uPAR, or the Urokinase Plasminogen Activator Receptor, is a cell surface receptor that plays a crucial role in various physiological and pathological processes, including cell migration, proliferation, and tissue remodeling. It is primarily involved in the plasminogen activation pathway, linking the fibrinolytic system with cellular signaling cascades. Research has shown that uPAR is overexpressed in several types of cancers, contributing to tumor progression, metastasis, and poor prognosis. Given its significant role in tumor biology, uPAR has emerged as a promising target for therapeutic interventions. The development of recombinant uPAR proteins serves as a critical tool for investigating its functional mechanisms and developing uPAR-targeted therapies. These recombinant proteins can be used in various applications, including drug screening, antibody generation, and as potential biomarkers for disease progression. Understanding the structure and function of uPAR through recombinant techniques can also provide insights into designing inhibitors that disrupt its interaction with ligands, thus potentially reducing cancer metastasis and improving treatment outcomes. The ongoing research around uPAR and its recombinant forms is crucial for advancing our knowledge of tumor biology and developing innovative therapeutic strategies.

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