Cat: IPD-X29518

Recombinant Human GPR87 Protein-VLP Protein (HEK293)

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Analytical Data

  • Gene name

    GPR87 Protein-VLP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GPR87; LG-protein coupled receptor 87; LG-protein coupled receptor 95; LGPR95; LFKSG78

  • Species

    Human

  • Source

    HEK293

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BY21

  • Expression Region

    M1-V358

  • Protein Length

    Full Length

  • 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

GPR87 is a member of the G-protein coupled receptor (GPCR) family, which plays a crucial role in various physiological processes and signaling pathways. Its expression is often upregulated in several cancer types, implicating it in tumorigenesis and making it a potential target for therapeutic intervention. Recent studies have shown that GPR87 can influence cellular proliferation, migration, and survival, suggesting its involvement in cancer progression. To explore the functional characteristics and therapeutic potential of GPR87, researchers have focused on the development of recombinant proteins, particularly using virus-like particles (VLPs) as delivery systems. VLPs offer several advantages, including their ability to present antigens in a native conformation, evoke strong immune responses, and enhance stability and delivery efficiency. Through the engineering of GPR87 Protein-VLP constructs, scientists aim to investigate the receptor's structural and functional properties, elucidate its signaling mechanisms, and evaluate its effectiveness as a vaccine or therapeutic target. This research not only contributes to the understanding of GPR87's role in cancer biology but also paves the way for innovative treatment strategies that could improve patient outcomes in malignancies associated with GPR87 dysregulation.

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