Cat: IPD-X29644

Recombinant Human Podoplanin Protein (HEK293),hFc

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Analytical Data

  • Gene name

    Podoplanin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Podoplanin; Aggrus; Glycoprotein 36; Gp36; PA2.26 Antigen; T1-Alpha; T1A; PDPN; GP36

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-hFc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q86YL7-1

  • Expression Region

    A23-L131

  • Molecular Weight

    60-70 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

Podoplanin is a type I transmembrane glycoprotein that plays a crucial role in various physiological and pathological processes, particularly in lymphangiogenesis, tumor progression, and immune response modulation. Initially discovered as a marker for lymphatic endothelium, podoplanin is also expressed in various tissues and associated with several types of cancer, where it contributes to cancer cell migration, invasion, and metastasis. Its unique structural features, including an O-glycosylated mucin-like domain, facilitate interactions with specific receptors, such as C-type lectin receptors, influencing cell behavior and signaling pathways. Research into recombinant podoplanin protein has gained momentum due to its potential applications in diagnostic and therapeutic settings. As a target for cancer immunotherapy and a tool for studying lymphatic system biology, recombinant podoplanin can be utilized to develop novel vaccines or therapeutic agents aimed at modulating immune responses. Additionally, understanding the biochemical properties and functional roles of podoplanin through recombinant technology can provide insights into its mechanisms in tumor biology and lymphatic vessel development. Consequently, the study of podoplanin-focused recombinant proteins is integral to advancing cancer research and developing effective strategies for disease management.

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