Cat: PA2000-1733

Recombinant Human GPC Protein,His

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Analytical Data

  • Gene name

    GPC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GPC;Glypican-6

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P04921

  • Expression Region

    1-57aa

  • AA Sequence

    ADPMWSTRSPNSTAWPLSLEPDPGMASASTTMHTTTIAEPDPGMSGWPDG RMETSTPTIMHHHHHH

  • Molecular Weight

    7 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

GPC (glypican) is a family of heparan sulfate proteoglycans that play pivotal roles in various cellular processes, including growth, differentiation, and regulation of cell signaling pathways. Research into GPC has gained momentum due to its involvement in pivotal biological functions and pathological conditions, such as cancer progression and development. GPCs are characterized by their attachment to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor, allowing them to interact with a range of ligands and modulate signaling pathways, such as those involving fibroblast growth factors (FGFs) and Wnt proteins. The role of GPCs in cancer biology is particularly notable, as they are often found to be upregulated in various tumor types, contributing to tumor growth, metastasis, and resistance to therapy. Thus, GPCs serve not only as potential biomarkers for cancer diagnosis and prognosis but also as promising therapeutic targets. Advances in recombinant protein technology have enabled the production and characterization of GPC proteins, facilitating deeper insights into their structure-function relationships and biological activities. Understanding the intricate mechanisms by which GPCs influence cellular processes is crucial for developing novel therapeutic strategies and improving patient outcomes in cancer treatment. As research continues to uncover the complexities of GPC interactions within the tumor microenvironment, the potential for innovative therapeutic interventions targeting GPCs is becoming increasingly viable. Overall, GPCs represent an exciting area of study in the realm of cell biology and oncology, with significant implications for both basic research and clinical applications.

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