Cat: IPD-X38438

Recombinant Human EREG Protein,His & GST

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Analytical Data

  • Gene name

    EREG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    EPR; ER; Proepiregulin

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O14944

  • Expression Region

    Val63~Leu108

  • Molecular Weight

    36kDa

  • 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.

Quality inspection process

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Protein Description

EREG (Epiregulin) is a member of the epidermal growth factor (EGF) family, which plays a crucial role in cellular processes such as proliferation, differentiation, and survival. It is expressed in various tissues and has been implicated in several physiological and pathological conditions, including cancer, wound healing, and inflammatory diseases. Recent studies emphasize the importance of EREG in tumor progression and metastasis, highlighting its potential as a therapeutic target. The research surrounding the EREG recombinant protein focuses on understanding its structure-function relationships, signaling pathways, and interactions with other growth factors and receptors. Additionally, the role of EREG in modulating the tumor microenvironment and its impact on immune responses are emerging areas of interest. Investigating the recombinant form of EREG not only aids in elucidating its biological functions but also facilitates the development of novel therapeutic strategies, such as monoclonal antibodies or inhibitors, to combat EREG-related pathologies. As we delve deeper into the mechanisms of EREG, its implications in oncology and regenerative medicine could lead to innovative approaches in treating various diseases, making it a significant target for future research and clinical applications.

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