Cat: PA1000-3722

Recombinant Human AREG Protein,His

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Analytical Data

  • Gene name

    AREG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    AREG;AREGB;Amphiregulin

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-6His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P15514

  • Expression Region

    101-198aa

  • AA Sequence

    SVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEFQNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMKTHSMIDSSLSK

  • Molecular Weight

    11.4 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

AREG, or Amphiregulin, is an epidermal growth factor (EGF) family member that plays a crucial role in various physiological processes, including cell proliferation, differentiation, and tissue repair. It has garnered significant interest in cancer research due to its involvement in tumor growth and progression, particularly in cancers such as breast and colon cancer. AREG is often overexpressed in various tumor types, promoting the activation of the EGF receptor (EGFR) signaling pathway, which is associated with enhanced cellular motility and invasion. In addition to its oncogenic properties, AREG is implicated in the development of the pulmonary system and wound healing processes, highlighting its dual role in both normal and pathological conditions. The study of AREG involves the exploration of its molecular mechanisms, regulatory pathways, and interactions with other growth factors and receptors. Understanding these elements is essential for developing targeted therapies, particularly in the context of EGFR inhibitors, which have shown efficacy in certain cancers but often face challenges due to resistance mechanisms that involve AREG. Continued research into AREG's structure-function relationships, its role in tumor microenvironments, and potential as a therapeutic target is vital for advancing both cancer treatment and regenerative medicine. This is further emphasized by the need for novel biomarkers in cancer diagnostics and prognostics, as AREG levels could serve as a predictive indicator of treatment response. Consequently, the investigation of AREG and its recombinant forms not only enhances our basic understanding of cell signaling and growth regulation but also opens avenues for innovative therapeutic strategies in oncology and other diseases where AREG is a critical player.

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