Cat: IPD-X38237

Recombinant Human CEA Protein,His

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Analytical Data

  • Gene name

    CEA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CD66E; CD66; CEACAM5; Carcinoembryonic Antigen-related Cell Adhesion Molecule 5; Carcinoembryonic Antigen

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P06731

  • Expression Region

    Ala566~Gly698

  • Molecular Weight

    16-25kDa

  • 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

Carcinoembryonic antigen (CEA) is a glycoprotein that is involved in cellular adhesion and is often overexpressed in various malignancies, particularly colorectal cancer. Its initial discovery dates back to the late 1960s, when it was recognized as a tumor marker in patients with cancer. Since then, the interest in CEA has expanded beyond its role as a diagnostic tool; researchers have been investigating its potential applications in targeted therapies and immunotherapy. The recombinant production of CEA has emerged as a crucial avenue for research, allowing scientists to produce large quantities of this protein for a variety of applications, including vaccine development, biomarker studies, and as a therapeutic target. The ability to produce recombinant CEA in host systems, such as bacteria or yeast, has paved the way for detailed structural and functional studies, enhancing our understanding of its biological roles and interactions in tumor progression. Additionally, modifications in the CEA structure can lead to improved characteristics for therapeutic use, making it a promising candidate for further investigation. Overall, the research on CEA recombinant proteins holds significant potential for advancing cancer diagnostics and therapies, contributing to the broader field of oncology.

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