Cat: IPD-X16129

Recombinant Mouse GYPA/CD235a Protein(HEK293) , hFc & His

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Analytical Data

  • Gene name

    GYPA/CD235a

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Glycophorin-A; GYPA; PAS-2; CD235a; GPA

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    N-hFc;C-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P14220

  • Expression Region

    M1-V108

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    60-66 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

Glycophorin A (GYPA), also known as CD235a, is a sialoglycoprotein primarily expressed on the surface of human red blood cells. It plays a crucial role in maintaining the structural integrity of the erythrocyte membrane and contributes to the negative charge of the red blood cell surface, which is vital for preventing cell aggregation. Research on GYPA/CD235a has garnered significant interest due to its implications in blood transfusion medicine, genetic blood disorders, and its potential as a target for therapeutic interventions. Additionally, variations in GYPA can serve as important markers for ethnic blood group typing and have been linked to certain diseases, including malaria, where the binding of the parasite to GYPA can influence susceptibility. The recombinant production of GYPA/CD235a, therefore, provides a valuable tool for studying its biological function and interactions, as well as for developing diagnostic reagents and therapeutic strategies. Advances in recombinant technology enable the generation of GYPA in sufficient quantities and with proper post-translational modifications, facilitating detailed investigations into its roles and applications in clinical settings. Researchers are exploring various expression systems, including mammalian cells, to ensure proper glycosylation patterns that are essential for the protein's functionality. Overall, the study of GYPA/CD235a not only enhances our understanding of erythrocyte biology but also opens avenues for novel therapeutic approaches in hematology and transfusion practices.

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