Cat: IPD-X21963

Recombinant Mouse IgJ Protein(Yeast), His

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Analytical Data

  • Gene name

    IgJ

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Jchain; IgjImmunoglobulin J chain

  • Species

    Mouse

  • Source

    Yeast

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01592

  • Expression Region

    22-159aa

  • Molecular Weight

    17.7 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.

Quality inspection process

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Protein Description

The study of FCAR (Fc alpha receptor) and CD89 (CD89 antigen) recombinant proteins has gained significant attention in immunology and therapeutic research due to their roles in the immune response. FCAR is a cell surface receptor predominantly expressed on myeloid cells, facilitating the interaction between IgA-bound pathogens and immune cells, thus enhancing immune responses. CD89, as the receptor for IgA, plays a crucial role in mediating IgA antibody-dependent cellular phagocytosis and inflammation, contributing to the body’s defense mechanisms against infections. Understanding the structure and function of FCAR/CD89 recombinant proteins can provide insights into their signaling pathways and interaction with pathogens. This knowledge is essential for developing novel immunotherapeutic strategies for treating diseases where immune regulation is compromised, such as autoimmune disorders and infections. Additionally, the production of these recombinant proteins allows for detailed studies on receptor-ligand interactions, which can reveal potential targets for drug development. Overall, the characterization of FCAR/CD89 recombinant proteins holds promise for advancing our understanding of immune responses and creating innovative therapeutic interventions.

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