Cat: IPD-X41798

Recombinant Rat Grpcb Protein (Yeast),His

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Analytical Data

  • Gene name

    Grpcb

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (GRP-CB)(Contiguous repeat polypeptide)(CRP)

  • Species

    Rat

  • Source

    Yeast

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P08462

  • Expression Region

    19-247aa

  • Molecular Weight

    27.2 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

Glycoprotein (Gp) is a fundamental component in various biological processes, playing crucial roles in cell signaling, immune responses, and pathogen interactions. Among the numerous glycoproteins, GpC, with its unique structural and functional characteristics, has garnered significant attention in recent years. The need for an in-depth understanding of GpC arises from its potential applications in vaccine development, therapeutic interventions, and diagnostic tools. The recombinant expression of GpC in suitable host systems allows researchers to study its structural biology, post-translational modifications, and interactions with other biomolecules. By producing GpC as a recombinant protein, scientists can generate sufficient quantities for biophysical and biochemical analyses, paving the way for insights into its functional mechanisms. Furthermore, the re-engineering of GpC holds promise for developing targeted therapies and novel vaccines, particularly in the context of infectious diseases and cancer. Overall, the study of recombinant GpC serves as a pivotal step in both fundamental research and the translation of findings into clinical applications.

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