Cat: PA2000-349DB

Recombinant E.coli GRa Protein,His

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Analytical Data

  • Gene name

    GRa

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GRa;Glycine receptor subunit alpha-1

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P13403

  • Expression Region

    25-190aa

  • AA Sequence

    AEGGDNQSSAVSDRASLFGLLSGGTGQGLGIGESVDLEMMGNTYRVERPTGNPDLLKIAIKASDGSYSEVGNVNVEEVIDTMKSMQRDEDIFLRALNKGETVEEAIEDVAQAEGLNSEQTLQLEDAVSAVASVVQDEMKVIDDVQQLEKDKQQLKDDIGFLTGERE

  • Molecular Weight

    19.9 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

GRa, a recombinant protein derived from specific genetic sequences, has garnered significant attention in the fields of molecular biology and biotechnology. Its study is primarily motivated by the potential applications in therapeutic development, vaccine formulation, and the understanding of cellular mechanisms. Recombinant proteins like GRa are engineered using techniques such as recombinant DNA technology, allowing for the production of proteins that mimic natural counterparts or exhibit enhanced properties. The production of GRa in host systems, such as bacteria or yeast, facilitates large-scale availability and cost-effectiveness. Furthermore, research on GRa focuses on its structural and functional characterization, providing insights into its biological activity and interactions with other biomolecules. Investigations into its immunogenicity and stability are crucial for applications in drug design and vaccine development. As the understanding of GRa expands, it holds promise for novel treatment strategies for various diseases, making it an integral subject of study in contemporary biomedical research. This research not only advances fundamental scientific knowledge but also paves the way for innovative therapeutic interventions.

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