Cat: IPD-X39116

Recombinant Human gABRq Protein,His

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Analytical Data

  • Gene name

    gABRq

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GABA(A) receptor subunit theta

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UN88

  • Expression Region

    Val66~Phe235

  • Molecular Weight

    24kDa

  • 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

gABRq recombinant proteins are derived from the gABRq gene, which plays a crucial role in various biological processes, particularly in signal transduction pathways. Research on this protein has gained prominence due to its involvement in cellular responses to environmental stimuli and its potential implications in diseases such as cancer and metabolic disorders. The ability to produce gABRq as a recombinant protein allows for in-depth functional studies, enabling scientists to investigate its structure-function relationships, post-translational modifications, and interaction with other cellular components. This research is pivotal not only for understanding the fundamental mechanisms of cell biology but also for the development of novel therapeutic strategies. By leveraging techniques such as genetic engineering and protein purification, researchers can generate large quantities of gABRq protein, facilitating both in vitro and in vivo studies that may reveal important insights into its role in disease pathology. Insights gained from gABRq studies may contribute to the identification of biomarkers for disease progression and aid in the design of targeted therapies that harness the unique properties of this protein. As such, ongoing research into gABRq recombinant proteins represents a significant area of scientific inquiry that holds promise for advancing our understanding of complex biological systems and improving health outcomes.

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