Cat: IPD-X28505

Recombinant Human GLRA3 Protein (Baculovirus),Strep

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Analytical Data

  • Gene name

    GLRA3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Glycine receptor subunit alpha-3; GLRA3; Homo sapiens; Human; Chloride channel; Ion channel; Ligand-gated ion channel; Receptor

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    Strep

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O75311-1

  • Expression Region

    M1–H460, del 343–418

  • Protein Length

    Full Length of Isoform-1 Mature Protein

  • 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

GLRA3, or Glycine Receptor Alpha-3, is a subunit of the inhibitory glycine receptor primarily found in the central nervous system, where it plays a crucial role in neurotransmission and the modulation of motor and sensory pathways. The receptor functions through the binding of glycine, leading to chloride ion influx and subsequent hyperpolarization of neurons. Abnormalities in GLRA3 expression or function have been implicated in various neurological disorders, including hyperekplexia, a condition characterized by exaggerated startle responses. The study of GLRA3 recombinant proteins has gained traction due to their potential therapeutic implications and their utility in deciphering the receptor's structure-function relationship. By generating and characterizing GLRA3 recombinant proteins, researchers aim to investigate the receptor's binding mechanisms, ion conductance properties, and interactions with various pharmacological agents. Furthermore, these studies could shed light on how mutations in GLRA3 contribute to disease manifestations. Understanding the detailed biochemistry of GLRA3 via recombinant protein studies not only enhances our knowledge of glycine receptor physiology but also aids in the development of targeted therapies for related neurological disorders. Through techniques such as crystallography, electrophysiology, and ligand-binding assays, scientists can obtain essential insights into the receptor's functional dynamics, ultimately contributing to advancements in neuropharmacology and therapeutic interventions.

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