Analytical Data
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Gene name
GLRA1
- Application
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Alternative Names
(Glycine receptor 48 kDa subunit)(Glycine receptor strychnine-binding subunit)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23415
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Expression Region
29-250aa
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Molecular Weight
33.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Related Products
Protein Description
GLRA1 (Glycine Receptor Alpha 1) is a crucial component of the glycine receptor, a ligand-gated ion channel that primarily mediates inhibitory neurotransmission in the central nervous system. Understanding GLRA1 is essential, as mutations in this gene have been linked to various neurological disorders, including hyperekplexia, a condition characterized by exaggerated startle responses. The importance of studying GLRA1 recombinant proteins stems from their potential applications in both basic research and therapeutic development. By producing these proteins in a recombinant system, researchers can investigate their structural and functional properties, elucidate the mechanisms of glycine receptor signaling, and explore how specific mutations affect receptor function. Furthermore, recombinant GLRA1 proteins serve as valuable tools for drug discovery, assisting in the identification of compounds that can modulate receptor activity, which may lead to novel treatments for disorders involving dysregulated glycinergic signaling. Given the diverse roles of glycine receptors in synaptic transmission and their involvement in various neurophysiological processes, understanding GLRA1 through recombinant protein studies provides critical insights into the molecular basis of related diseases and the development of targeted therapies.
