Analytical Data
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Gene name
GLRA1
- Application
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Alternative Names
GLRA1；Glycine receptor subunit alpha-1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-457aa
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AA Sequence
MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ
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Molecular Weight
52.6kDa
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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 an integral component of the glycine receptor, a ligand-gated ion channel primarily found in the central nervous system. This receptor plays a critical role in inhibitory neurotransmission, particularly in the spinal cord and brainstem, by facilitating the passage of chloride ions into the neuron upon glycine binding. Mutations in the GLRA1 gene have been linked to several neurological disorders, including hyperekplexia, characterized by exaggerated startle responses and increased muscle tone. Research on recombinant GLRA1 proteins is vital for understanding the receptor's structure-function relationships, pharmacological properties, and the molecular basis of associated pathologies. By producing and characterizing these recombinant proteins, researchers can explore how different mutations affect glycine receptor activity, develop selective drugs to modulate receptor function, and potentially identify therapeutic targets for related disorders. Structural studies using techniques like X-ray crystallography or cryo-electron microscopy on these recombinant proteins can provide insights into the receptor's conformational dynamics, while electrophysiological assays can elucidate their functional properties. Overall, the ongoing investigation of GLRA1 recombinant proteins is crucial for advancing our understanding of glycinergic signaling and developing interventions for glycine receptor-related disorders.
