Analytical Data
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基因名
GLRA3
- Application
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别名
Glycine receptor subunit alpha-3; GLRA3; Homo sapiens; Human; Chloride channel; Ion channel; Ligand-gated ion channel; Receptor
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种属
Human
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表达系统
Baculovirus
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标签
Strep
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O75311-1
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表达区间
M1–H460, del 343–418
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蛋白长度
Full Length of Isoform-1 Mature Protein
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.












