| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gABRa3 |
| Uniprot No | P34903 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-492aa |
| 氨基酸序列 | GESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYD NRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKF DGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTL PYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNK SVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFV IQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSL PKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALE MKKKTPAAPAKKTSTTFNIVGTTYPINLAKDTEFSTISKGAAPSASSTPT IIASPKATYVQDSPTETKTYNSVSKVDKISRIIFPVLFAIFNLVYWATYV NRESAIKGMIRKQ |
| 预测分子量 | 77 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是基于GABRA3重组蛋白研究领域常见方向的概括性文献示例(请注意，这些为模拟示例，非真实存在的论文，实际文献需通过学术数据库检索)：
1. **《Expression and functional characterization of recombinant human GABAA receptor α3 subunit in HEK293 cells》**
- 作者：Smith A, et al.
- 摘要：研究通过HEK293细胞系统成功表达GABRA3重组蛋白，并验证其与β2、γ2亚基共组装形成功能性GABA受体，电生理实验表明其对苯二氮䓬类药物的敏感性，为受体药理学研究提供模型。
2. **《Cryo-EM structure of the GABAA receptor α3β2γ2 subtype reveals subunit arrangement and benzodiazepine binding site》**
- 作者：Zhang Y, et al.
- 摘要：利用冷冻电镜解析GABRA3重组蛋白与β2、γ2亚基的复合物结构，揭示了α3亚基的跨膜域构象及苯二氮䓬结合位点的分子细节，为靶向药物设计提供结构基础。
3. **《Altered GABRA3 function in epilepsy-associated mutations: Insights from recombinant receptor studies》**
- 作者：Chen L, et al.
- 摘要：通过体外表达携带癫痫相关突变的GABRA3重组蛋白，发现特定突变导致受体脱敏速率加快和氯离子通道活性降低，提示α3亚基功能障碍在疾病中的潜在作用。
4. **《High-throughput screening identifies novel positive allosteric modulators of GABRA3-containing receptors》**
- 作者：Brown K, et al.
- 摘要：基于GABRA3重组蛋白构建高通量筛选平台，发现新型小分子变构调节剂可增强受体活性，可能为焦虑症治疗提供先导化合物。
**建议检索真实文献的关键词**：
- "GABRA3 recombinant protein expression"
- "GABAA receptor α3 subunit structure"
- "GABRA3 mutation functional analysis"
- "GABAAR α3 pharmacology"
可通过PubMed、Google Scholar或Web of Science检索最新研究，并筛选实验涉及重组蛋白技术的文献。
**Background of gABRa3 Recombinant Protein**
The gamma-aminobutyric acid type A receptor subunit alpha-3 (gABRa3 or GABRA3) is a critical component of GABAA receptors, ligand-gated ion channels that mediate inhibitory neurotransmission in the central nervous system. These receptors are pentameric complexes typically composed of combinations of α, β, γ, δ, ε, or θ subunits. The α3 subunit, encoded by the *GABRA3* gene, is predominantly expressed in brain regions such as the thalamus, cortex, and spinal cord, where it influences neuronal excitability, anxiety regulation, and motor control.
Recombinant gABRa3 protein is engineered *in vitro* using expression systems (e.g., mammalian or insect cells) to produce a purified, functional subunit for structural and pharmacological studies. This recombinant approach allows precise control over subunit composition, enabling researchers to investigate α3-specific receptor properties without interference from other GABAA subunits. The protein typically retains key structural features, including the extracellular N-terminal domain (responsible for ligand binding), four transmembrane helices, and intracellular loops involved in receptor trafficking and modulation.
Dysregulation of GABRA3 has been linked to neurodevelopmental disorders, epilepsy, and mood disorders. For example, mutations or altered expression of α3 subunits may disrupt inhibitory signaling, contributing to hyperexcitability or cognitive deficits. Recombinant gABRa3 is thus a vital tool for studying disease mechanisms, screening therapeutics (e.g., benzodiazepines or neurosteroids that target GABAA receptors), and designing subunit-selective drugs to minimize side effects. Its use in electrophysiology, binding assays, and structural biology (e.g., cryo-EM) continues to advance our understanding of GABAergic signaling and its therapeutic potential.
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