| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gABRb2 |
| Uniprot No | P47870 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-244aa |
| 氨基酸序列 | SVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGY |
| 预测分子量 | 29.3 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. |
以下是关于GABRB2重组蛋白的模拟参考文献示例(非真实文献，供参考格式和方向)：
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1. **标题**: *"Functional characterization of recombinant GABRB2 subunits in neurotransmitter receptor assembly"*
**作者**: Smith A, et al.
**摘要**: 研究通过体外重组表达GABRB2蛋白，结合电生理学实验证明其与α和γ亚基共同形成功能性GABA_A受体，并揭示β2亚基对受体通道门控特性的调控作用。
2. **标题**: *"Cryo-EM structure of the human GABAA receptor β2 homopentamer"*
**作者**: Chen L, et al.
**摘要**: 利用冷冻电镜技术解析了重组GABRB2蛋白形成的同源五聚体结构，揭示了β2亚基的跨膜域和配体结合位点特征，为药物靶点设计提供结构基础。
3. **标题**: *"GABRB2 mutations and impaired recombinant protein trafficking in epilepsy"*
**作者**: Wang Y, et al.
**摘要**: 通过表达携带癫痫相关突变的GABRB2重组蛋白，发现部分突变导致蛋白错误折叠和内质网滞留，提示突变的致病机制可能与受体运输障碍相关。
4. **标题**: *"Optimization of recombinant GABRB2 expression in HEK293 cells for pharmacological screening"*
**作者**: Gonzalez R, et al.
**摘要**: 报道了在HEK293细胞中高效表达GABRB2重组蛋白的优化策略，并验证其在高通量药物筛选中的应用潜力。
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**注意**：以上为模拟文献，实际研究中请通过PubMed、Google Scholar或Web of Science等数据库检索真实文献(关键词：GABRB2 recombinant protein, GABA receptor beta2 subunit)。
The gamma-aminobutyric acid type A (GABAₐ) receptor beta 2 subunit (GABRB2) is a critical component of GABAₐ receptors, ligand-gated chloride channels that mediate inhibitory neurotransmission in the central nervous system. These receptors are pentameric complexes typically composed of α, β, and γ subunits, with the β2 subunit playing a pivotal role in receptor assembly, trafficking, and functional modulation. GABRB2-containing receptors contribute to synaptic and extrasynaptic inhibition, influencing neuronal excitability, anxiety regulation, and sleep patterns. Dysregulation of GABRB2 has been linked to neuropsychiatric disorders, including epilepsy, schizophrenia, and mood disorders, highlighting its therapeutic relevance.
Recombinant GABRB2 protein is engineered using heterologous expression systems, such as mammalian HEK293 or insect cells, to produce purified subunits for structural and functional studies. This approach enables precise investigation of β2 subunit interactions with ligands, allosteric modulators (e.g., benzodiazepines), and other receptor subunits. Recombinant technology also facilitates the study of disease-associated mutations, allowing researchers to dissect their effects on receptor kinetics, surface expression, and pharmacology. Recent structural studies using cryo-EM and X-ray crystallography have leveraged recombinant GABRB2 to resolve binding sites for GABA and neurosteroids, advancing drug discovery for targeted neuromodulation. Additionally, recombinant proteins serve as antigens for antibody development in diagnostic applications. The ability to produce homogenous GABRB2 protein supports high-throughput screening of novel therapeutics aiming to restore GABAergic signaling imbalances in neurological diseases, while minimizing off-target effects associated with traditional GABAₐ receptor drugs.
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