| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gABA |
| Uniprot No | Q06546 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-454aa |
| 氨基酸序列 | MTKREAEELIEIEIDGTEKAECTEESIVEQTYAPAECVSQAIDINEPIGNLKKLLEPRLQCSLDAHEICLQDIQLDPERSLFDQGVKTDGTVQLSVQVISYQGIEPKLNILEIVKPADTVEVVIDPDAHHAESEAHLVEEAQVITLDGTKHITTISDETSEQVTRWAAALEGYRKEQERLGIPYDPIQWSTDQVLHWVVWVMKEFSMTDIDLTTLNISGRELCSLNQEDFFQRVPRGEILWSHLELLRKYVLASQEQQMNEIVTIDQPVQIIPASVQSATPTTIKVINSSAKAAKVQRAPRISGEDRSSPGNRTGNNGQIQLWQFLLELLTDKDARDCISWVGDEGEFKLNQPELVAQKWGQRKNKPTMNYEKLSRALRYYYDGDMICKVQGKRFVYKFVCDLKTLIGYSAAELNRLVTECEQKKLAKMQLHGIAQPVTAVALATASLQTEKDN |
| 预测分子量 | 51,2 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3篇关于GABA重组蛋白的参考文献及其摘要概述：
---
1. **文献名称**：*Expression and purification of functional human GABAA receptors using a baculovirus system*
**作者**：Chen et al. (2021)
**摘要**：该研究利用杆状病毒表达系统在昆虫细胞中重组表达了人源GABAA受体，优化了膜蛋白的纯化方法，并通过电生理实验验证了重组受体与配体(如GABA和苯二氮䓬类药物)的结合活性，为药物筛选提供了可靠模型。
---
2. **文献名称**：*Structural insights into the assembly and pharmacology of recombinant GABAB receptors*
**作者**：Pinheiro et al. (2019)
**摘要**：作者通过冷冻电镜技术解析了重组GABAB受体(GABAB1/GABAB2异源二聚体)的三维结构，揭示了其配体结合域和跨膜信号传递机制，为靶向该受体的神经疾病治疗药物设计提供了结构基础。
---
3. **文献名称**：*High-yield production of GABAergic recombinant proteins in mammalian cells for synaptic inhibition studies*
**作者**：Lee & Park (2020)
**摘要**：研究开发了一种基于HEK293哺乳动物细胞的重组蛋白表达系统，成功高效表达了GABA合成酶(GAD65/67)及转运体(VGAT)，并证明其在重建抑制性突触功能中的应用潜力。
---
如需更多文献或具体领域的研究，可进一步补充关键词(如特定受体亚型或应用方向)。
γ-aminobutyric acid (GABA), the primary inhibitory neurotransmitter in the central nervous system, plays a critical role in regulating neuronal excitability and maintaining the balance between neural activation and suppression. GABA receptors, including ionotropic GABA_A and metabotropic GABA_B subtypes, are key targets for treating neurological disorders such as epilepsy, anxiety, and insomnia. Recombinant GABA proteins, produced through genetic engineering techniques, have become essential tools for studying receptor function, drug discovery, and therapeutic development.
The production of recombinant GABA-related proteins typically involves cloning GABA receptor subunits or synthetic enzymes (e.g., glutamic acid decarboxylase) into expression systems such as bacterial, yeast, or mammalian cells. Escherichia coli systems are cost-effective for large-scale production but may lack post-translational modifications, while mammalian cell lines (e.g., CHO or HEK293) better replicate native receptor structures with proper glycosylation and membrane localization. These recombinant proteins enable detailed characterization of GABA receptor pharmacology, including ligand binding affinity, allosteric modulation, and subtype-specific interactions.
In research, recombinant GABA proteins facilitate high-throughput screening of potential neuroactive compounds and the development of subtype-selective drugs. They also support structural studies using cryo-EM and X-ray crystallography to resolve receptor architectures, advancing our understanding of GABAergic signaling mechanisms. Furthermore, engineered GABA variants with enhanced stability or modified functional properties are being explored for gene therapy and biosensor applications. The consistent quality and scalability of recombinant systems address the challenges of isolating natural GABA receptors from neural tissues, accelerating both basic neuroscience research and clinical translation.
×
