| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gABRq |
| Uniprot No | Q9UN88 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-632aa |
| 氨基酸序列 | MGIRGMLRAAVILLLIRTWLAEGNYPSPIPKFHFEFSSAVPEVVLNLFNCKNCANEAVVQKILDRVLSRYDVRLRPNFGGAPVPVRISIYVTSIEQISEMNMDYTITMFFHQTWKDSRLAYYETTLNLTLDYRMHEKLWVPDCYFLNSKDAFVHDVTVENRVFQLHPDGTVRYGIRLTTTAACSLDLHKFPMDKQACNLVVESYGYTVEDIILFWDDNGNAIHMTEELHIPQFTFLGRTITSKEVYFYTGSYIRLILKFQVQREVNSYLVQVYWPTVLTTITSWISFWMNYDSSAARVTIGLTSMLILTTIDSHLRDKLPNISCIKAIDIYILVCLFFVFLSLLEYVYINYLFYSRGPRRQPRRHRRPRRVIARYRYQQVVVGNVQDGLINVEDGVSSLPITPAQAPLASPESLGSLTSTSEQAQLATSESLSPLTSLSGQAPLATGESLSDLPSTSEQARHSYGVRFNGFQADDSIIPTEIRNRVEAHGHGVTHDHEDSNESLSSDERHGHGPSGKPMLHHGEKGVQEAGWDLDDNNDKSDCLAIKEQFKCDTNSTWGLNDDELMAHGQEKDSSSESEDSCPPSPGCSFTEGFSFDLFNPDYVPKVDKWSRFLFPLAFGLFNIVYWVYHMY |
| 预测分子量 | 71,9 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GABA A ρ(可能为用户所指的gABRq)重组蛋白研究的模拟参考文献示例，供参考：
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1. **文献名称**：*Heterologous Expression and Pharmacological Characterization of the Human GABA A ρ1 Receptor in HEK293 Cells*
**作者**：Wang, L. et al.
**摘要**：该研究成功在HEK293细胞中表达了人源GABA A ρ1重组蛋白，分析了其对GABA及类似激动剂的剂量反应，发现ρ1受体对经典激动剂敏感性较低，提示其独特的药理学特性。
2. **文献名称**：*Cryo-EM Structure of the Human GABA A ρ1 Homopentamer Reveals a Novel Gating Mechanism*
**作者**：Zhang, Y. et al.
**摘要**：通过冷冻电镜解析了GABA A ρ1重组受体的高分辨率结构，揭示了其同源五聚体组装模式及不同于其他GABA A亚型的离子通道门控机制。
3. **文献名称**：*Recombinant GABAρ Receptor as a Tool for High-Throughput Screening of Neuroactive Compounds*
**作者**：Johnson, R. et al.
**摘要**：开发了一种基于GABA A ρ2重组蛋白的高通量药物筛选平台，验证了其对神经活性化合物(如荷包牡丹碱)的特异性响应，为药物发现提供新工具。
4. **文献名称**：*Functional Characterization of Retina-Specific GABA A ρ Subunits Expressed in Xenopus Oocytes*
**作者**：Tanaka, K. et al.
**摘要**：利用非洲爪蟾卵母细胞表达系统研究GABA A ρ亚基重组蛋白的电生理特性，证实其在视网膜信号传递中的快速脱敏现象及潜在生理意义。
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**说明**：以上文献为模拟示例，实际引用需以真实出版物为准。若需精准文献，建议通过PubMed/Google Scholar以关键词“GABA A rho recombinant”“GABRR1 expression”等检索。
**Background of gABRq Recombinant Protein**
The gABRq recombinant protein is a engineered variant derived from the gamma-aminobutyric acid (GABA) receptor-associated protein (GABARAP) family, which plays a critical role in intracellular trafficking, autophagy, and receptor clustering. GABARAP proteins are ubiquitin-like modifiers involved in membrane transport processes, particularly in the delivery of GABAA receptors to synaptic membranes, thereby regulating neuronal inhibitory signaling. The "gABRq" designation likely reflects a specific isoform or modified form designed for enhanced stability, solubility, or functional specificity in experimental applications.
Recombinant gABRq is typically produced using heterologous expression systems, such as *E. coli* or mammalian cell cultures, followed by purification via affinity chromatography. Its engineered features may include tags (e.g., His-tag, GST-tag) to facilitate detection and purification. This protein is widely utilized in neuroscience and cell biology research to study autophagy mechanisms, GABA receptor dynamics, and protein-protein interactions. Its role in autophagy—a process linked to neurodegenerative diseases, cancer, and immune responses—has spurred interest in gABRq as a tool for probing disease mechanisms or screening therapeutic compounds.
Recent studies highlight its involvement in bridging autophagosomes with lysosomes and modulating mTOR signaling pathways. Additionally, gABRq's interaction with viral proteins or pathogen-derived molecules suggests potential applications in virology and infectious disease research. Despite its specialized functions, challenges remain in standardizing activity assays and ensuring batch-to-batch consistency, common hurdles in recombinant protein production. Ongoing work aims to optimize gABRq for *in vivo* studies, drug discovery, and structural biology, underscoring its versatility as a molecular tool in biomedical research.
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