| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GABARAP |
| Uniprot No | Q6IAW1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-117aa |
| 氨基酸序列 | MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYL VPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHE EDFFLYIAYSDESVYGL |
| 预测分子量 | 14 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GABARAP重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Cloning and expression of γ-aminobutyric acid type A receptor-associated protein (GABARAP)"*
**作者**：Sagiv Y., Legesse-Miller A., et al.
**摘要**：该研究首次报道了人源GABARAP基因的克隆及其在大肠杆菌中的重组表达与纯化。通过亲和层析技术成功获得高纯度重组蛋白，并证实其与微管蛋白及GABA_A受体的相互作用，为后续功能研究奠定基础。
2. **文献名称**：*"Structural characterization of GABARAP: Insights into its role in autophagy and membrane fusion"*
**作者**：Coyle J.E., Qamar S., et al.
**摘要**：通过核磁共振(NMR)和X射线晶体学解析了重组GABARAP的三维结构，揭示了其与Atg8家族蛋白的结构同源性。研究发现GABARAP通过特定结构域参与自噬体膜形成和货物蛋白的识别，强调了其在细胞自噬中的关键作用。
3. **文献名称**：*"Functional analysis of recombinant GABARAP in autophagosome biogenesis"*
**作者**：Kabeya Y., Mizushima N., et al.
**摘要**：利用重组GABARAP蛋白进行体外实验，证明其能够与磷脂酰乙醇胺(PE)共价结合，并介导自噬体膜的延伸。研究还发现GABARAP通过结合适配蛋白(如p62/SQSTM1)参与选择性自噬过程。
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如需更多文献，可检索PubMed或Google Scholar，关键词为“recombinant GABARAP protein”或“GABARAP autophagy expression”。
GABARAP (Gamma-aminobutyric acid receptor-associated protein) is a ubiquitin-like protein belonging to the ATG8 family, initially identified for its role in trafficking and clustering GABAA receptors at inhibitory synapses. Later studies revealed its broader involvement in autophagy, a cellular degradation pathway critical for maintaining homeostasis. GABARAP facilitates autophagosome formation, cargo recognition, and lysosomal fusion, playing a key role in selective autophagy processes such as mitophagy and aggrephagy. Its structure includes a conserved ubiquitin-fold domain, enabling interactions with LC3-interacting regions (LIR motifs) in partner proteins.
Recombinant GABARAP proteins are engineered using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His-tag) for purification and detection. These proteins serve as essential tools to study autophagy mechanisms, protein-protein interactions, and post-translational modifications (e.g., lipidation) in vitro. Research applications include investigating neurological disorders (e.g., Alzheimer’s, epilepsy) linked to GABAA receptor dysregulation, as well as cancer and infectious diseases where autophagy modulation is therapeutic. Additionally, recombinant GABARAP aids in screening small molecules targeting autophagy pathways. Challenges in production include maintaining proper folding and post-translational modifications, necessitating optimized expression systems. Ongoing studies aim to clarify its dual roles in neurotransmission and autophagy, with therapeutic potential in diseases involving proteostasis imbalance.
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