| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GABARAPL2 |
| Uniprot No | P60520 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-117aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMKWMFKEDHSLEHRCVESAKIRAKYPDRVP VIVEKVSGSQIVDIDKRKYLVPSDITVAQFMWIIRKRIQLPSEKAIFLFV DKTVPQSSLTMGQLYEKEKDEDGFLYVAYSGENTFGF |
| 预测分子量 | 16 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GABARAPL2重组蛋白的3篇代表性文献(虚拟示例，实际文献需根据具体研究检索)：
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1. **文献名称**：*GABARAPL2 is a modifier of autophagy and metabolism in cancer cells*
**作者**：Smith A, et al.
**摘要**：研究通过重组GABARAPL2蛋白体外实验，发现其通过调控自噬小体形成影响肿瘤细胞的代谢重编程，抑制GABARAPL2表达可降低癌细胞存活率。
2. **文献名称**：*Structural insights into the interaction of GABARAPL2 with the LC3-interacting region*
**作者**：Tanaka K, et al.
**摘要**：利用重组GABARAPL2蛋白进行X射线晶体学分析，揭示了其与LC3家族蛋白相互作用的分子机制，为自噬相关蛋白的靶向设计提供结构基础。
3. **文献名称**：*Recombinant GABARAPL2 modulates mTOR signaling in neurodegenerative models*
**作者**：Chen L, et al.
**摘要**：通过表达纯化GABARAPL2重组蛋白，证明其在体外可结合mTOR通路组分，并在帕金森病模型中缓解神经元自噬缺陷。
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实际应用中建议通过PubMed或Google Scholar检索关键词“GABARAPL2 recombinant protein”获取最新文献，并关注其在自噬、癌症或神经退行性疾病中的功能研究。
GABARAPL2 (Gamma-aminobutyric acid receptor-associated protein-like 2), also known as GATE-16 or ATG8L, is a ubiquitin-like protein belonging to the ATG8 family, which includes homologs like GABARAP and LC3. It plays a critical role in autophagy, a conserved cellular process for degrading damaged organelles, protein aggregates, and pathogens. Autophagy involves the formation of double-membrane vesicles called autophagosomes, where GABARAPL2 contributes to membrane elongation, cargo recruitment, and autophagosome-lysosome fusion. Its ubiquitin-like structure allows it to conjugate with phosphatidylethanolamine (PE) on autophagosomal membranes, a process essential for autophagy progression.
Beyond autophagy, GABARAPL2 participates in intracellular trafficking, vesicle transport, and receptor recycling. It interacts with components of the ULK1 kinase complex, Beclin-1. and other modulators to fine-tune autophagic flux under stress conditions like nutrient deprivation or infection. Dysregulation of GABARAPL2 has been linked to cancer, neurodegenerative diseases (e.g., Alzheimer’s), and immune disorders. In cancer, it exhibits dual roles—acting as a tumor suppressor by promoting autophagic cell death or supporting tumor survival under metabolic stress.
Recombinant GABARAPL2 protein is produced using expression systems like E. coli or mammalian cells, often tagged with fluorescent markers (e.g., GFP) or purification tags (e.g., His-tag) for functional studies. It serves as a tool to investigate protein-protein interactions, autophagy mechanisms, and drug screening. Structural studies using recombinant GABARAPL2 have revealed its binding motifs for LC3-interacting regions (LIRs) and its role in recruiting selective autophagy adaptors like p62/SQSTM1. Its therapeutic potential is being explored in diseases where autophagy modulation is clinically relevant.
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