| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ARL5A |
| Uniprot No | Q9Y689 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-179aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMGILFTRIWRLFNHQEHKVIIVGLDN AGKTTILYQFSMNEVVHTSPTIGSNVEEIVINNTRFLMWDIGGQESLRSS WNTYYTNTEFVIVVVDSTDRERISVTREELYKMLAHEDLRKAGLLIFANK QDVKECMTVAEISQFLKLTSIKDHQWHIQACCALTGEGLCQGLEWMMSRL KIR |
| 预测分子量 | 23 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ARL5A重组蛋白的3篇代表性文献摘要(注：文献为虚构示例，实际文献需通过数据库检索确认)：
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1. **文献名称**: *"Expression and characterization of recombinant human ARL5A in Escherichia coli"*
**作者**: Chen L, et al.
**摘要**: 本研究成功构建了ARL5A的重组表达载体，利用大肠杆菌系统高效表达并纯化出可溶性蛋白。通过亲和层析和凝胶过滤获得高纯度ARL5A，并证实其具有GTP结合活性，为后续功能研究奠定基础。
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2. **文献名称**: *"Structural insights into ARL5A-GTP complex by X-ray crystallography"*
**作者**: Tanaka K, et al.
**摘要**: 通过重组表达人源ARL5A并解析其与GTP结合的晶体结构(分辨率2.1Å)，揭示了ARL5A独特的核苷酸结合域构象，提示其与ARL家族其他成员在信号传导中的功能差异。
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3. **文献名称**: *"ARL5A interacts with the retromer complex: A study using recombinant protein pull-down assays"*
**作者**: Smith J, et al.
**摘要**: 利用重组ARL5A蛋白进行体外互作实验，发现其与逆转运复合体(retromer)亚基VPS35存在直接结合，暗示ARL5A可能参与细胞内囊泡运输调控。
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如需具体文献，建议通过PubMed或SciFinder以“ARL5A recombinant”为关键词检索。
**Background of ARL5A Recombinant Protein**
ARL5A (ADP-ribosylation factor-like protein 5A) is a member of the ARF/ARL GTPase family, which plays critical roles in intracellular membrane trafficking, organelle dynamics, and signaling. As a small GTP-binding protein, ARL5A cycles between GTP-bound (active) and GDP-bound (inactive) states, regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Structurally, it contains a conserved GTPase domain and unique motifs that mediate interactions with effector molecules.
ARL5A is implicated in lipid metabolism, particularly in regulating cholesterol distribution and lipid droplet formation. Studies suggest its involvement in Golgi-associated processes and ciliary function, linking it to cellular homeostasis and development. Dysregulation of ARL5A has been observed in metabolic disorders and cancers, though its precise mechanistic contributions remain under investigation.
Recombinant ARL5A protein is produced using expression systems like *E. coli* or mammalian cells, ensuring proper folding and post-translational modifications. Purification typically involves affinity chromatography (e.g., His-tag) followed by gel filtration to achieve high purity. This recombinant tool enables *in vitro* studies, including GTP-binding assays, protein interaction analyses, and structural characterization (e.g., X-ray crystallography). Its application extends to screening small molecules targeting ARL5A-related pathways, offering potential therapeutic insights.
Recent research highlights ARL5A's role in autophagosome-lysosome fusion and its interaction with vesicular trafficking adaptors, expanding its relevance in neurodegenerative and metabolic diseases. Further exploration of ARL5A's molecular networks may uncover novel biomarkers or drug targets for associated pathologies.
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