| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ARL5B |
| Uniprot No | Q96KC2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-299aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGLIFAKLWSLFCNQEHKVIIVGLDNAGKT TILYQFLMNEVVHTSPTIGSNVEEIVVKNTHFLMWDIGGQESLRSSWNTY YSNTEFIILVVDSIDRERLAITKEELYRMLAHEDLRKAAVLIFANKQDMK GCMTAAEISKYLTLSSIKDHPWHIQSCCALTGEGLCQGLEWMTSRIGVR |
| 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ARL5B重组蛋白的示例参考文献(注：以下内容为模拟示例，实际文献需通过学术数据库查询)：
1. **文献名称**: "Expression and Functional Analysis of Recombinant ARL5B in Cancer Cell Lines"
**作者**: Chen X, et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了重组ARL5B蛋白，通过体外实验证实其GTP结合活性，并发现ARL5B过表达可抑制结肠癌细胞迁移，提示其在肿瘤转移中的潜在调控作用。
2. **文献名称**: "Structural Characterization of Human ARL5B Using Cryo-EM"
**作者**: Gupta R, et al.
**摘要**: 利用冷冻电镜技术解析了重组ARL5B蛋白的三维结构，揭示了其与GTP/GDP结合状态下的构象变化，为ARL5B参与细胞内囊泡运输的分子机制提供了结构基础。
3. **文献名称**: "ARL5B Recombinant Protein Interacts with Tubulin in Vitro"
**作者**: Müller T, et al.
**摘要**: 通过Pull-down实验证明重组ARL5B蛋白与微管蛋白β-tubulin直接结合，暗示ARL5B可能在细胞骨架动力学或有丝分裂中发挥功能。
4. **文献名称**: "Development of an ARL5B-Specific ELISA Using Recombinant Protein"
**作者**: Kim H, et al.
**摘要**: 基于重组ARL5B蛋白开发了高灵敏度的ELISA检测方法，用于定量分析血清中ARL5B水平，初步研究表明其与代谢综合征患者的相关性。
建议通过PubMed、Web of Science等平台以“ARL5B recombinant protein”为关键词检索最新文献以获取真实数据。
ARL5B (ADP-ribosylation factor-like protein 5B) is a member of the ARF/ARL family of small GTPases, which are evolutionarily conserved molecular switches regulating diverse cellular processes. Discovered in the early 2000s, ARL5B shares structural homology with other ARF/ARL proteins, featuring a conserved GTP-binding domain and a unique N-terminal helix critical for effector interactions. Unlike classical ARF proteins involved in vesicle trafficking, ARL5B localizes primarily to the trans-Golgi network and endosomal compartments, suggesting specialized roles in membrane dynamics and intracellular signaling.
Functionally, ARL5B is implicated in regulating secretory pathways, cell division, and cilia formation. Studies link it to lipid metabolism through interactions with phosphatidylinositol phosphate kinases (PIPKs) and lipid transporters. Its GTPase cycle (GTP/GDP binding and hydrolysis) modulates conformational changes necessary for effector recruitment, though its exact regulatory mechanisms remain under investigation. Dysregulation of ARL5B has been associated with cancers, metabolic disorders, and ciliopathies. For instance, ARL5B overexpression in tumors correlates with enhanced proliferation and metastasis, potentially serving as a biomarker or therapeutic target.
Recombinant ARL5B protein is typically produced using bacterial (e.g., E. coli) or eukaryotic expression systems, enabling structural and functional studies. Purification often involves affinity chromatography tags (e.g., GST, His-tag) followed by biochemical validation. This recombinant tool facilitates research into ARL5B’s 3D structure, GTPase kinetics, and protein interaction networks. It also aids in drug screening campaigns targeting ARL5B-related pathways. Despite progress, unanswered questions persist regarding its tissue-specific roles, post-translational modifications, and crosstalk with other signaling hubs. Current efforts focus on elucidating its contributions to cellular homeostasis and disease pathogenesis using recombinant protein-based assays and knockout models.
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