| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RAB24 |
| Uniprot No | Q969Q5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-227aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMSGQRVDVKVVMLGKEYVGKTSLVER YVHDRFLVGPYQNTIGAAFVAKVMSVGDRTVTLGIWDTAGSERYEAMSRI YYRGAKAAIVCYDLTDSSSFERAKFWVKELRSLEEGCQIYLCGTKSDLLE EDRRRRRVDFHDVQDYADNIKAQLFETSSKTGQSVDELFQKVAEDYVSVA AFQVMTEDKGVDLGQKPNPYFYSCCHH |
| 预测分子量 | 26 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RAB24重组蛋白的3篇参考文献及其摘要概括(文献为虚构示例，仅供参考)：
1. **"Functional Analysis of Recombinant RAB24 in Autophagic Vesicle Trafficking"**
- **作者**: Tanaka K. et al.
- **摘要**: 研究通过在大肠杆菌中表达重组RAB24蛋白，发现其通过调控GTP结合状态参与自噬小体与溶酶体的膜融合过程，并揭示其异常表达与细胞清除蛋白聚集体的能力下降相关。
2. **"Expression and Purification of Human RAB24 Recombinant Protein for Structural Studies"**
- **作者**: Müller S. et al.
- **摘要**: 报道了一种高效的真核表达系统(如昆虫细胞)制备重组RAB24蛋白的方法，并通过X射线晶体学解析其三维结构，揭示了其与特定效应蛋白结合的分子机制。
3. **"RAB24 Recombinant Protein Attenuates Oxidative Stress-Induced Apoptosis in Neuronal Cells"**
- **作者**: Chen L. et al.
- **摘要**: 利用哺乳动物细胞表达的重组RAB24蛋白，证明其通过调节线粒体膜稳定性减少氧化应激诱导的神经元凋亡，提示其在神经退行性疾病中的潜在治疗价值。
4. **"Role of RAB24 in Viral Pathogenesis: Insights from Recombinant Protein-Mediated Pathway Inhibition"**
- **作者**: Gupta R. et al.
- **摘要**: 通过体外实验发现，重组RAB24蛋白可通过竞争性结合宿主细胞运输通路的关键因子，抑制某些包膜病毒(如疱疹病毒)的细胞内运输和释放。
(注：以上文献为示例，实际研究中请通过学术数据库检索真实发表论文。)
**Background of RAB24 Recombinant Protein**
RAB24. a member of the RAS superfamily of small GTPases, plays critical roles in intracellular membrane trafficking, autophagy, and cellular stress responses. Unlike other RAB proteins that cycle between GTP-bound (active) and GDP-bound (inactive) states, RAB24 exhibits unique regulatory behaviors, including prolonged GTPase activity and atypical localization patterns, suggesting specialized functions in vesicle trafficking or autophagosome maturation. It is implicated in maintaining cellular homeostasis by facilitating the clearance of protein aggregates and damaged organelles through autophagy-lysosomal pathways.
The recombinant RAB24 protein is engineered using heterologous expression systems (e.g., *E. coli*, mammalian cells) to enable functional and structural studies. Its production often involves codon optimization, affinity tag fusion (e.g., His-tag, GST), and purification via chromatography to ensure high purity and bioactivity. Structural analyses reveal conserved GTP-binding domains and effector interaction motifs, while post-translational modifications (e.g., prenylation) may influence its membrane association and trafficking roles.
Research highlights RAB24's involvement in pathological conditions. Dysregulation of RAB24 expression or activity has been linked to neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s), cancer progression (via altered autophagy or apoptosis), and microbial infection responses. For instance, RAB24 may promote tumor cell survival under stress by enhancing autophagic flux or modulate viral replication by interacting with pathogen components.
The recombinant protein serves as a vital tool for deciphering RAB24's molecular mechanisms, screening therapeutic agents targeting autophagy-related disorders, and developing diagnostic biomarkers. Ongoing studies aim to clarify its interplay with other RAB GTPases, stress-responsive signaling pathways, and potential as a drug target. Despite progress, RAB24's precise physiological and pathological roles remain partially elusive, necessitating further exploration using recombinant protein-based models.
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