纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | RBP5 |
Uniprot No | P82980 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-135aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPPNLTGYYRFVSQKNMEDYLQALNISLAV RKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDG RKCQTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQV FRKVR |
预测分子量 | 18 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RBP5重组蛋白的参考文献示例(内容为虚构,仅供参考):
1. **《Expression and Purification of Recombinant Human RBP5 in E. coli》**
- 作者:Zhang, L. et al.
- 摘要:本研究成功构建了人源RBP5基因的重组质粒,并在大肠杆菌中高效表达。通过亲和层析纯化获得高纯度蛋白,验证了其与视黄醇的结合活性,为后续功能研究奠定基础。
2. **《Structural Insights into RBP5-Ligand Interactions by X-ray Crystallography》**
- 作者:Smith, J.R. & Tanaka, K.
- 摘要:首次解析了RBP5重组蛋白与视黄酸复合物的晶体结构,揭示了其特异性结合口袋的关键氨基酸残基,为设计靶向RBP5的小分子药物提供结构依据。
3. **《RBP5 Recombinant Protein Attenuates Retinal Degeneration in Mouse Models》**
- 作者:Chen, H. et al.
- 摘要:通过注射重组RBP5蛋白治疗遗传性视网膜病变小鼠模型,发现其显著延缓光感受器细胞凋亡,表明RBP5可能在维生素A代谢相关的眼病治疗中具有潜力。
4. **《RBP5 as a Novel Biomarker in Ovarian Cancer: Recombinant Protein-based ELISA Development》**
- 作者:Wang, Y. et al.
- 摘要:利用重组RBP5蛋白开发了高灵敏度ELISA检测法,发现卵巢癌患者血清中RBP5水平显著升高,提示其可能作为新型诊断标志物。
(注:以上文献为模拟内容,实际研究中请通过学术数据库检索具体文献。)
Recombinant retinol-binding protein 5 (RBP5) is a engineered version of the naturally occurring protein involved in vitamin A metabolism. RBP5. also known as cellular retinol-binding protein 3 (CRBP3), belongs to the lipocalin family of transport proteins that specifically bind and transport hydrophobic molecules. In humans, RBP5 plays a regulatory role in retinoid storage and mobilization, facilitating the intracellular transport of retinol (vitamin A alcohol) and protecting it from nonspecific oxidation. Its expression is particularly observed in ocular tissues, adipocytes, and certain epithelial cells.
Structurally, RBP5 contains a conserved β-barrel fold characteristic of lipid-binding proteins, with a hydrophobic pocket that accommodates retinol. The recombinant form is typically produced using bacterial (E. coli) or mammalian expression systems, enabling large-scale production for research and therapeutic applications. Compared to serum RBP4. RBP5 exhibits distinct tissue-specific functions and lower circulating concentrations, making it particularly relevant for studying localized vitamin A metabolism.
Current research focuses on its potential as a biomarker for metabolic disorders and its role in ocular diseases. Recombinant RBP5 serves as a critical tool for investigating retinoid-related pathways in conditions like age-related macular degeneration, retinal dystrophies, and certain cancers. Challenges in its application include maintaining proper protein folding during recombinant production and understanding isoform-specific interactions with nuclear receptors. Recent advances in structural biology have enabled better characterization of its retinol-binding mechanisms, supporting drug development efforts targeting retinoid signaling pathways.
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