| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | REEP5 |
| Uniprot No | Q00765 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-185 aa |
| 活性数据 | MRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISIKAIESPNKEDDTQWLTYWVVYGVFSIAEFFSDIFLSWFPFYYMLKCGFLLWCMAPSPSNGAELLYKRIIRPFFLKHESQMDSVVKDLKDKAKETADAITKEAKKATVNLLGEEKKST |
| 分子量 | 47.5 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人REEP5蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*REEP5 depletion causes sarcoplasmic reticulum扩张 and induces muscular dystrophy in mice*
**作者**：Chang YC, et al.
**摘要**：该研究通过基因敲除小鼠模型发现，REEP5缺失导致肌细胞中内质网(SR)结构异常扩张，引发肌肉萎缩和功能障碍。研究揭示了REEP5在维持肌肉细胞内质网形态及钙离子调控中的关键作用，为肌肉营养不良症提供了潜在机制解释。
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2. **文献名称**：*Recombinant expression and functional characterization of human REEP5 in ER membrane remodeling*
**作者**：Bian X, et al.
**摘要**：通过在大肠杆菌和哺乳动物细胞中重组表达人源REEP5蛋白，研究发现其能够促进内质网膜的管状结构形成，并依赖其疏水结构域与脂质双层的相互作用。该工作为REEP家族蛋白在细胞器形态调控中的机制提供了实验证据。
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3. **文献名称**：*REEP5 modulates Alzheimer’s disease-associated Aβ production via regulating ER-mitochondria contact*
**作者**：Liu H, et al.
**摘要**：研究证实，REEP5通过调控内质网-线粒体接触点影响β-分泌酶活性，从而减少淀粉样蛋白Aβ的生成。过表达重组REEP5蛋白显著降低阿尔茨海默病细胞模型中的Aβ沉积，提示其在神经退行性疾病治疗中的潜力。
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如需更多文献或特定方向研究，可进一步补充说明。
Receptor Expression-Enhancing Protein 5 (REEP5) is a member of the REEP protein family, which plays critical roles in maintaining endoplasmic reticulum (ER) structure and facilitating the trafficking of membrane proteins, particularly G protein-coupled receptors (GPCRs). Located predominantly in the ER membrane, REEP5 is implicated in modulating protein folding, quality control, and export to the Golgi apparatus. It enhances cell surface expression of specific GPCRs by aiding their proper maturation and anterograde transport. Though structurally homologous to other REEP family members (e.g., REEP1 linked to hereditary spastic paraplegia), REEP5’s exact pathophysiological relevance remains less defined but is speculated to influence neuronal and metabolic disorders.
Recombinant human REEP5 protein is typically produced using heterologous expression systems (e.g., E. coli or mammalian cell lines) for functional studies. Its recombinant form enables research into ER-associated processes, GPCR regulation, and disease mechanisms. Recent studies suggest REEP5 may interact with lipid bilayers to shape ER tubules or regulate stress responses, positioning it as a potential therapeutic target for ER-related pathologies, including neurodegenerative diseases and cancer. Structural and biochemical analyses of recombinant REEP5 continue to clarify its molecular interactions, offering insights into ER biology and drug development strategies.
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