| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COPE |
| Uniprot No | O14579 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-308aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAPPAPGPASGGSGEVDELFDVKNAFY IGSYQQCINEAQRVKLSSPERDVERDVFLYRAYLAQRKFGVVLDEIKPSS APELQAVRMFADYLAHESRRDSIVAELDREMSRSVDVTNTTFLLMAASIY LHDQNPDAALRALHQGDSLECTAMTVQILLKLDRLDLARKELKRMQDLDE DATLTQLATAWVSLATGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHM AQGRWEAAEGLLQEALDKDSGYPETLVNLIVLSQHLGKPPEVTNRYLSQL KDAHRSHPFIKEYQAKENDFDRLVLQYAPSA |
| 预测分子量 | 37 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3篇关于COPE重组蛋白的假设性参考文献示例(注：文献为示例性质，具体文献需通过学术数据库核实)：
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1. **文献名称**: *"Recombinant Expression and Functional Analysis of COPE in COP-I Vesicle Assembly"*
**作者**: Zhang, Y., et al.
**摘要**: 本研究通过在大肠杆菌系统中重组表达人源COPE蛋白，优化了纯化条件并获得高纯度蛋白。通过体外重构实验，证明重组COPE对COP-I囊泡形成的关键作用，并揭示其与β-COP亚基的互作机制。
2. **文献名称**: *"Structural Insights into COPE Dimerization via Cryo-EM"*
**作者**: Lee, S., & Chen, X.
**摘要**: 利用冷冻电镜技术解析了重组COPE蛋白二聚体的高分辨率结构，发现其N端结构域通过疏水相互作用介导二聚化，为理解COP-I复合体组装及膜运输调控提供了结构基础。
3. **文献名称**: *"COPE Knockdown Disrupts Golgi-to-ER Retrograde Transport in Human Cells"*
**作者**: Müller, M., et al.
**摘要**: 通过CRISPR/Cas9敲低细胞中COPE表达，结合重组COPE蛋白回补实验，证实COPE缺失导致内质网逆向运输缺陷，并引发未折叠蛋白反应(UPR)激活，提示其在细胞稳态中的关键角色。
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建议通过PubMed、Web of Science等平台，以关键词 **"COPE protein recombinant"** 或 **"COPI vesicle COPE"** 检索最新文献，重点关注蛋白功能、结构或疾病相关研究。
**Background of COPE Recombinant Protein**
The COPE (Coatomer Protein Epsilon) recombinant protein is a key component of the coat protein complex I (COPI), which plays a critical role in intracellular vesicular transport. COPI-coated vesicles mediate retrograde trafficking within the Golgi apparatus and between the Golgi and endoplasmic reticulum (ER), ensuring proper sorting, recycling, and maintenance of organelle integrity. The COPI complex comprises seven subunits (α-ζ), with COPE (ε-COP) contributing to the structural stability of the coat and participating in cargo recognition.
COPE was first identified in the 1990s during studies elucidating the mechanisms of vesicle formation and cargo selection. Its recombinant form is produced using expression systems like *E. coli* or mammalian cells, enabling researchers to study its biochemical properties, interactions, and role in membrane trafficking without isolating it from native tissues. Recombinant COPE retains functional domains critical for binding to other COPI subunits and cytosolic adaptors, such as those involved in Arf1-dependent vesicle assembly.
Research on COPE recombinant protein has advanced understanding of diseases linked to trafficking defects, including neurodegenerative disorders, cancer, and metabolic syndromes. For example, mutations or dysregulation in COPI components disrupt protein secretion, lipid homeostasis, and organelle function, contributing to pathological conditions. Additionally, COPE is explored as a tool in synthetic biology for engineering targeted vesicle delivery systems.
The availability of recombinant COPE has facilitated *in vitro* reconstitution assays, structural studies (e.g., cryo-EM), and drug screening aimed at modulating vesicular transport. Its application spans basic research, therapeutic development, and biotechnology, underscoring its importance in cell biology and biomedical innovation.
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