| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EDEM1 |
| Uniprot No | Q92611 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 559-656 |
| 氨基酸序列 | YLLFDEDNPVHKSGTRYMFTTEGHIVSVDEHLRELPWKEFFSEEGGQDQGGKSVHRPKPHELKVINSSSNCNRVPDERRYSLPLKSIYMRQIDQMVGL |
| 分子量 | 36.52 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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EDEM1蛋白的3篇参考文献，包含文献名称、作者和摘要概括：
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### 1. **"EDEM1 accelerates the degradation of misfolded α1-antitrypsin via interaction with ER mannosidase I"**
**作者**: Hosokawa, N. et al. (2003)
**摘要**:
本文通过重组表达人EDEM1蛋白(在HEK293细胞中)，证实其通过结合内质网甘露糖苷酶I，加速错误折叠的α1-抗胰蛋白酶(α1-AT)的靶向降解，揭示了EDEM1在ERAD(内质网相关降解)中识别异常糖基化底物的关键作用。
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### 2. **"EDEM1 and EDEM2 regulate ER-associated degradation by competing for substrates in a glycan-dependent manner"**
**作者**: Cormier, J.H. et al. (2008)
**摘要**:
研究利用重组EDEM1和EDEM2蛋白，通过体外结合实验和细胞模型发现，两者通过识别糖蛋白的高甘露糖结构，竞争性结合错误折叠蛋白以调控其降解效率，证明了EDEM1直接参与ERAD底物筛选的分子机制。
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### 3. **"Structural basis of the ERAD process mediated by EDEM1"**
**作者**: Oda, Y. et al. (2009)
**摘要**:
该研究解析了重组人EDEM1蛋白的晶体结构，发现其具有独特的碳水化合物识别结构域(CRD)，并通过体外实验验证EDEM1优先结合带有终端α1.2-甘露糖残基的异常糖蛋白，阐明了其在ERAD中识别“标记蛋白”的结构基础。
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### (可选)4. **"EDEM1 modulates oxidative stress tolerance by regulating ER-associated degradation of misfolded proteins"**
**作者**: Olivari, S. et al. (2015)
**摘要**:
通过重组EDEM1过表达实验，研究表明EDEM1在氧化应激条件下显著促进错误折叠蛋白的降解，并减轻内质网压力，揭示了其在细胞应激反应中的保护性功能。
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以上文献均围绕重组人EDEM1在ERAD途径中的功能展开，涵盖其作用机制、结构基础及生理意义。如需具体全文或出版信息，可在PubMed或Web of Science中检索标题获取。
**Background of Recombinant Human EDEM1 Protein**
EDEM1 (Endoplasmic reticulum Degradation Enhancing Alpha-Mannosidase-like 1) is a key chaperone involved in endoplasmic reticulum (ER)-associated degradation (ERAD), a quality control mechanism that identifies and disposes of misfolded glycoproteins in the ER. Structurally, EDEM1 belongs to the glycosyl hydrolase 47 family, though its enzymatic activity remains debated. Instead, it primarily acts as a recognition factor for terminally misfolded glycoproteins by trimming mannose residues from N-linked glycans, marking them for ERAD.
Recombinant human EDEM1 is produced in vitro (e.g., mammalian or insect cell systems) to study its role in ERAD and disease contexts. The protein typically includes tags (e.g., His, FLAG) for purification and detection. Research highlights its interaction with ERAD components like SEL1L/HRD1 and its ability to accelerate the clearance of misfolded proteins, preventing ER stress. Dysregulation of EDEM1 is linked to pathologies such as neurodegenerative disorders, diabetes, and cancer, making it a therapeutic interest. Its recombinant form enables mechanistic studies, drug screening, and exploration of ERAD’s role in cellular proteostasis.
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