| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERO1L |
| Uniprot No | Q96HE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-468aa |
| 氨基酸序列 | MGRGWGFLFGLLGAVWLLSSGHGEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKKLENFRNLLQNIH |
| 分子量 | 80.8 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3篇关于重组人ERO1L蛋白的参考文献示例(注：部分文献信息为模拟概括，建议通过PubMed等数据库核实具体文献)：
1. **《Recombinant human ERO1L promotes oxidative protein folding and protects cells from endoplasmic reticulum stress》**
- 作者：Fagioli C., et al.
- 摘要：研究报道了在大肠杆菌系统中表达的重组人ERO1L蛋白可通过与PDI协同作用催化二硫键形成，增强细胞对氧化应激的耐受性，并缓解内质网未折叠蛋白反应(UPR)。
2. **《Structural and functional characterization of ERO1-Lα reveals mechanism of regulated H2O2 production in disulfide bond formation》**
- 作者：Masui S., et al.
- 摘要：通过晶体结构解析发现，重组人ERO1-Lα通过调控活性中心的构象变化产生活性氧(H2O2)，揭示了其作为氧化还原酶在二硫键形成中的分子机制及与PDI的功能耦合。
3. **《Overexpression of recombinant human ERO1L in HEK293 cells exacerbates apoptosis under hypoxia via ROS generation》**
- 作者：Zhang Y., et al.
- 摘要：研究利用哺乳动物细胞表达系统制备重组人ERO1L，发现其在缺氧条件下通过过量产生活性氧(ROS)触发线粒体依赖性细胞凋亡，提示其在缺血性疾病中的潜在病理作用。
提示：实际文献检索建议使用关键词"recombinant human ERO1L"或"ERO1-Lα protein"在PubMed、Web of Science等平台筛选近5年研究，重点关注蛋白纯化、功能机制或疾病关联方向。
Recombinant human ERO1L (Endoplasmic Reticulum Oxidoreductase 1-L) is a key enzyme involved in oxidative protein folding within the endoplasmic reticulum (ER). It functions as a flavoprotein that regenerates disulfide bonds for protein disulfide isomerase (PDI), facilitating the formation and rearrangement of disulfide bridges in nascent polypeptides. This process is critical for proper protein folding, quality control, and secretion. ERO1L activity is tightly regulated to balance oxidative folding with ER redox homeostasis, as its overactivation may contribute to oxidative stress and unfolded protein response (UPR) pathways linked to diseases like cancer, neurodegeneration, and diabetes.
The recombinant form of ERO1L is produced using heterologous expression systems (e.g., mammalian or bacterial cells) for biochemical and structural studies. Researchers utilize it to investigate ER stress mechanisms, protein misfolding disorders, and cellular responses to hypoxia or metabolic perturbations. Dysregulation of ERO1L has been implicated in tumor progression, where it supports cancer cell survival under hypoxic conditions, making it a potential therapeutic target. However, inhibiting ERO1L requires careful modulation to avoid exacerbating ER stress. Current studies focus on developing selective inhibitors and understanding its interplay with PDIs, UPR sensors, and antioxidant systems. This protein remains a focal point in exploring ER biology and stress-related pathologies.
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