| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERO1A |
| Uniprot No | Q96HE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-468aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSEEQPPETAAQRCFCQVSGYLDDCTCDV ETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCA VKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQK AVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIW NVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRL ISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRR LKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHE IKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLW GKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRI STSVKELENFRNLLQNIH |
| 预测分子量 | 54 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ERO1A重组蛋白的3篇参考文献概览：
1. **文献名称**：*Production of recombinant human ERO1-Lα and its inhibitory effects on the inflammatory response in vitro*
**作者**：Li X. et al.
**摘要**：该研究报道了在大肠杆菌中高效表达并纯化重组人ERO1A蛋白的方法，验证了其体外促进二硫键形成的氧化酶活性，并发现该蛋白可抑制巨噬细胞的炎症反应，提示其潜在抗炎应用价值。
2. **文献名称**：*Structural insights into the redox-regulated dynamic conformations of human ERO1α*
**作者**：Wang L. et al.
**摘要**：通过X射线晶体学解析了重组人ERO1A蛋白在不同氧化还原状态下的三维结构，揭示了其活性中心构象变化机制，为设计靶向ERO1A的小分子药物提供了结构基础。
3. **文献名称**：*Targeting ERO1α with small-molecule inhibitors suppresses tumor growth in preclinical models*
**作者**：Cheng Z. et al.
**摘要**：研究团队利用重组人ERO1A蛋白进行高通量药物筛选，鉴定出选择性小分子抑制剂，并在多种肿瘤模型中验证了其通过扰乱内质网氧化稳态抑制癌细胞增殖的效果。
注：以上文献信息为模拟示例，实际引用时建议通过PubMed或Web of Science核对准确信息。
ERO1A (Endoplasmic Reticulum Oxidoreductase 1 Alpha) is a pivotal enzyme in the endoplasmic reticulum (ER) responsible for oxidative protein folding. It functions as a flavoprotein oxidase that regenerates disulfide bonds in protein disulfide isomerase (PDI), a key chaperone facilitating correct disulfide bridge formation in nascent polypeptides. By transferring electrons from reduced PDI to molecular oxygen, ERO1A maintains the oxidative environment of the ER, ensuring proper protein folding and quality control. Its activity is tightly regulated through feedback mechanisms involving reduced PDI and hypoxia-inducible factors to prevent hyperoxidation or ER stress.
Recombinant ERO1A proteins are engineered for research and therapeutic applications. Produced via heterologous expression systems (e.g., mammalian cells or E. coli), these proteins retain catalytic domains critical for oxidase activity, including the FAD-binding site and cysteine-rich regions. Purification typically involves affinity chromatography followed by functional validation using redox assays. Recombinant ERO1A enables studies on ER stress pathways, particularly in diseases like cancer (where its overexpression correlates with tumor progression) and neurodegenerative disorders (linked to protein misfolding). It also serves as a tool for investigating thiol-disulfide homeostasis and developing inhibitors targeting oxidative folding in pathological conditions. Current research explores its role in diabetes, inflammation, and cellular responses to hypoxia, highlighting its multifaceted biological significance.
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