| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SERP1 |
| Uniprot No | Q9Y6X1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-66 aa |
| 活性数据 | MVAKQRIRMANEKHSKNITQRGNVAKTSRNAPEEKASVGPWLLALFIFVVCGSAIFQIIQSIRMGM |
| 分子量 | 32.89 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. |
以下为虚构的示例文献，仅供格式参考(非真实存在的论文)：
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1. **文献名称**: "Recombinant Human SERP1 Protein Attenuates Endoplasmic Reticulum Stress in Atherosclerotic Models"
**作者**: Li, X., et al.
**摘要**: 研究重组人SERP1蛋白通过调节内质网应激通路抑制动脉粥样硬化斑块形成，揭示其在血管保护中的潜在治疗价值。
2. **文献名称**: "Expression and Functional Characterization of Recombinant SERP1 in Cancer Cell Apoptosis"
**作者**: Wang, Y., et al.
**摘要**: 报道重组SERP1蛋白的高效表达与纯化，并验证其通过调控凋亡相关蛋白(如Caspase-3)抑制肿瘤细胞生长的作用机制。
3. **文献名称**: "SERP1 as a Novel Chaperone: Structural Insights from Recombinant Protein Analysis"
**作者**: Johnson, R., & Smith, K.
**摘要**: 通过X射线晶体学解析重组SERP1蛋白的三维结构，揭示其作为分子伴侣参与内质网蛋白质折叠的功能域特征。
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如需真实文献，建议通过**PubMed**或**Google Scholar**检索关键词(如“recombinant SERP1 protein”)，并筛选近年的功能研究或应用类论文。
Recombinant human SERP1 protein, a member of the serine protease inhibitor (Serpin) superfamily, plays critical roles in regulating proteolytic cascades involved in coagulation, inflammation, and cellular homeostasis. SERP1. also known as stress-associated endoplasmic reticulum protein 1 (Serp1/RAMP4), is uniquely localized to the endoplasmic reticulum (ER) and participates in ER stress response pathways. It acts as a molecular chaperone, facilitating the folding and trafficking of secretory proteins while modulating unfolded protein response (UPR) signaling to mitigate ER stress.
Produced via genetic engineering in expression systems like mammalian cells or bacteria, recombinant SERP1 retains its functional properties, including binding to specific serine proteases or ER-resident proteins. Its therapeutic potential is explored in conditions linked to ER dysfunction, such as neurodegenerative diseases, cardiovascular disorders, and metabolic syndromes. Additionally, recombinant SERP1 serves as a research tool to study ER stress mechanisms and protein quality control. Challenges in production include maintaining proper post-translational modifications and structural integrity, often addressed through advanced bioprocessing techniques. Current studies focus on its dual role as a protease inhibitor and stress adaptor, highlighting its emerging significance in biomedical research and drug development.
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