| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DERL1 |
| Uniprot No | Q9BUN8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-251aa |
| 氨基酸序列 | MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATFYFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVGHLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ |
| 分子量 | 55.2 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. |
以下是与重组人DERL1蛋白相关的3篇代表性文献(内容基于领域知识模拟，仅供参考)：
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1. **文献名称**：Structural insights into the human DERL1 protein in ER-associated degradation
**作者**：Smith J.R., et al.
**摘要**：通过冷冻电镜解析重组人DERL1蛋白的三维结构，揭示了其在内质网相关降解(ERAD)中与其他组分(如VCP/p97和UBAC1)的相互作用机制，强调了其跨膜域对底物识别的重要性。
2. **文献名称**：Functional characterization of recombinant DERL1 in cancer cell migration
**作者**：Wang L., et al.
**摘要**：利用重组人DERL1蛋白体外实验，证明其通过调控内质网应激反应促进肿瘤细胞转移。研究显示，抑制DERL1可显著降低乳腺癌细胞侵袭能力，并影响HSP90等伴侣蛋白的表达。
3. **文献名称**：Role of DERL1 in α-synuclein clearance: Implications for Parkinson's disease
**作者**：Zhang H., et al.
**摘要**：研究重组DERL1蛋白在神经细胞中的作用，发现其通过ERAD通路促进错误折叠的α-synuclein降解，提示DERL1功能障碍可能加剧帕金森病中的蛋白聚集毒性。
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**说明**：以上文献名称及内容为模拟示例，实际研究需查阅具体数据库(如PubMed)。建议以“DERL1 protein recombinant”或“DERL1 ERAD function”等关键词检索最新文献。
Derlin-1 (DERL1), a key component of the endoplasmic reticulum-associated degradation (ERAD) pathway, plays a critical role in cellular protein quality control. As a member of the Derlin family, it facilitates the recognition and retrotranslocation of misfolded or unassembled proteins from the ER lumen to the cytoplasm for proteasomal degradation. Structurally, DERL1 contains multiple transmembrane domains and interacts with other ERAD machinery components like Sec61. p97/VCP, and ubiquitin ligases. Its function is crucial in resolving ER stress, maintaining cellular homeostasis, and preventing protein aggregation-related pathologies.
Recombinant human DERL1 protein is engineered for in vitro studies to dissect ERAD mechanisms, screen drug candidates targeting protein degradation pathways, or explore diseases linked to ERAD dysfunction (e.g., neurodegenerative disorders, cancer). Produced typically in mammalian or insect cell systems, recombinant DERL1 retains post-translational modifications and structural integrity necessary for functional assays. Research highlights its involvement in viral infection responses, cancer cell survival under stress, and crosstalk with autophagy. However, its precise structural dynamics and regulatory networks remain partially understood, driving ongoing investigations into its therapeutic potential.
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