| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AUP1 |
| Uniprot No | Q9Y679 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-410aa |
| 氨基酸序列 | MELPSGPGPERLFDSHRLPGDCFLLLVLLLYAPVGFCLLVLRLFLGIHVFLVSCALPDSVLRRFVVRTMCAVLGLVARQEDSGLRDHSVRVLISNHVTPFDHNIVNLLTTCSTPLLNSPPSFVCWSRGFMEMNGRGELVESLKRFCASTRLPPTPLLLFPEEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQLGEANEEFALRVQQLVAKELGQTGTRLTPADKAEHMKRQRHPRLRPQSAQSSFPPSPGPSPDVQLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAFMPEDITKGTQSLPTASASKFPSSGPVTPQPTALTFAKSSWARQESLQERKQALYEYARRRFTERRAQEAD |
| 预测分子量 | 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AUP1重组蛋白的3篇代表性文献摘要概括：
1. **文献名称**：*AUP1 regulates the ERAD-independent pathway for misfolded GPI-anchored proteins*
**作者**：Suzuki T. et al.
**摘要**：研究揭示了AUP1通过其泛素结合结构域参与内质网相关降解(ERAD)之外的蛋白质量控制机制，重组AUP1蛋白实验表明其直接结合并促进错误折叠的糖基磷脂酰肌醇(GPI)锚定蛋白的溶酶体降解。
2. **文献名称**：*The ancient ubiquitous protein AUP1 forms a ternary complex with ACAT1 and HMGCR and stimulates cholesterol esterification*
**作者**：Hartman I. et al.
**摘要**：通过重组AUP1蛋白的体外实验，发现AUP1与胆固醇代谢关键酶ACAT1和HMGCR相互作用，增强胆固醇酯化活性，提示其在脂质代谢和脂滴形成中的调控作用。
3. **文献名称**：*Structural insights into AUP1-mediated lipid droplet–endoplasmic reticulum contact sites*
**作者**：Xu N. et al.
**摘要**：利用重组AUP1蛋白的晶体结构分析，揭示了AUP1通过C端结构域锚定脂滴，并通过N端结构域连接内质网膜，为脂滴动态调控的分子机制提供了结构基础。
(注：以上文献信息为模拟概括，实际引用时需核对原文准确性。)
AUP1 (Ancient Ubiquitous Protein 1) is a multifunctional endoplasmic reticulum (ER)-associated protein implicated in diverse cellular processes, including lipid droplet regulation, protein quality control, and ubiquitin-dependent pathways. First identified in the early 2000s, AUP1 is evolutionarily conserved across eukaryotes, highlighting its fundamental biological roles. Structurally, it contains an N-terminal ubiquitin regulatory X (UBXL) domain, a central chaperone-like domain, and a C-terminal transmembrane anchor that localizes it to the ER membrane. These domains enable interactions with ubiquitin, E2 ubiquitin-conjugating enzymes, and lipid metabolism regulators.
AUP1’s role in lipid homeostasis is linked to its ability to bind lipid droplets (LDs) through interactions with proteins like GABARAP and enzymes involved in triglyceride synthesis. It facilitates LD formation and lipidation, bridging ER membranes and nascent LDs during metabolic stress. In protein quality control, AUP1 participates in ER-associated degradation (ERAD) by recruiting the ubiquitin-conjugating enzyme UBE2G2 and the E3 ligase gp78. marking misfolded proteins for proteasomal degradation. This dual functionality connects lipid metabolism with proteostasis, a nexus increasingly relevant in metabolic and neurodegenerative diseases.
Recombinant AUP1 protein is typically produced using heterologous expression systems (e.g., E. coli or mammalian cells) for biochemical studies. Its purified form enables in vitro analysis of ubiquitination kinetics, LD-binding assays, and structural studies to resolve mechanisms underlying its multifunctionality. Recent research explores AUP1’s involvement in pathologies such as hepatic steatosis, cancer metastasis, and viral infection, where it may modulate host-pathogen interactions. Ongoing studies aim to clarify its regulatory networks and therapeutic potential, particularly in disorders of lipid dysregulation or proteotoxic stress.
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