| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLAAT3 |
| Uniprot No | P53816 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-162aa |
| 氨基酸序列 | MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ |
| 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PLAAT3重组蛋白的3篇代表性文献的简要总结(注：文献信息为模拟示例，具体内容需根据实际文献调整)：
1. **文献名称**：*"Recombinant PLAAT3 exhibits phospholipase A1/A2 activity and modulates lipid droplet formation in hepatocytes"*
**作者**：Smith J. et al.
**摘要**：本研究成功在大肠杆菌中表达了重组PLAAT3蛋白，并证实其具有磷脂酶A1/A2双功能活性。实验表明，PLAAT3通过水解磷脂酸调控肝细胞脂滴动态，可能影响脂质储存代谢。
2. **文献名称**：*"Structural insights into PLAAT3 substrate specificity and membrane interaction"*
**作者**：Yamamoto K. et al.
**摘要**：通过X射线晶体学解析了重组PLAAT3的三维结构，揭示了其催化口袋中关键氨基酸对底物选择性的作用，并阐明了其通过两亲性螺旋与细胞膜结合的分子机制。
3. **文献名称**：*"PLAAT3 suppresses colorectal cancer progression by altering cellular lipidome and inducing ferroptosis"*
**作者**：Chen L. et al.
**摘要**：研究发现重组PLAAT3蛋白在结肠癌细胞中过表达可诱导铁死亡，其机制与催化多不饱和脂肪酸氧化及降低抗氧化酶GPX4水平相关，提示其作为肿瘤治疗靶点的潜力。
(如需真实文献，建议通过PubMed或Google Scholar以“PLAAT3 recombinant protein”“PLAAT3 structure/function”等关键词检索近年论文。)
PLAAT3 (Phospholipase A and Acyltransferase 3), also known as HRASLS3 or H-REV107. is a member of the PLAAT (HREV107) protein family, characterized by conserved phospholipid-metabolizing enzyme activity. It plays a dual role as a phospholipase and acyltransferase, primarily involved in remodeling phospholipid membranes by catalyzing the transfer of fatty acyl chains. Structurally, PLAAT3 contains a conserved NC domain critical for its enzymatic function and a hydrophobic region enabling membrane association.
Originally identified as a tumor suppressor, PLAAT3 is downregulated in various cancers, where its loss correlates with poor prognosis. Beyond oncology, it regulates lipid droplet formation, autophagy, and inflammatory responses by modulating lipid signaling pathways, such as producing lipid mediators like N-acylethanolamines (NAEs). These molecules influence cellular processes, including apoptosis and energy homeostasis.
Recombinant PLAAT3 proteins are typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, often fused with tags (e.g., His-tag) for purification. Studies using recombinant PLAAT3 have clarified its enzymatic mechanisms, substrate preferences, and interactions with proteins like Ras GTPases. Recent research highlights its potential therapeutic relevance in metabolic disorders and neurodegenerative diseases, where lipid dysregulation is implicated. However, its pleiotropic roles and tissue-specific expression patterns necessitate further investigation to fully harness its biomedical applications.
In summary, PLAAT3 is a multifunctional lipid-metabolizing enzyme with implications in cancer, metabolism, and inflammation, making recombinant PLAAT3 a valuable tool for both mechanistic studies and drug discovery.
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