| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Plaa |
| Uniprot No | P27612 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 495-584aa |
| 氨基酸序列 | TGAGRYMPGSAGMDTTMTGVDPFTGNSAYRSAASKTVNIYFPKKEALTFDQANPTQILGKLKELNGTAPEEKKLTEDDLVLLEKILSLIC |
| 预测分子量 | 13.6 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. |
以下为虚构的示例参考文献，供参考学习(实际文献请通过学术数据库检索)：
1. **标题**: "Recombinant PLAA Protein Enhances Phospholipase A2 Activity in Inflammatory Response"
**作者**: Smith J, et al.
**摘要**: 本研究在大肠杆菌系统中成功表达并纯化了重组PLAA蛋白，验证了其通过激活磷脂酶A2(PLA2)促进花生四烯酸释放的功能，揭示了PLAA在炎症信号通路中的关键作用。
2. **标题**: "Structural Characterization of PLAA and Its Role in Protein Aggregation Diseases"
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析了重组PLAA蛋白的三维结构，发现其与泛素结合域的相互作用，为研究PLAA在神经退行性疾病(如亨廷顿病)中调控蛋白聚集的机制提供了结构基础。
3. **标题**: "Development of a Mammalian Cell Expression System for High-Yield PLAA Production"
**作者**: García R, et al.
**摘要**: 开发了一种基于HEK293细胞的重组PLAA蛋白高效表达系统，优化后的工艺使蛋白产量提升5倍，并证实其生物活性适用于药物筛选及功能研究。
4. **标题**: "PLAA Knockdown and Recombinant Rescue in Zebrafish Inflammation Models"
**作者**: Tanaka K, et al.
**摘要**: 利用斑马鱼模型证明，重组PLAA蛋白可逆转PLAA基因敲低导致的炎症反应缺陷，为靶向PLAA的免疫调节疗法提供了体内实验依据。
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**提示**：如需真实文献，建议使用以下关键词在PubMed或Web of Science检索：
`"PLAA protein recombinant"`、`"Phospholipase A2 activating protein expression"`、`"PLAA inflammation"`。注意区分基因名PLAA(Proline-rich coiled-coil 2A, 曾用名)与其他缩写。
Plaa (Phospholipase A2-activating protein) is a multifunctional protein implicated in various cellular processes, including inflammation, proteostasis, and neurodegeneration. It was initially identified as a regulator of group IV cytosolic phospholipase A2 (cPLA2), enhancing the production of arachidonic acid and pro-inflammatory lipid mediators. Structurally, Plaa contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal ubiquitin-like (UBL) domain, which facilitate interactions with ubiquitinated proteins and proteasomal components. This architecture positions Plaa as a potential mediator of protein quality control, linking ubiquitination pathways to proteasomal degradation.
Recent studies highlight Plaa's role in neurodegenerative diseases, particularly in protein aggregation disorders. It interacts with misfolded proteins, such as mutant huntingtin in Huntington’s disease, and modulates their clearance via the ubiquitin-proteasome system (UPS) or autophagy. Plaa’s UBL domain is critical for recruiting proteasomal machinery, while its UBA domain may recognize polyubiquitinated substrates, suggesting a chaperone-like function in triaging damaged proteins. Dysregulation of Plaa has been associated with disrupted proteostasis, contributing to the accumulation of toxic aggregates observed in Alzheimer’s and Parkinson’s diseases.
Recombinant Plaa protein, produced through heterologous expression systems like *E. coli* or mammalian cells, is widely used to study these mechanisms *in vitro* and *in vivo*. Its purified form enables biochemical assays to map interaction networks, screen for modulators of proteostasis, or explore therapeutic strategies for neurodegenerative conditions. For instance, recombinant Plaa has been tested in cellular models to enhance clearance of pathogenic protein aggregates, demonstrating its potential as a research tool or therapeutic candidate. Ongoing research aims to unravel its dual roles in inflammation and neurodegeneration, offering insights into disease pathogenesis and targeted interventions.
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