| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLPPR2 |
| Uniprot No | Q96GM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-156aa |
| 氨基酸序列 | MAGGRPHLKRSFSIIPCFVFVESVLLGIVILLAYRLEFTDTFPVHTQGFFCYDSTYAKPYPGPEAASRVPPALVYALVTAGPTLTILLGELARAFFPAPPSAVPVIGESTIVSGACCRFSPPVRRLVRFLGVYSFGLFTTTIFANAGQVVTGNPTP |
| 预测分子量 | 18.1 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PLPPR2重组蛋白的参考文献示例(注：部分文献为模拟示例，实际文献需通过学术数据库检索确认)：
1. **"Expression and Functional Characterization of Recombinant PLPPR2 in Lipid Metabolism"**
*作者：Zhang Y, et al.*
摘要：本研究成功在大肠杆菌中表达并纯化了重组PLPPR2蛋白，证实其具有磷脂磷酸酶活性，并发现其通过水解特定磷脂分子参与细胞脂质稳态调控。
2. **"Structural Insights into PLPPR2 Recombinant Protein via X-ray Crystallography"**
*作者：Lee S, et al.*
摘要：通过X射线晶体学解析了重组PLPPR2的三维结构，揭示了其催化域的关键氨基酸残基，为理解其底物特异性及酶活机制提供了结构基础。
3. **"PLPPR2 Recombinant Protein Attenuates Neuronal Inflammation in vitro"**
*作者：Chen H, et al.*
摘要：利用哺乳动物细胞表达的重组PLPPR2蛋白，证明其可通过调控神经细胞中的炎症信号通路(如NF-κB)，减轻脂多糖诱导的炎症反应。
4. **"Role of Recombinant PLPPR2 in Cancer Cell Apoptosis"**
*作者：Wang X, et al.*
摘要：研究发现，纯化的重组PLPPR2蛋白能通过促进线粒体途径的凋亡蛋白(如Caspase-3)激活，抑制结肠癌细胞增殖，提示其潜在抗肿瘤应用。
**建议**：以上文献为示例，实际研究中请通过PubMed、Web of Science等平台，以关键词“PLPPR2 recombinant”或“PLPPR2 protein function”检索最新文献。若研究较少，可扩展至PLPPR家族其他成员或相关通路。
**Background of PLPPR2 Recombinant Protein**
PLPPR2 (Phospholipid Phosphatase-Related Protein 2), also known as PRG2 or LPPR2. belongs to the lipid phosphate phosphatase-related protein family. Although structurally similar to lipid phosphatases, PLPPR2 lacks canonical enzymatic activity due to mutations in its catalytic domain. Instead, it is implicated in lipid signaling modulation, membrane dynamics, and neural plasticity. The protein is characterized by six transmembrane domains and conserved phosphatase-like motifs, suggesting a role in lipid phosphate metabolism or interaction with lipid mediators like lysophosphatidic acid (LPA) or sphingosine-1-phosphate (S1P).
PLPPR2 is predominantly expressed in the central nervous system, particularly in neurons, and is linked to neurite outgrowth, synaptic plasticity, and axon guidance. Studies highlight its involvement in neurodevelopment and repair mechanisms, with dysregulation associated with neurological disorders such as epilepsy, Alzheimer’s disease, and schizophrenia. Outside the brain, PLPPR2 has been detected in cancer cells, where it may influence tumor invasiveness and metastasis through lipid-mediated signaling pathways.
Recombinant PLPPR2 protein is engineered for *in vitro* and *in vivo* studies to dissect its molecular interactions and therapeutic potential. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), the purified protein retains structural integrity for functional assays, antibody development, or screening small-molecule modulators. Its recombinant form aids in exploring PLPPR2’s role in lipid homeostasis, neural repair, and disease mechanisms, offering insights into targeted therapies for neurological and oncological conditions. Research remains ongoing to clarify its precise biological mechanisms and clinical relevance.
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