| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PISD |
| Uniprot No | Q9UG56 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-375aa |
| 氨基酸序列 | MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGALRPLSRVGWRPVSRVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL |
| 预测分子量 | 56.0 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3篇与PISD(磷脂酰丝氨酸脱羧酶)重组蛋白相关的文献摘要概览：
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1. **文献名称**：*"Recombinant expression and functional characterization of human phosphatidylserine decarboxylase (PISD) in yeast"*
**作者**：Smith et al., 2018
**摘要**：研究通过酵母表达系统成功重组表达了人源PISD酶，验证其催化磷脂酰丝氨酸转化为磷脂酰乙醇胺的活性，并发现其在线粒体膜脂质代谢中的关键作用。
2. **文献名称**：*"Structural insights into the mechanism of PISD-mediated phospholipid biosynthesis"*
**作者**：Chen & Lee, 2020
**摘要**：利用大肠杆菌表达纯化的重组PISD蛋白进行晶体结构解析，揭示了其活性位点及底物结合机制，为靶向PISD的代谢疾病治疗提供结构基础。
3. **文献名称**：*"Mitochondrial dysfunction and PISD deficiency: Rescue by recombinant enzyme delivery"*
**作者**：Wang et al., 2021
**摘要**：通过哺乳动物细胞系表达重组PISD蛋白，证明其可恢复线粒体功能缺陷细胞的脂质稳态，为PISD相关遗传性疾病的基因治疗提供实验依据。
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注：上述文献为模拟案例，实际研究中请结合具体数据库(如PubMed、Web of Science)检索最新文献。
**Background of PISD Recombinant Protein**
Phosphatidylserine decarboxylase (PISD) is a mitochondrial enzyme critical for phospholipid metabolism, catalyzing the conversion of phosphatidylserine (PS) to phosphatidylethanolamine (PE). This process is essential for maintaining membrane integrity, mitochondrial dynamics, and cellular homeostasis. PISD plays a pivotal role in lipid bilayer remodeling, influencing organelle function, autophagy, and apoptosis. Dysregulation of PISD has been linked to metabolic disorders, neurodegenerative diseases, and cancer, underscoring its biological and therapeutic relevance.
Recombinant PISD protein is engineered through genetic cloning and expression in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells*), enabling large-scale production of the enzyme for functional studies. By omitting regulatory elements or modifying specific domains, recombinant PISD can be optimized for stability, solubility, or activity. Its applications span *in vitro* assays to investigate enzymatic kinetics, lipid-protein interactions, and structural analysis (e.g., X-ray crystallography or cryo-EM).
Research leveraging recombinant PISD has advanced understanding of mitochondrial lipid synthesis, particularly in contexts like membrane asymmetry, ER-mitochondria crosstalk, and disease mechanisms. For instance, PISD deficiency models reveal disrupted PE levels, impairing mitochondrial respiration and promoting oxidative stress. Conversely, overexpression studies explore its potential in mitigating lipid metabolic defects.
Therapeutic interest in PISD focuses on modulating its activity to address lipid-related pathologies. Small-molecule inhibitors or activators targeting PISD are under investigation for cancer therapy, while gene-editing approaches aim to restore PISD function in genetic disorders. As a tool, recombinant PISD remains indispensable for unraveling lipid biology and developing precision medicine strategies.
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