| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | iPLA2 |
| Uniprot No | Q9NST1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 63-481aa |
| 氨基酸序列 | EQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTRVSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDELLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTLPVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCTPEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKSL |
| 预测分子量 | 53.7 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. |
以下为模拟生成的关于iPLA2重组蛋白的参考文献示例(实际文献请通过学术数据库查询)：
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1. **《重组iPLA2β在大肠杆菌中的表达与功能表征》**
*作者：Smith A, et al.*
摘要：本研究成功在大肠杆菌中表达了重组人源iPLA2β蛋白，并通过亲和层析纯化。酶活性实验表明，重组蛋白具有钙离子非依赖性的磷脂水解活性，且在抗氧化应激中发挥潜在作用。
2. **《iPLA2γ的结构解析及其在膜修复中的机制》**
*作者：Zhang L, Wang Y.*
摘要：利用X射线晶体学解析了重组iPLA2γ的三维结构，揭示了其催化中心的独特构象。功能实验证明该蛋白通过水解受损膜磷脂促进细胞膜稳定性。
3. **《重组iPLA2在神经退行性疾病模型中的保护作用》**
*作者：Chen R, et al.*
摘要：在阿尔茨海默病细胞模型中，过表达重组iPLA2显著减少氧化脂质积累，并抑制神经元凋亡，提示其作为治疗靶点的潜力。
4. **《iPLA2重组蛋白的抑制剂筛选与药物开发》**
*作者：Johnson M, et al.*
摘要：通过高通量筛选发现两种小分子化合物可特异性抑制重组iPLA2活性，为炎症性疾病的新型药物研发提供基础。
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**备注**：以上内容为模拟生成，仅供参考。实际文献请查询PubMed、Web of Science等平台，使用关键词“iPLA2 recombinant protein”“calcium-independent phospholipase A2”等。
iPLA2 (calcium-independent phospholipase A2) is a member of the phospholipase A2 superfamily, which hydrolyzes phospholipids at the sn-2 position to release free fatty acids (e.g., arachidonic acid) and lysophospholipids. Unlike secretory PLA2 (sPLA2) or cytosolic PLA2 (cPLA2), iPLA2 operates independently of calcium ions, making it critical for basal phospholipid metabolism and homeostatic regulation. It is encoded by the PLA2G6 gene in humans and plays essential roles in membrane remodeling, signal transduction, and inflammatory responses. Dysregulation of iPLA2 activity is linked to neurodegenerative diseases (e.g., Parkinson’s), metabolic disorders, and cardiovascular pathologies.
Recombinant iPLA2 proteins are engineered using expression systems like E. coli or mammalian cells, enabling precise study of their enzymatic mechanisms and interactions. These proteins retain key structural features, including a catalytic domain with a conserved GXSXG motif and ankyrin repeats involved in protein-protein interactions. Researchers utilize recombinant iPLA2 to investigate lipid-mediated pathways, evaluate inhibitors for therapeutic development, and model disease-associated mutations. Its calcium-independent nature makes it particularly valuable for studying lipid signaling under physiological conditions where calcium levels are low. Additionally, recombinant iPLA2 serves as a tool in drug screening and biomarker discovery, highlighting its dual role as a biochemical reagent and a therapeutic target. Advances in protein engineering continue to enhance its stability and activity, expanding applications in both basic research and translational medicine.
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