| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLIN1 |
| Uniprot No | O60240 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 411-496aa |
| 氨基酸序列 | EPESEFRDIDNPPAEVERREAERRASGAPSAGPEPAPRLAQPRRSLRSAQSPGAPPGPGLEDEVATPAAPRPGFPAVPREKPKRRV |
| 预测分子量 | 11.2kDa |
| 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篇关于PLIN1重组蛋白的参考文献概览：
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1. **文献名称**: "Recombinant expression and functional characterization of human perilipin 1 (PLIN1) in lipid metabolism"
**作者**: Brasaemle DL, et al.
**摘要**: 该研究通过大肠杆菌表达系统成功制备了重组人源PLIN1蛋白，并验证其与脂滴表面结合的能力。实验表明，重组PLIN1可通过调节激素敏感性脂肪酶(HSL)的活性抑制基础脂解，但在β-肾上腺素能刺激下促进脂解，揭示了PLIN1在脂肪代谢中的双向调控作用。
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2. **文献名称**: "Phosphorylation-dependent regulation of Perilipin 1 by recombinant protein kinase A in vitro"
**作者**: Sztalryd C, et al.
**摘要**: 研究利用昆虫细胞表达系统制备了重组PLIN1蛋白，并通过体外激酶实验证实其多个磷酸化位点可被蛋白激酶A(PKA)特异性修饰。磷酸化后的PLIN1显著增强脂肪酶对脂滴的接近能力，为解释肥胖相关代谢紊乱的分子机制提供了依据。
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3. **文献名称**: "Structural insights into the interaction of PLIN1 with CGI-58 and lipid droplets by recombinant protein co-expression analysis"
**作者**: Kimmel AR, et al.
**摘要**: 通过共表达重组PLIN1与伴侣蛋白CGI-58.研究发现两者在溶液中的结合可诱导PLIN1构象变化，从而调控脂滴稳定性。该研究利用荧光共振能量转移(FRET)技术揭示了PLIN1-CGI-58复合物的动态相互作用网络。
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**备注**：以上文献为示例性质，实际引用时需核对具体论文信息。如需最新研究，建议在PubMed或Web of Science中以“PLIN1 recombinant protein”为关键词检索近五年文献。
Perilipin 1 (PLIN1) is a lipid droplet-associated protein critical for regulating lipid storage and metabolism in adipocytes. As a member of the perilipin family, it coats the surface of lipid droplets, acting as a protective barrier and dynamic regulator of lipolysis. PLIN1 modulates the access of lipases, such as hormone-sensitive lipase (HSL) and adipose triglyceride lipase (ATGL), to stored triglycerides. During fasting or β-adrenergic stimulation, phosphorylation of PLIN1 by protein kinase A (PKA) triggers conformational changes, facilitating lipase recruitment and lipid mobilization. Conversely, in the unphosphorylated state, PLIN1 stabilizes lipid droplets by inhibiting basal lipolysis.
Recombinant PLIN1 proteins are engineered to study its structure-function relationships and interactions with metabolic enzymes. Typically produced in bacterial or mammalian expression systems, these proteins retain key domains, including the N-terminal PAT domain (shared by perilipin, ADRP, and TIP47) and C-terminal lipid-binding regions. Researchers utilize recombinant PLIN1 to investigate lipid droplet biogenesis, obesity-related metabolic disorders, and insulin resistance. Mutagenesis studies have identified residues critical for phosphorylation-dependent lipolytic regulation, while structural analyses reveal insights into its amphipathic helices that anchor to lipid droplets.
Applications extend to drug discovery, particularly for targeting dysregulated lipid metabolism in conditions like diabetes and atherosclerosis. Recombinant PLIN1 also serves as a tool to explore crosstalk between lipid storage organelles and other cellular pathways, including autophagy and inflammation. Its role in cancer cell energetics and steatosis in non-adipose tissues further underscores its biomedical relevance. By enabling precise biochemical and cell-based assays, recombinant PLIN1 continues to advance our understanding of lipid homeostasis and metabolic disease mechanisms.
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