| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLIN |
| Uniprot No | O60240 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 101-208 aa |
| 活性数据 | KIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPADKEESAPAPGHQQA |
| 分子量 | 37.62 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人PLIN(Perilipin)蛋白的3篇示例参考文献(内容为模拟，建议通过学术数据库核实具体信息)：
---
1. **文献名称**：*Recombinant Human Perilipin 1 Expression in Adipocytes Regulates Lipolysis and Adiponectin Secretion*
**作者**：Zhang Y, et al.
**摘要**：研究通过在大肠杆菌中表达重组人Perilipin 1(PLIN1)蛋白，验证其在脂肪细胞中对脂解作用的调控机制，发现PLIN1磷酸化可抑制脂解，并间接影响脂联素分泌，为肥胖相关代谢疾病提供新靶点。
2. **文献名称**：*Structural and Functional Analysis of Recombinant PLIN2 in Lipid Droplet Formation*
**作者**：Wang L, et al.
**摘要**：利用真核系统表达重组人PLIN2蛋白，结合冷冻电镜技术解析其结构，揭示PLIN2通过特定结构域结合脂滴表面，调控肝细胞脂质储存异常相关的病理过程。
3. **文献名称**：*Recombinant PLIN3 as a Biomarker for Atherosclerosis: In Vitro and Clinical Cohort Studies*
**作者**：Garcia R, et al.
**摘要**：通过重组PLIN3蛋白制备抗体，发现其在动脉粥样硬化患者血清中高表达，且体外实验表明PLIN3促进巨噬细胞脂质蓄积，提示其作为心血管疾病生物标志物的潜力。
---
**建议**：如需真实文献，可通过**PubMed**或**Google Scholar**搜索关键词：`recombinant human PLIN protein` `perilipin expression` `lipid metabolism`，并筛选近5年高被引研究。
Perilipin (PLIN) proteins are a conserved family of lipid-droplet-associated proteins critical for regulating lipid storage and metabolism in eukaryotic cells. In humans, the PLIN family comprises five members (PLIN1–PLIN5), each with distinct tissue expression patterns and functions. PLIN1. the most studied isoform, is predominantly expressed in adipocytes and steroidogenic cells, where it coats lipid droplets to modulate lipolysis by interacting with lipases and co-regulators. PLIN2 and PLIN3 are ubiquitously expressed and involved in stabilizing lipid droplets in non-adipose tissues, while PLIN4 and PLIN5 play specialized roles in tissues like skeletal muscle and liver, influencing fatty acid oxidation.
Recombinant human PLIN proteins are produced using expression systems (e.g., E. coli, mammalian cells) for structural and functional studies. These engineered proteins retain key domains, such as the PAT (Perilipin, ADRP, TIP47) region, enabling researchers to investigate their phosphorylation-dependent interactions with enzymes like hormone-sensitive lipase (HSL) or adipose triglyceride lipase (ATGL). Studies leveraging recombinant PLINs have clarified their roles in metabolic disorders, including obesity, diabetes, and atherosclerosis, highlighting their potential as therapeutic targets for modulating lipid homeostasis. Ongoing research focuses on PLIN isoform-specific mechanisms and their implications in metabolic diseases.
×
