| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLIN4 |
| Uniprot No | Q96Q06 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 308-418aa |
| 氨基酸序列 | GVDTSKTVLTGTKDTVCSGVTGAMNVAKGTIQTGVDTTKTVLTGTKNTVCSGVTGAVNLAKEAIQGGLDTTKSMVMGTKDTMSTGLTGAANVAKGAMQTGLNTTQNIATGT |
| 预测分子量 | 12.9 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PLIN4重组蛋白相关的模拟参考文献(注：内容为虚构示例，实际文献需通过学术数据库查询)：
1. **文献名称**：*Recombinant PLIN4 Expression and Its Role in Lipid Droplet Dynamics*
**作者**：Chen L, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组PLIN4蛋白，验证其与脂滴表面结合的能力，发现PLIN4通过调控脂解酶活性影响脂肪储存代谢。
2. **文献名称**：*Structural Characterization of Human PLIN4 Using Recombinant Protein Technology*
**作者**：Martinez R, et al.
**摘要**：通过X射线晶体学解析了重组PLIN4蛋白的C端结构域，揭示其与脂滴膜相互作用的分子机制，为肥胖相关疾病的靶点研究提供依据。
3. **文献名称**：*PLIN4 Recombinant Protein Modulates Adipocyte Differentiation In Vitro*
**作者**：Kim S, et al.
**摘要**：利用哺乳动物细胞表达系统获得功能性PLIN4重组蛋白，实验证明其通过激活PPARγ通路促进前脂肪细胞分化，提示其在代谢调控中的潜在应用。
建议通过PubMed、Google Scholar等平台检索真实文献，关键词：**PLIN4 recombinant protein**, **Perilipin 4 expression**, **lipid metabolism**。
**Background of PLIN4 Recombinant Protein**
Perilipin-4 (PLIN4), also known as S3-12. is a lipid droplet-associated protein belonging to the perilipin family, which includes PLIN1–PLIN5. These proteins play critical roles in lipid storage and metabolism by regulating the formation, stabilization, and degradation of lipid droplets (LDs). PLIN4 is predominantly expressed in adipose tissue and steroidogenic cells, where it coats LDs and modulates interactions with lipases and other regulatory proteins. Unlike other perilipins, PLIN4 contains unique repetitive sequences, contributing to its large molecular weight and distinct functional properties.
Recombinant PLIN4 protein is engineered *in vitro* using expression systems (e.g., bacterial, mammalian, or insect cells) to produce purified, functional PLIN4 for research. Its recombinant form enables studies on LD dynamics, lipolysis, and metabolic disorders such as obesity, diabetes, and atherosclerosis. PLIN4’s role in promoting lipid storage and inhibiting uncontrolled lipolysis makes it a potential therapeutic target. Researchers also explore its involvement in cancer, where altered lipid metabolism supports tumor growth.
Structurally, PLIN4 contains N-terminal α-β hydrolase domains and C-terminal amphipathic helices, facilitating LD binding. Post-translational modifications, including phosphorylation, regulate its activity. However, studying native PLIN4 is challenging due to its low solubility and membrane association. Recombinant technology overcomes these hurdles, allowing biochemical assays, antibody development, and structural studies.
Recent advances in recombinant protein production, such as codon optimization and fusion tags, have improved PLIN4 yield and stability. Despite progress, functional redundancy within the perilipin family and incomplete structural data remain challenges. Ongoing research aims to elucidate PLIN4’s precise mechanisms and therapeutic potential, leveraging recombinant tools to dissect its role in health and disease.
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