| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APOC3 |
| Uniprot No | P02656 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-99aa |
| 氨基酸序列 | SEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA |
| 预测分子量 | 24.8 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. |
以下是关于APOC3重组蛋白的3-4篇参考文献示例(注：以下内容为模拟示例，实际文献需通过学术数据库检索获取)：
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1. **文献名称**：*Expression and Purification of Functional Recombinant Human Apolipoprotein C-III in E. coli*
**作者**：Chen L, et al.
**摘要**：研究报道了利用大肠杆菌表达系统高效生产重组人APOC3蛋白的方法，并通过质谱和脂质结合实验验证其生物活性，为后续功能研究提供可靠工具。
2. **文献名称**：*Recombinant APOC3 Modulates Lipoprotein Lipase Activity and Triglyceride Metabolism in vitro*
**作者**：Wang R, et al.
**摘要**：通过体外实验证明重组APOC3蛋白能够抑制脂蛋白脂肪酶(LPL)活性，导致甘油三酯水解减少，揭示了其在调节血脂代谢中的分子机制。
3. **文献名称**：*Crystal Structure of APOC3 Reveals Key Lipid-Binding Domains*
**作者**：Kumar S, et al.
**摘要**：首次解析了重组APOC3蛋白的晶体结构，发现其通过特定疏水区域与脂质颗粒结合，为开发靶向APOC3的降脂药物提供了结构依据。
4. **文献名称**：*Adenoviral Overexpression of Recombinant APOC3 Induces Hypertriglyceridemia in Mice*
**作者**：Gonzalez-Navarro H, et al.
**摘要**：利用腺病毒载体在小鼠中过表达重组APOC3.观察到血浆甘油三酯水平显著升高，证实了APOC3在体内促进高脂血症的作用。
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建议通过PubMed、Web of Science等平台，以关键词“APOC3 recombinant protein”“APOC3 expression”或“APOC3 structure”检索最新文献，重点关注《Journal of Lipid Research》《Atherosclerosis》等期刊的相关研究。
**Background of APOC3 Recombinant Protein**
Apolipoprotein C-III (APOC3) is a small, liver-synthesized protein that plays a critical role in lipid metabolism. It is a component of triglyceride-rich lipoproteins, such as very-low-density lipoproteins (VLDL) and chylomicrons, and functions as a modulator of lipid processing. APOC3 inhibits lipoprotein lipase (LPL), an enzyme responsible for hydrolyzing triglycerides in circulating lipoproteins, and interferes with hepatic uptake of lipoprotein remnants. This regulatory role positions APOC3 as a key factor in maintaining plasma triglyceride levels. Elevated APOC3 expression is strongly associated with hypertriglyceridemia, a risk factor for cardiovascular diseases, pancreatitis, and metabolic syndromes.
The development of recombinant APOC3 protein has been driven by the need to study its molecular mechanisms and therapeutic potential. Recombinant APOC3 is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems, enabling large-scale purification for research. Its applications span *in vitro* studies to elucidate interactions with lipoproteins, receptors (e.g., LDL receptor family), and enzymes like LPL. Additionally, recombinant APOC3 serves as an antigen in immunoassays to measure endogenous APOC3 levels in clinical diagnostics.
Recent interest in APOC3 as a therapeutic target has surged. Genetic studies linking *APOC3* loss-of-function mutations to reduced cardiovascular risk have spurred drug development. Antisense oligonucleotides (e.g., volanesorsen) and monoclonal antibodies targeting APOC3 aim to lower triglycerides and mitigate associated pathologies. Recombinant APOC3 protein is instrumental in validating these therapies, enabling structure-function analyses and high-throughput screening for drug candidates.
Overall, APOC3 recombinant protein bridges basic research and clinical innovation, offering insights into lipid disorders and paving the way for novel treatments targeting metabolic diseases.
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