纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ACSL1 |
Uniprot No | P33121 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 48-145aa |
氨基酸序列 | PKPLKPPCDLSMQSVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQ RGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKTA |
预测分子量 | 36 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. |
1. **"Functional characterization of recombinant human acyl-CoA synthetase 1 (ACSL1) in lipid metabolism"**
- **Authors**: Li et al.
- **摘要**: 本研究通过重组表达人源ACSL1蛋白,验证其在脂肪酸活化中的催化活性,发现ACSL1对长链脂肪酸(C16-C20)具有高度特异性,并揭示其在高脂饮食模型中的代谢调控作用。
2. **"ACSL1-dependent ferroptosis resistance in cancer cells mediated by lipid remodeling"**
- **Authors**: Doll et al.
- **摘要**: 通过重组ACSL1蛋白实验,证明其通过促进多不饱和脂肪酸(PUFA)酯化形成磷脂,抑制铁死亡(ferroptosis),为癌症细胞耐药机制提供了新靶点。
3. **"Crystal structure of ACSL1 reveals conformational changes during substrate binding"**
- **Authors**: Wang et al.
- **摘要**: 首次解析重组小鼠ACSL1蛋白的晶体结构,阐明其底物结合口袋的构象变化及ATP依赖的催化机制,为药物设计提供结构基础。
4. **"ACSL1 deletion in hepatocytes exacerbates hepatic steatosis via impaired VLDL secretion"**
- **Authors**: Klett et al.
- **摘要**: 利用重组ACSL1蛋白体外实验结合肝脏特异性敲除模型,证实ACSL1通过促进甘油三酯合成与极低密度脂蛋白(VLDL)分泌,缓解非酒精性脂肪肝发展。
(注:以上文献为模拟示例,实际引用需核对真实数据库)
ACSL1 (Acyl-CoA Synthetase Long-Chain Family Member 1) is a key enzyme in lipid metabolism that catalyzes the activation of long-chain fatty acids into acyl-CoA esters, a critical step for fatty acid utilization in energy production, membrane synthesis, and signaling pathways. As a member of the ACSL family, ACSL1 exhibits substrate specificity for fatty acids with 12–20 carbon chains. It is ubiquitously expressed, with high levels in metabolic tissues such as liver, adipose, heart, and skeletal muscle, reflecting its role in regulating lipid homeostasis.
Recombinant ACSL1 protein is produced using expression systems like *E. coli* or mammalian cells, enabling detailed study of its enzymatic activity, structural features, and interactions. Researchers employ it to investigate ACSL1's regulation under metabolic stress, hormonal signaling (e.g., insulin, glucagon), and its involvement in diseases such as obesity, diabetes, and cardiovascular disorders. ACSL1 dysfunction is linked to altered lipid partitioning, contributing to ectopic fat deposition and insulin resistance. Its role in cancer is also emerging, as aberrant ACSL1 expression may influence tumor cell proliferation via lipid-driven energy pathways.
Structural studies using recombinant ACSL1 have identified functional domains, including the ATP/AMP-binding site and fatty acid-binding motifs, aiding drug discovery efforts. The protein’s activity is modulated by post-translational modifications (e.g., phosphorylation) and interaction with cellular proteins, which can be analyzed using recombinant variants. By providing a purified, bioactive form of ACSL1. recombinant technology accelerates mechanistic research and therapeutic targeting of lipid-related metabolic disorders.
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