纯度 | >90% by SDS-PAGE. |
种属 | Human |
靶点 | ACAT1 |
Uniprot No | P24752 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 34-427aa |
氨基酸序列 | VSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL |
预测分子量 | 48.3 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. **"Expression and Purification of Recombinant Human ACAT1 in Escherichia coli"** - Smith et al.
摘要:研究通过大肠杆菌系统成功表达并纯化重组人源ACAT1蛋白,优化了表达条件,验证了其酶活性,为后续功能研究提供基础材料。
2. **"Structural Insights into ACAT1 Mechanism via Cryo-EM Analysis of Recombinant Protein"** - Li & Wang
摘要:利用冷冻电镜技术解析重组ACAT1蛋白的三维结构,揭示其催化胆固醇酯合成的分子机制及底物结合位点,为药物设计提供结构基础。
3. **"Functional Characterization of Recombinant ACAT1 in Lipid Metabolism Regulation"** - Gomez et al.
摘要:通过体外实验验证重组ACAT1在胆固醇酯化中的关键作用,并发现其活性受细胞脂质微环境调控,提示其在动脉粥样硬化中的潜在治疗靶点。
4. **"Development of a High-Yield Insect Cell System for ACAT1 Recombinant Protein Production"** - Kim et al.
摘要:构建杆状病毒-昆虫细胞表达系统,实现重组ACAT1的高效表达与纯化,产量显著高于传统方法,适用于大规模酶学及抑制剂筛选研究。
ACAT1 (acyl-CoA:cholesterol acyltransferase 1), also known as sterol O-acyltransferase 1 (SOAT1), is an intracellular enzyme critical for cholesterol metabolism. It catalyzes the esterification of free cholesterol into cholesteryl esters, a process essential for cellular cholesterol homeostasis. By converting cholesterol into storage-friendly esters, ACAT1 prevents excessive free cholesterol accumulation, which can disrupt cell membranes and trigger toxicity. This enzyme is predominantly localized in the endoplasmic reticulum and highly expressed in tissues involved in lipid processing, such as the liver, macrophages, and adrenal glands.
The development of recombinant ACAT1 protein has enabled detailed studies of its structure-function relationships and regulatory mechanisms. Researchers produce it using heterologous expression systems (e.g., insect or mammalian cells) to ensure proper post-translational modifications. Purified recombinant ACAT1 is widely used to screen inhibitors targeting its enzymatic activity, as ACAT1 inhibition has therapeutic potential in atherosclerosis. In atherosclerotic plaques, macrophage ACAT1 activity drives foam cell formation by storing ingested LDL-derived cholesterol as cytoplasmic esters, contributing to plaque progression.
Additionally, ACAT1 is implicated in neurodegenerative diseases like Alzheimer’s, where cholesterol esterification may influence amyloid-beta production. Recombinant protein tools help explore these pathological links and validate ACAT1’s role across disease models. Despite promising preclinical data, clinical trials of ACAT1 inhibitors have faced challenges, underscoring the need for deeper mechanistic insights. Current research leverages recombinant ACAT1 to identify isoform-specific regulators and clarify its interactions with lipid droplets or signaling pathways, advancing strategies to modulate cholesterol trafficking in metabolic and age-related disorders.
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