纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ACSM1 |
Uniprot No | Q08AH1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 32-577aa |
氨基酸序列 | LSEFGAPRW NDYEVPEEFN FASYVLDYWA QKEKEGKRGP NPAFWWVNGQ GDEVKWSFRE MGDLTRRVAN VFTQTCGLQQ GDHLALMLPR VPEWWLVAVG CMRTGIIFIP ATILLKAKDI LYRLQLSKAK GIVTIDALAS EVDSIASQCP SLKTKLLVSD HSREGWLDFR SLVKSASPEH TCVKSKTLDP MVIFFTSGTT GFPKMAKHSH GLALQPSFPG SRKLRSLKTS DVSWCLSDSG WIVATIWTLV EPWTAGCTVF IHHLPQFDTK VIIQTLLKYP INHFWGVSSI YRMILQQDFT SIRFPALEHC YTGGEVVLPK DQEEWKRRTG LLLYENYGQS ETGLICATYW GMKIKPGFMG KATPPYDVQV IDDKGSILPP NTEGNIGIRI KPVRPVSLFM CYEGDPEKTA KVECGDFYNT GDRGKMDEEG YICFLGRSDD IINASGYRIG PAEVESALVE HPAVAESAVV GSPDPIRGEV VKAFIVLTPQ FLSHDKDQLT KELQQHVKSV TAPYKYPRKV EFVSELPKTI TGKIERKELR KKETGQM |
预测分子量 | 65,2 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ACSM1重组蛋白的3篇示例文献及其摘要(注:以下文献为虚构示例,仅供格式参考):
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1. **文献名称**: "Heterologous Expression and Functional Characterization of Human ACSM1 in Escherichia coli"
**作者**: Smith J, et al.
**摘要**: 本研究成功将人类ACSM1基因克隆至大肠杆菌表达系统,通过His标签纯化获得高纯度重组蛋白。酶活性分析显示,重组ACSM1可催化中链脂肪酸(如辛酸)的酰基辅酶A合成,最适pH为7.5.Km值为15 μM,证实其体外功能活性。
2. **文献名称**: "Structural Insights into ACSM1 Catalytic Mechanism by X-ray Crystallography"
**作者**: Zhang L, et al.
**摘要**: 通过X射线晶体学解析了ACSM1重组蛋白的3D结构(分辨率2.1 Å),揭示了其ATP/脂肪酸结合域的关键氨基酸残基。突变实验证实Asp203和Arg307在底物识别中起核心作用,为开发靶向抑制剂提供结构基础。
3. **文献名称**: "ACSM1 Recombinant Protein Attenuates Lipid Accumulation in Hepatocyte Models"
**作者**: Tanaka K, et al.
**摘要**: 在哺乳动物细胞中表达ACSM1重组蛋白,发现其过表达可减少肝细胞中甘油三酯沉积并增强脂肪酸氧化能力。机制研究表明ACSM1通过AMPK/mTOR通路调节脂代谢,提示其在非酒精性脂肪肝治疗中的潜在应用。
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**备注**:上述文献为模拟内容,实际研究中请通过PubMed、Web of Science等平台检索真实文献(关键词:ACSM1. recombinant protein, acyl-CoA synthetase)。
ACSM1 (Acyl-CoA Synthetase Medium-Chain Family Member 1) is a key enzyme involved in lipid metabolism, specifically activating medium-chain fatty acids (MCFAs, 4–12 carbons) by catalyzing their conversion into acyl-CoA derivatives. This process is essential for fatty acid utilization in energy production, membrane synthesis, and signaling pathways. The ACSM1 gene is part of the acyl-CoA synthetase family, which exhibits substrate specificity based on chain length. It is predominantly expressed in metabolic tissues such as the liver, adipose tissue, and skeletal muscle, linking it to energy homeostasis and metabolic disorders.
Recombinant ACSM1 protein is engineered for in vitro studies to elucidate its structural and functional properties. Produced using expression systems like *E. coli* or mammalian cells, it retains enzymatic activity, enabling researchers to analyze kinetics, substrate preferences, and regulatory mechanisms. Studies suggest ACSM1 dysregulation may contribute to metabolic syndromes, including obesity, insulin resistance, and non-alcoholic fatty liver disease (NAFLD). Its role in modulating lipid accumulation and inflammation has sparked interest in therapeutic targeting.
Additionally, recombinant ACSM1 aids in drug discovery, serving as a tool for screening inhibitors or activators to modulate fatty acid metabolism. Recent research also explores its interaction with peroxisome proliferator-activated receptors (PPARs), transcription factors regulating lipid metabolism, highlighting potential cross-talk in metabolic pathways. Despite progress, questions remain about tissue-specific isoforms, post-translational modifications, and its precise role in disease progression. Recombinant protein-based approaches continue to advance understanding of ACSM1’s pathophysiological relevance and therapeutic potential.
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