纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | AEA |
Uniprot No | P34972 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-360aa |
氨基酸序列 | MEECWVTEIANGSKDGLDSNPMKDYMILSGPQKTAVAVLCTLLGLLSALENVAVLYLILSSHQLRRKPSYLFIGSLAGADFLASVVFACSFVNFHVFHGVDSKAVFLLKIGSVTMTFTASVGSLLLTAIDRYLCLRYPPSYKALLTRGRALVTLGIMWVLSALVSYLPLMGWTCCPRPCSELFPLIPNDYLLSWLLFIAFLFSGIIYTYGHVLWKAHQHVASLSGHQDRQVPGMARMRLDVRLAKTLGLVLAVLLICWFPVLALMAHSLATTLSDQVKKAFAFCSMLCLINSMVNPVIYALRSGEIRSSAHHCLAHWKKCVRGLGSEAKEEAPRSSVTETEADGKITPWPDSRDLDLSDC |
预测分子量 | 39,6 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AEA(假设为Anandamide相关)重组蛋白研究的3条概括性参考文献示例:
1. **文献名称**:*Heterologous Expression and Functional Characterization of Recombinant Anandamide-Synthesizing Enzymes in Yeast*
**作者**:Zhang L et al.
**摘要**:研究利用酵母表达系统重组表达了N-酰基磷脂酰乙醇胺磷脂酶D(NAPE-PLD),成功实现AEA的高效体外合成,并分析了其催化活性和稳定性。
2. **文献名称**:*Optimization of Recombinant FAAH Production in Pichia pastoris for Therapeutic Applications*
**作者**:Martinez R et al.
**摘要**:通过优化毕赤酵母表达系统,规模化生产重组脂肪酸酰胺水解酶(FAAH),评估其在AEA代谢调控中的潜在治疗价值。
3. **文献名称**:*Crystallographic Analysis of Recombinant CB2 Receptor Bound to Anandamide Analogues*
**作者**:Thompson M et al.
**摘要**:利用重组表达的人源CB2大麻素受体,解析其与AEA类似物复合物的晶体结构,揭示配体结合域的关键相互作用位点。
注:以上为基于领域知识的概括性示例,实际文献需通过学术数据库(如PubMed、Google Scholar)检索确认。
**Background of AEA Recombinant Proteins**
Arachidonoylethanolamine (AEA), commonly known as anandamide, is an endogenous cannabinoid neurotransmitter that plays a critical role in regulating physiological processes such as pain perception, mood, appetite, and immune response. It binds primarily to cannabinoid receptors (CB1 and CB2), activating signaling pathways that modulate neuronal and immune functions. Due to its lipid nature and rapid enzymatic degradation by fatty acid amide hydrolase (FAAH), studying AEA's biological mechanisms or therapeutic potential in native form poses challenges.
Recombinant protein technology has emerged as a pivotal tool to overcome these limitations. AEA-related recombinant proteins, including engineered enzymes (e.g., FAAH, N-acylphosphatidylethanolamine phospholipase D), receptors (CB1/CB2), or AEA-binding proteins, are produced via heterologous expression systems (e.g., *E. coli*, yeast, mammalian cells*). These proteins retain functional properties while offering enhanced stability, scalability, and purity compared to native isolates. For instance, recombinant CB1/CB2 receptors enable high-throughput drug screening for cannabinoid-based therapies, while modified FAAH variants aid in studying AEA metabolism or developing enzyme inhibitors.
Additionally, recombinant AEA-associated proteins facilitate structural studies (e.g., X-ray crystallography) to elucidate ligand-receptor interactions, guiding rational drug design. Their applications extend to diagnostic tools, biosensors, and targeted therapies for conditions like chronic pain, anxiety, and neurodegenerative disorders.
In summary, AEA recombinant proteins bridge gaps in cannabinoid research, offering precise, reproducible tools to decode AEA's complex biology and accelerate therapeutic innovation.
×