| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAAH |
| Uniprot No | O00519 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 480-579aa |
| 氨基酸序列 | DLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGD IWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS |
| 预测分子量 | 37 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3篇关于FAAH重组蛋白的代表性文献，简要概括如下：
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1. **文献名称**：Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
**作者**：Cravatt BF, et al.
**摘要**：该研究首次克隆并重组表达了人源FAAH蛋白，证实其通过水解作用降解内源性大麻素(如anandamide)，揭示了其在神经信号调控中的关键作用。
2. **文献名称**：Structural basis for human monoglyceride lipase inhibition by the reversible inhibitor SAR127303
**作者**：Romero FA, et al.
**摘要**：通过重组表达人源FAAH蛋白并解析其晶体结构，阐明了酶活性位点的构象特征，为基于结构的抑制剂设计提供了关键依据。
3. **文献名称**：Substrate-specificity of recombinant human fatty acid amide hydrolase
**作者**：Patricelli MP, et al.
**摘要**：利用重组FAAH蛋白系统评估其对多种脂肪酸酰胺底物的催化效率，揭示了酶促反应动力学特征及底物选择性机制。
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以上文献涵盖了FAAH重组蛋白的早期功能研究、结构解析及酶学特性分析，均为该领域的经典研究。如需具体年份或期刊信息，可进一步补充。
**Background of FAAH Recombinant Protein**
Fatty acid amide hydrolase (FAAH) is a membrane-associated enzyme central to lipid metabolism, primarily known for catalyzing the hydrolysis of endogenous fatty acid amides, including the endocannabinoid anandamide (AEA) and oleoylethanolamide (OEA). These signaling molecules regulate diverse physiological processes such as pain perception, mood, inflammation, and appetite. Dysregulation of FAAH activity is linked to neurological disorders (e.g., anxiety, neurodegeneration) and metabolic conditions, making it a therapeutic target.
Recombinant FAAH proteins are engineered versions of the enzyme produced via heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*) for structural and functional studies. The human FAAH gene (*FAAH1*) encodes a 579-amino-acid protein with a serine hydrolase catalytic domain and an unusual transmembrane domain that anchors it to the endoplasmic reticulum. Recombinant expression allows large-scale production of soluble, active FAAH variants, often modified (e.g., truncation of transmembrane regions) to enhance stability and facilitate purification.
Structural studies using recombinant FAAH (e.g., X-ray crystallography) revealed its catalytic mechanism and substrate-binding pockets, enabling rational drug design. FAAH inhibitors (e.g., PF-04457845. URB597) developed using recombinant enzyme assays show promise in preclinical models for pain management and neuroprotection. Additionally, recombinant FAAH is critical for biochemical assays, inhibitor screening, and studying post-translational modifications affecting enzyme activity.
Challenges include maintaining native conformation during purification and addressing species-specific differences (e.g., rodent vs. human FAAH). Current research focuses on isoform FAAH-2. tissue-specific roles, and allosteric modulation. Recombinant FAAH remains indispensable for advancing therapeutic strategies targeting the endocannabinoid system.
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