| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AADAC |
| Uniprot No | P22760 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-399aa |
| 氨基酸序列 | PDNVEEPWRMMWINAHLKTIQNLATFVELLGLHHFMDSFKVVGSFDEVPP TSDENVTVTETKFNNILVRVYVPKRKSEALRRGLFYIHGGGWCVGSAALS GYDLLSRWTADRLDAVVVSTNYRLAPKYHFPIQFEDVYNALRWFLRKKVL AKYGVNPERIGISGDSAGGNLAAAVTQQLLDDPDVKIKLKIQSLIYPALQ PLDVDLPSYQENSNFLFLSKSLMVRFWSEYFTTDRSLEKAMLSRQHVPVE SSHLFKFVNWSSLLPERFIKGHVYNNPNYGSSELAKKYPGFLDVRAAPLL ADDNKLRGLPLTYVITCQYDLLRDDGLMYVTRLRNTGVQVTHNHVEDGFH GAFSFLGLKISHRLINQYIEWLKENL |
| 预测分子量 | 63 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AADAC重组蛋白的3篇参考文献示例(注：文献为虚拟示例，实际引用需核实)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Human AADAC in Escherichia coli*
**作者**：Tanaka K, et al.
**摘要**：研究报道了人源AADAC重组蛋白在大肠杆菌中的高效表达与纯化，证实其具有水解醋酸芳胺类化合物(如抗肿瘤前药CPT-11)的活性，并分析了酶动力学参数。
2. **文献名称**：*Structural Insights into Substrate Specificity of AADAC through Recombinant Protein Crystallography*
**作者**：Zhang Y, et al.
**摘要**：利用重组AADAC蛋白的晶体结构解析，揭示了其底物结合口袋的关键氨基酸残基，解释了其对不同芳基乙酰胺类药物的选择性脱乙酰机制。
3. **文献名称**：*Role of Recombinant AADAC in Lipid Metabolism: In Vitro Inhibition Studies*
**作者**：Matsuda S, et al.
**摘要**：通过体外实验证明，重组AADAC不仅参与药物代谢，还可能通过调节胆固醇酯水解影响脂质代谢，为代谢疾病研究提供新方向。
(注：如需真实文献，建议在PubMed或Web of Science检索关键词“AADAC recombinant protein”或“recombinant arylacetamide deacetylase”。)
Arylacetamide deacetylase (AADAC) is a hydrolytic enzyme encoded by the AADAC gene, primarily expressed in the liver and gastrointestinal tract. It belongs to the serine hydrolase superfamily and plays a role in metabolizing xenobiotics, including clinical drugs, environmental toxins, and endogenous lipids. AADAC catalyzes the deacetylation of substrates such as arylacetamide drugs (e.g., rifamycins) and lipid-derived compounds, influencing their bioavailability, toxicity, or pharmacological activity. Its activity impacts drug pharmacokinetics and interindividual variability in therapeutic responses.
Recombinant AADAC protein is produced using genetic engineering techniques, typically by expressing the AADAC gene in heterologous systems like Escherichia coli or mammalian cell lines (e.g., HEK293). This allows large-scale production of the purified enzyme for functional and structural studies. Recombinant AADAC retains catalytic properties of the native enzyme, enabling researchers to investigate substrate specificity, enzyme kinetics, and inhibition mechanisms in vitro. It serves as a critical tool for drug metabolism studies, toxicity screening, and personalized medicine research.
Interest in AADAC has grown due to its role in activating prodrugs (e.g., irinotecan) and its association with metabolic disorders. Genetic polymorphisms in AADAC may contribute to altered drug efficacy or adverse effects. Recombinant variants are also used to study enzyme-drug interactions, aiding the development of safer pharmaceuticals. Recent studies explore its potential in cancer metabolism and lipid homeostasis, expanding its relevance beyond detoxification pathways. Despite progress, questions remain about its physiological substrates and regulatory mechanisms, driving ongoing research with recombinant AADAC models.
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