| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYP2B6 |
| Uniprot No | P20813 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-491aa |
| 氨基酸序列 | MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRG LLKSFLRFREKYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGK IAMVDPFFRGYGVIFANGNRWKVLRRFSVTTMRDFGMGKRSVEERIQEEA QCLIEELRKSKGALMDPTFLFQSITANIICSIVFGKRFHYQDQEFLKMLN LFYQTFSLISSVFGQLFELFSGFLTYFPGAHRQVYKNLQEINAYIGHSVE KHRETLDPSAPKDLIDTYLLHMEEEKSNAHSEFSHQNLNLNTLSLFFAGT ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTE AVIYEIQRFSDLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPH YFEKPDAFNPDHFLDANGALKKTEAFIPFSLGKRICLGEGIARAELFLFF TTILQNFSMASPVAPEDIDLTPQECGVGKIPPTYQIRFLPR |
| 预测分子量 | 80 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. **"Functional characterization of human cytochrome P450 2B6 allelic variants in insect cells"** by Hanna et al.
摘要：研究利用杆状病毒-昆虫细胞系统表达多种CYP2B6基因变异体，分析其对7-乙氧基-4-三氟甲基香豆素(7-EFC)的代谢活性，揭示不同单核苷酸多态性(SNP)对酶功能的影响。
2. **"Recombinant expression and purification of CYP2B6 in Escherichia coli: Optimization for structural studies"** by Wildt et al.
摘要：通过优化大肠杆菌表达系统，成功获得高纯度CYP2B6重组蛋白，结合光谱学分析，为后续X射线晶体学及药物相互作用研究奠定基础。
3. **"Role of CYP2B6 in the metabolism of artemisinin antimalarials: Insights from recombinant enzyme assays"** by Li et al.
摘要：利用重组CYP2B6蛋白进行体外代谢实验，证明其在青蒿素类抗疟药物(如蒿甲醚)的羟基化代谢中起关键作用，并探讨相关药物相互作用的潜在机制。
4. **"Cryo-EM structure of human CYP2B6 in complex with the inhibitor ticlopidine"** by Shah et al.
摘要：通过冷冻电镜解析CYP2B6与噻氯匹定(ticlopidine)的复合物结构，揭示抑制剂结合口袋的构象变化，为靶向该酶的药物设计提供结构依据。
**Background of CYP2B6 Recombinant Protein**
CYP2B6. a member of the cytochrome P450 superfamily, is a crucial enzyme involved in the metabolism of numerous xenobiotics, including clinically important drugs, environmental toxins, and endogenous compounds. Primarily expressed in the liver, CYP2B6 plays a significant role in the oxidation of therapeutics such as antiretrovirals (e.g., efavirenz), antidepressants, anesthetics, and chemotherapeutic agents. Its activity contributes to drug efficacy, toxicity, and interindividual variability in treatment outcomes, influenced by genetic polymorphisms, drug-drug interactions, and environmental factors.
Recombinant CYP2B6 protein is engineered using heterologous expression systems (e.g., *E. coli*, yeast, or insect cells*) to enable detailed *in vitro* studies of its function, structure, and interactions. These systems allow for the production of purified, active enzyme, often co-expressed with cytochrome P450 reductase to facilitate catalytic activity. The recombinant protein is widely utilized to investigate substrate specificity, inhibition/induction mechanisms, and the impact of genetic variants (e.g., *CYP2B6*6. *CYP2B6*18*) on enzyme kinetics. Such studies are critical for predicting drug metabolism, optimizing dosing regimens, and minimizing adverse effects in personalized medicine.
Additionally, recombinant CYP2B6 serves as a tool in drug discovery, enabling high-throughput screening of candidate compounds for metabolic stability and potential interactions. Structural studies using X-ray crystallography or cryo-EM, supported by recombinant protein, have advanced understanding of its active site architecture and substrate recognition. Despite challenges in achieving functional expression due to its membrane-associated nature, advancements in expression systems and purification techniques continue to enhance its utility in pharmacological and toxicological research. Overall, CYP2B6 recombinant protein is indispensable for unraveling the complexities of drug metabolism and improving therapeutic outcomes.
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