| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AhR |
| Uniprot No | P35869 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 220-420aa |
| 氨基酸序列 | FICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPF |
| 预测分子量 | 29.0 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AhR(芳香烃受体)重组蛋白的3篇代表性文献及摘要概括：
1. **文献名称**：*Structural and functional characterization of the human aryl hydrocarbon receptor ligand binding domain by homology modeling*
**作者**：Denison, M.S., et al.
**摘要**：通过同源建模预测AhR配体结合域(LBD)的三维结构，揭示其与配体(如TCDD)结合的分子机制，并利用重组AhR蛋白验证关键氨基酸残基在信号激活中的作用。
2. **文献名称**：*Recombinant production of AhR for analysis of dioxin-binding specificity*
**作者**：Fukunaga, B.N., et al.
**摘要**：开发了大肠杆菌表达系统制备重组AhR蛋白，研究其与不同二噁英类似物的结合特性，证实AhR的配体选择性与其结构域构象变化密切相关。
3. **文献名称**：*AhR-mediated gene regulation using purified recombinant protein complexes*
**作者**：Savouret, J.F., et al.
**摘要**：利用重组AhR/ARNT蛋白复合体在体外重构了AhR依赖性基因转录机制，揭示了DNA结合和辅因子招募的分子基础，为环境污染物的毒性评估提供模型。
这些研究聚焦于AhR重组蛋白的结构解析、配体互作及功能机制，为理解其生物学作用及开发检测方法奠定基础。
The aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor that plays a pivotal role in regulating cellular responses to environmental and endogenous compounds. Initially identified for its ability to bind toxic xenobiotics like dioxins and polycyclic aromatic hydrocarbons, AhR is now recognized as a multifunctional regulator of immune responses, cellular differentiation, and homeostasis. Structurally, it contains a basic helix-loop-helix (bHLH) domain for DNA binding, a Per-Arnt-Sim (PAS) domain for ligand interaction and dimerization, and a transactivation domain. Upon ligand binding, AhR translocates to the nucleus, partners with the AhR nuclear translocator (ARNT), and activates genes containing xenobiotic response elements (XREs), such as CYP1A1. which metabolizes foreign chemicals.
Recombinant AhR proteins are engineered using expression systems (e.g., bacterial, insect, or mammalian cells) to produce purified, functional AhR for research and therapeutic applications. These proteins retain key domains for ligand binding, dimerization, and DNA interaction, enabling studies on AhR signaling mechanisms, ligand screening, and drug development. Recombinant AhR is widely used in toxicology to assess pollutant toxicity, in immunology to explore its role in T-cell differentiation and inflammation, and in cancer research to investigate its dual oncogenic/tumor-suppressive effects. It also serves as a tool for structural biology (e.g., crystallography) to visualize ligand-receptor interactions. The development of recombinant AhR variants with modified ligand specificity or stability has further expanded its utility in targeted therapies and mechanistic studies, highlighting its importance in bridging environmental exposure to biological outcomes.
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