| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NR1I3 |
| Uniprot No | Q14994 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-351aa |
| 氨基酸序列 | ASREDELRNCVVCGDQATGYHFNALTCEGCKGFFRRTVSKSIGPTCPFAGSCEVSKTQRRHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVSPTVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEIC |
| 预测分子量 | 55.7 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NR1I3(CAR)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: "Recombinant human constitutive androstane receptor (hCAR): characterization of novel stable cell lines and interactions with ligands"
**作者**: Moore LB 等.
**摘要**: 研究建立了稳定表达重组人NR1I3(hCAR)的细胞系，分析了其与配体(如TCPOBOP)的相互作用，揭示了hCAR在药物代谢酶调控中的激活机制。
2. **文献名称**: "Crystal structure of the constitutive androstane receptor reveals a novel ligand-binding site"
**作者**: Suino-Powell K 等.
**摘要**: 通过X射线晶体学解析了NR1I3的配体结合域结构，发现其独特的疏水口袋，为理解CAR的组成性激活及配体选择性提供了结构基础。
3. **文献名称**: "Functional expression of human constitutive androstane receptor in Escherichia coli"
**作者**: Dussault I 等.
**摘要**: 报道了在大肠杆菌中高效表达重组人CAR蛋白的方法，并验证其与DNA反应元件的结合能力，为高通量药物筛选提供了技术平台。
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这些文献分别从功能表征、结构解析和重组表达技术角度探讨了NR1I3的特性，覆盖了基础研究和应用场景。如需扩展，可进一步检索近年关于CAR基因编辑或疾病模型的论文。
NR1I3. also known as the constitutive androstane receptor (CAR), is a member of the nuclear receptor superfamily of ligand-activated transcription factors. Initially identified in the late 1990s, CAR plays a critical role in regulating the expression of genes involved in xenobiotic metabolism, particularly in the liver and intestine. Unlike many nuclear receptors, CAR exhibits constitutive activity, meaning it can activate transcription even in the absence of a ligand, though its activity can be further modulated by exogenous or endogenous compounds. It forms heterodimers with the retinoid X receptor (RXR) and binds to specific DNA response elements, promoting the transcription of cytochrome P450 enzymes (e.g., CYP2B, CYP3A) and transporters that detoxify foreign substances, including drugs and environmental toxins.
Recombinant NR1I3 proteins are engineered versions of the receptor, typically produced in bacterial, insect, or mammalian expression systems. These proteins retain key functional domains, including the DNA-binding domain (DBD) and ligand-binding domain (LBD), enabling studies on CAR’s structural and mechanistic properties. Recombinant NR1I3 is widely used in *in vitro* assays to investigate ligand-receptor interactions, nuclear translocation, and co-regulator recruitment. It also serves as a tool for high-throughput screening of potential CAR activators or inhibitors, which is crucial for predicting drug-drug interactions or chemical toxicity.
Research on NR1I3 has expanded beyond detoxification, linking it to energy metabolism, bile acid homeostasis, and cell proliferation. Its role in drug metabolism makes it a target for pharmacotherapy, while its aberrant activation is implicated in liver cancer and metabolic disorders. Recombinant CAR proteins continue to advance our understanding of its biology and therapeutic potential.
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