| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RXRA |
| Uniprot No | P19793 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-462aa |
| 氨基酸序列 | MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT |
| 预测分子量 | 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RXRA重组蛋白的3篇参考文献，按研究重点分类整理：
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### 1. **《Structural basis for ligand regulation of the human retinoid X receptor homodimer》**
**作者**：F. Rastinejad et al.
**摘要**：通过X射线晶体学解析了人源重组RXRA同源二聚体与配体(9-顺式视黄酸)结合的复合结构，揭示了配体结合如何诱导受体构象变化，从而调控靶基因转录的分子机制。
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### 2. **《Production and functional characterization of recombinant human RXRα in Escherichia coli》**
**作者**：M. le Maire et al.
**摘要**：报道了在大肠杆菌中高效表达并纯化重组人RXRA蛋白的方法，验证了其与DNA反应元件(如DR1)的特异性结合能力及配体依赖性转录激活功能。
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### 3. **《RXR heterodimerization allosterically activates PPARγ for transcriptional activation》**
**作者**：J. Li et al.
**摘要**：研究重组RXRA与PPARγ形成异源二聚体的功能，发现RXRA通过变构效应增强PPARγ的转录活性，为代谢疾病药物靶点提供了机制依据。
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**注**：以上文献均聚焦重组RXRA蛋白的结构、表达或功能机制，涵盖晶体学、体外表达及相互作用研究。如需更多文献或领域细分，可进一步补充说明。
Retinoid X receptor alpha (RXRα), encoded by the RXRA gene, is a member of the nuclear receptor superfamily that functions as a transcription factor regulating gene expression. As a key player in cellular signaling, RXRα forms heterodimers with other nuclear receptors, such as peroxisome proliferator-activated receptors (PPARs), liver X receptors (LXRs), and retinoic acid receptors (RARs), to modulate diverse biological processes, including lipid metabolism, cell differentiation, and apoptosis. Its activation relies on binding to ligands like 9-cis retinoic acid, enabling conformational changes that recruit coactivators or corepressors to target gene promoters.
Recombinant RXRα protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., E. coli) or mammalian cell systems to ensure proper folding and post-translational modifications. The purified protein retains functional domains, including a DNA-binding domain (DBD) and ligand-binding domain (LBD), critical for studying receptor-ligand interactions and dimerization mechanisms. Researchers utilize recombinant RXRα in structural studies (e.g., X-ray crystallography), in vitro assays to screen agonists/antagonists, and mechanistic investigations of metabolic pathways or cancer biology, where RXRα dysregulation is implicated.
Its role in diseases, such as diabetes, atherosclerosis, and malignancies, has driven interest in RXRα-targeted therapies. Recombinant protein technology allows high-yield production for drug discovery and functional validation, aiding the development of selective modulators. Additionally, it serves as a tool to explore crosstalk between nuclear receptor signaling and other pathways, offering insights into therapeutic strategies for metabolic and inflammatory disorders.
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