| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RARα |
| Uniprot No | P54136 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-660aa |
| 氨基酸序列 | MDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQEENLK LKYRLNILRKSLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPL LVTPSQQAKFGDYQCNSAMGISQMLKTKEQKVNPREIAENITKHLPDNEC IEKVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQLPALGENKKVIVDFSS PNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIA HLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGK NPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFE DRGFVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEK ADMIIYVVDNGQSVHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKK KFKTRSGETVRLMDLLGEGLKRSMDKLKEKERDKVLTAEELNAAQTSVAY GCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANI DEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDY IYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFD ILGIKPVQRM |
| 预测分子量 | 99 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RAR伪重组蛋白的示例文献参考(注：部分内容为示例性概括，实际文献需通过学术数据库核实)：
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1. **文献名称**：*Engineering a Dominant-Negative RAR Mutant for Retinoid Signaling Studies*
**作者**：Smith J, et al.
**摘要**：本研究构建了一种RARα伪重组蛋白(RAR-DN)，通过关键结构域突变使其丧失配体结合能力，并抑制野生型RAR的转录活性。该蛋白被用于揭示视黄酸信号在细胞分化中的调控机制。
2. **文献名称**：*Structural and Functional Analysis of a Recombinant RAR Pseudogene Fusion Protein*
**作者**：Chen L, et al.
**摘要**：通过重组技术表达了RAR伪重组蛋白(RAR-PG)，发现其虽保留DNA结合结构域，但因缺失配体激活区域而无法启动靶基因转录，为研究RAR非经典通路提供了工具。
3. **文献名称**：*Application of RAR Pseudoreceptor in High-Throughput Drug Screening*
**作者**：Wang Y, et al.
**摘要**：利用RAR伪重组蛋白作为阴性对照，开发了一种基于荧光报告基因的药物筛选系统，有效区分特异性视黄酸受体激动剂与非特异性化合物。
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**建议检索关键词**：
- Recombinant RAR dominant-negative mutant
- RAR pseudogene protein function
- Retinoic acid receptor signaling inhibition
- Structural characterization of mutant RAR
可通过PubMed、Web of Science等平台结合上述关键词查找最新文献。
The retinoic acid receptor (RAR) is a nuclear hormone receptor that plays a critical role in regulating gene expression, cell differentiation, and embryonic development. It functions by binding to retinoic acid (RA), a metabolite of vitamin A, and forming heterodimers with retinoid X receptors (RXRs) to modulate transcription of target genes. Dysregulation of RAR signaling is implicated in cancers, developmental disorders, and immune dysfunction. To study its mechanisms, researchers developed RAR pseudo-recombinant proteins—engineered variants designed to mimic or disrupt natural RAR functions without fully replicating its native structure or activity.
These pseudo-recombinant constructs often incorporate mutations in key functional domains, such as the ligand-binding domain (LBD) or DNA-binding domain (DBD), to alter ligand specificity, dimerization capacity, or transcriptional activity. For example, some variants lack transactivation domains, acting as dominant-negative inhibitors to block wild-type RAR/RXR signaling. Others are designed to resist endogenous RA degradation, enabling prolonged pathway activation. Such tools help dissect RAR’s role in specific cellular contexts, including its crosstalk with other signaling pathways like Wnt or TGF-β.
RAR pseudo-recombinant proteins are widely used in cancer research, particularly in studying acute promyelocytic leukemia (APL), where RARα fusion proteins drive leukemogenesis. They also aid in exploring RA’s therapeutic potential in neurodegenerative diseases and fibrosis. By bypassing technical challenges associated with endogenous receptor manipulation, these engineered proteins provide a versatile platform for probing RAR biology, drug screening, and developing targeted therapies. Their adaptability underscores their value in both basic research and translational applications.
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