| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NR2F1 |
| Uniprot No | P10589 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-423aa |
| 氨基酸序列 | MAMVVSSWRDPQDDVAGGNPGGPNPAAQAARGGGGGAGEQQQQAGSGAPHTPQTPGQPGAPATPGTAGDKGQGPPGSGQSQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPNPGQYALTNGDPLNGHCYLSGYISLLLRAEPYPTSRYGSQCMQPNNIMGIENICELAARLLFSAVEWARNIPFFPDLQITDQVSLLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDAAHIESLQEKSQCALEEYVRSQYPNQPSRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMSIQCS |
| 预测分子量 | 50.2 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NR2F1重组蛋白的3篇参考文献的简要信息(注：以下内容基于领域内典型研究方向的模拟概括，实际文献需通过学术数据库验证)：
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1. **标题**: *Structural Insights into NR2F1 DNA Binding Domain and Its Role in Transcriptional Regulation*
**作者**: Smith J, et al.
**摘要**: 本研究解析了NR2F1重组蛋白DNA结合域(DBD)的晶体结构，揭示了其与靶基因启动子结合的分子机制，为理解其在胚胎发育和细胞分化中的调控作用提供结构基础。
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2. **标题**: *Functional Characterization of Recombinant NR2F1 in Neural Stem Cell Differentiation*
**作者**: Lee S, et al.
**摘要**: 通过体外表达纯化的NR2F1重组蛋白，证明其通过调控Notch信号通路促进神经干细胞向特定神经元亚型分化，提示其在神经发育疾病中的潜在治疗价值。
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3. **标题**: *NR2F1 Recombinant Protein Attenuates Tumor Growth by Modulating Angiogenesis in Breast Cancer*
**作者**: Garcia R, et al.
**摘要**: 研究发现，外源性NR2F1重组蛋白通过抑制VEGF信号通路降低乳腺癌模型中的血管生成，表明其作为肿瘤治疗靶点的潜力。
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4. **标题**: *Optimization of NR2F1 Recombinant Protein Expression in E. coli for High-Yield Production*
**作者**: Chen L, et al.
**摘要**: 报道了一种在大肠杆菌中高效表达和纯化NR2F1重组蛋白的优化方法，解决了蛋白可溶性和稳定性问题，为后续功能研究提供可靠技术方案。
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如需具体文献，建议通过PubMed或Web of Science检索关键词“NR2F1 recombinant protein”“COUP-TFI purification”等获取最新研究。
**Background of NR2F1 Recombinant Protein**
NR2F1 (Nuclear Receptor Subfamily 2 Group F Member 1), also known as COUP-TFI (Chicken Ovalbumin Upstream Promoter-Transcription Factor I), is a member of the steroid/thyroid hormone nuclear receptor superfamily. It functions as a transcription factor, regulating gene expression by binding to specific DNA sequences and interacting with co-regulators. NR2F1 plays critical roles in embryonic development, cell differentiation, and tissue homeostasis, particularly in the nervous system, retina, and cardiovascular organs. Its involvement in stem cell pluripotency, angiogenesis, and metabolic processes underscores its broad biological significance.
Recombinant NR2F1 protein is engineered *in vitro* using heterologous expression systems, such as *E. coli* or mammalian cell lines, to produce purified, functional protein for research applications. The recombinant form retains the DNA-binding and ligand-binding domains essential for its transcriptional activity, enabling studies on its molecular mechanisms. Researchers utilize it to investigate NR2F1’s role in gene regulation networks, cellular reprogramming, and disease models, including cancer, neurodevelopmental disorders, and metabolic syndromes.
The production of recombinant NR2F1 often involves affinity tag fusion (e.g., His-tag, GST) for simplified purification and detection. Quality control measures, such as SDS-PAGE and Western blotting, ensure protein integrity and specificity. Its application spans *in vitro* assays (e.g., electrophoretic mobility shift assays, chromatin immunoprecipitation) and *in vivo* studies to explore therapeutic targets.
As dysregulation of NR2F1 is linked to pathologies like Bosch-Boonstra-Schaaf optic atrophy syndrome and tumor progression, recombinant NR2F1 serves as a vital tool for deciphering its pathophysiological roles and developing targeted interventions. Advances in structural biology (e.g., X-ray crystallography) using recombinant protein further elucidate its interaction interfaces, aiding drug discovery efforts.
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