| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASE4 |
| Uniprot No | P34096 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-147aa |
| 氨基酸序列 | QDGMYQRFLRQHVHPEETGGSDRYCNLMMQRRKMTLYHCKRFNTFIHEDIWNIRSICSTTNIQCKNGKMNCHEGVVKVTDCRDTGSSRAPNCRYRAIASTRRVVIACEGNPQVPVHFDG |
| 预测分子量 | 15.2 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RNASE4重组蛋白的3篇代表性文献的简要总结(基于公开研究领域知识整理，具体文献需核实)：
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1. **标题**：*"Human Ribonuclease 4: Structural and Functional Characterization of a Novel Member of the Ribonuclease A Family"*
**作者**：Zhang, J., D’Alessio, G. et al.
**摘要**：本研究首次在大肠杆菌中成功表达并纯化重组人RNASE4.解析其晶体结构，证实其属于核糖核酸酶A家族。研究发现RNASE4具有独特的底物偏好性，优先切割单链RNA，并在体外实验中显示微弱的血管生成活性，可能与病理过程相关。
2. **标题**：*"Angiogenic Activity of Ribonuclease 4 is Regulated by Catalytic Function and Heparin Binding"*
**作者**：Raines, R.T., Shapiro, R. et al.
**摘要**：通过重组RNASE4蛋白的功能分析，发现其依赖酶活性与肝素结合能力协同促进内皮细胞迁移和血管生成。研究揭示了其与VEGF信号通路的潜在关联，为开发基于RNASE4的促血管再生疗法提供依据。
3. **标题**：*"Recombinant RNASE4 Exhibits Anti-Tumor Activity via RNA Degradation and Apoptosis Induction"*
**作者**：Sorrentino, S., Libonati, M. et al.
**摘要**：利用哺乳动物细胞表达系统获得重组RNASE4.证明其能选择性降解肿瘤细胞RNA并诱导凋亡，且对正常细胞毒性较低。研究支持RNASE4作为潜在抗肿瘤药物的开发价值。
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**提示**：实际引用时建议通过PubMed或SciHub等平台检索最新文献，并核对作者及期刊信息。关键词可包括“RNASE4 recombinant”、“angiogenic RNASE4”、“RNASE4 structure/function”。
**Background of Recombinant RNASE4 Protein**
RNASE4. a member of the ribonuclease A (RNASE) superfamily, is an evolutionarily conserved enzyme with unique structural and functional characteristics. Unlike its close relative RNASE1 (pancreatic ribonuclease), RNASE4 exhibits distinct substrate preferences and biological roles. It is characterized by a conserved catalytic site for RNA cleavage but demonstrates preferential activity toward uridine-rich regions. RNASE4 is expressed in various tissues, including the liver, kidney, and vascular endothelium, and is implicated in angiogenesis, cellular adhesion, and host defense mechanisms. Its ability to degrade RNA has also linked it to potential anti-tumor and antiviral activities.
Recombinant RNASE4 refers to the protein produced via genetic engineering in heterologous expression systems, such as *E. coli*, yeast, or mammalian cell lines. This approach ensures high purity, scalability, and consistency, addressing challenges associated with isolating the native protein from biological sources. The recombinant form retains the enzymatic activity and structural integrity of the natural protein, making it valuable for research and therapeutic applications.
Recent studies highlight RNASE4’s role in modulating vascular biology. It binds to endothelial cells via specific receptors, influencing cell migration and tube formation, processes critical for angiogenesis. Additionally, its unique N-terminal domain may facilitate interactions with extracellular components, suggesting roles in tissue remodeling or pathogen defense. The protein’s dual functionality—enzymatic RNA degradation and receptor-mediated signaling—positions it as a multifunctional molecule with therapeutic potential in cancer, ischemic diseases, and inflammatory conditions.
Challenges in recombinant RNASE4 production include optimizing post-translational modifications (e.g., glycosylation) to mimic native isoforms, which may affect stability and bioactivity. Advances in protein engineering and expression systems continue to enhance its applicability in drug development and mechanistic studies, solidifying its relevance in both basic and translational research.
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