纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RNASE2 |
Uniprot No | P10153 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 28-161aa |
氨基酸序列 | KPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII |
预测分子量 | 17.0 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RNASE2重组蛋白的参考文献示例(注:以下内容为假设性概括,实际文献需通过学术数据库核实):
1. **《Expression and characterization of recombinant human RNASE2 in Escherichia coli》**
- **作者**: Smith A, et al.
- **摘要**: 该研究成功将人源RNASE2基因克隆至大肠杆菌表达系统,通过亲和层析纯化获得高纯度重组蛋白。实验证实重组RNASE2具有核糖核酸酶活性,并对特定病毒RNA表现出降解能力,为抗病毒治疗研究奠定基础。
2. **《Glycosylation modulates the stability and antiviral activity of recombinant RNASE2 in mammalian cells》**
- **作者**: Lee JH, et al.
- **摘要**: 研究在CHO细胞中表达糖基化修饰的重组RNASE2.发现糖基化显著增强蛋白稳定性及对呼吸道合胞病毒(RSV)RNA的切割效率,提示翻译后修饰对其功能的重要性。
3. **《Recombinant RNASE2 suppresses parasite survival in a murine helminth infection model》**
- **作者**: Zhang Y, et al.
- **摘要**: 通过昆虫细胞表达系统制备重组RNASE2.并在蠕虫感染小鼠模型中验证其抗寄生虫活性。结果显示该蛋白通过降解寄生虫RNA并激活宿主免疫反应,显著降低虫体负荷。
4. **《Structural and functional analysis of RNASE2 catalytic residues using site-directed mutagenesis》**
- **作者**: Johnson R, et al.
- **摘要**: 研究通过定点突变技术构建RNASE2重组突变体,结合晶体结构数据揭示关键氨基酸(如His15、Lys38)在酶活性和细胞毒性中的核心作用,为设计功能优化变体提供依据。
建议通过PubMed或Google Scholar以关键词“recombinant RNASE2”、“RNASE2 expression”或“eosinophil-derived neurotoxin”检索真实文献。
**Background of RNASE2 Recombinant Protein**
RNASE2. also known as eosinophil-derived neurotoxin (EDN), is a member of the ribonuclease A (RNASE) superfamily. It is primarily secreted by eosinophils, a type of immune cell involved in anti-parasitic and inflammatory responses. RNASE2 exhibits ribonucleolytic activity, enabling it to cleave single-stranded RNA, a mechanism critical for its role in host defense against RNA viruses and parasites. Unlike its close homolog RNASE3 (eosinophil cationic protein), RNASE2 has weaker cytotoxic effects but demonstrates potent neurotoxic and antiviral properties.
The recombinant RNASE2 protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to ensure high purity and bioactivity. Recombinant production allows for precise control over post-translational modifications, enhancing its stability and functional consistency for research or therapeutic applications. Structurally, RNASE2 contains conserved catalytic residues (His-Lys-His) essential for enzymatic activity and a cationic region that facilitates interactions with negatively charged viral or microbial surfaces.
Research highlights RNASE2's dual role in immunity: (1) Direct pathogen clearance via RNA degradation and (2) modulation of immune responses by acting as an alarmin to activate dendritic cells or enhance T-cell responses. Its antiviral activity against HIV, respiratory syncytial virus (RSV), and influenza has been documented, positioning it as a potential therapeutic candidate. Additionally, elevated RNASE2 levels are linked to eosinophil-associated diseases (e.g., asthma, allergies), making it a biomarker for disease monitoring.
In cancer biology, RNASE2's role remains underexplored, though its ribonuclease activity and immunomodulatory functions suggest potential antitumor applications. Ongoing studies focus on engineering RNASE2 variants to improve specificity, reduce off-target effects, and optimize delivery systems for clinical translation. Overall, RNASE2 recombinant protein serves as a valuable tool for dissecting eosinophil biology and developing novel antiviral or immunotherapeutic strategies.
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