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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INFα1 |
| Uniprot No | Q63W31 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-88aa |
| 氨基酸序列 | MAKEELIELDGIVDEVLPDSRYRVTLDNGVVVGAYASGQMRRHRIRILAGDRVTLELSVYDLTKGRINFRHKDERRSDAAPRASARRR |
| 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. |
以下是关于重组干扰素(假设为IFN类似物或工程化重组蛋白)的假设性参考文献示例。请注意，这些文献为模拟示例，实际引用时请核实准确性：
1. **"Expression and Purification of Recombinant IFN-α1 in E. coli for Antiviral Therapy"**
- 作者：Johnson, R. et al.
- 摘要：研究利用大肠杆菌系统高效表达重组IFN-α1.优化纯化工艺并验证其在抑制肝炎病毒复制中的活性。
2. **"Structural Modification of Recombinant IFN-β Enhances Stability and Bioactivity"**
- 作者：Chen, L. & Tanaka, M.
- 摘要：通过定点突变改造IFN-β结构，提升其热稳定性及受体结合能力，为长效干扰素制剂开发提供依据。
3. **"Engineered IFN-γ Variants with Improved Antitumor Efficacy in Mouse Models"**
- 作者：Gupta, S. et al.
- 摘要：设计重组IFN-γ类似物，通过体外和体内实验证明其增强的肿瘤微环境穿透能力和凋亡诱导作用。
4. **"PEGylated Recombinant IFN-λ1: Pharmacokinetics and Clinical Potential"**
- 作者：Wang, Y. et al.
- 摘要：评估聚乙二醇化修饰的IFN-λ1重组蛋白的药代动力学特性，显示其半衰期延长且免疫原性降低，适用于慢性病毒感染治疗。
**注意事项**：
- 上述文献为示例，实际研究中请通过PubMed、Google Scholar等平台检索具体关键词(如“recombinant interferon”、“IFN variant”、“engineered IFN”等)。
- 若“INF伪1”为特定蛋白代号，建议核对术语准确性或联系相关领域数据库(如UniProt)获取正式命名。
Interferon (IFN) pseudo-receptor 1 recombinant protein is an engineered biomolecule designed to mimic or modulate IFN signaling pathways. IFNs are cytokines critical for antiviral responses, immune regulation, and antitumor activity, acting through cell-surface receptors (e.g., IFNAR for type I IFNs). However, dysregulated IFN signaling is implicated in autoimmune diseases (e.g., lupus) or viral immune evasion, driving interest in therapeutic interventions.
The "pseudo-receptor 1" concept refers to a modified receptor component, often lacking functional domains, to competitively bind IFN ligands or disrupt receptor complex assembly. This decoy strategy aims to attenuate excessive signaling. Recombinant versions are produced via expression systems (e.g., E. coli, mammalian cells), ensuring proper folding and post-translational modifications. They typically include tags (e.g., His-tag) for purification and tracking.
Research applications include elucidating IFN-receptor interactions, screening inhibitors, or studying signaling crosstalk. Therapeutically, such proteins could balance hyperactive IFN pathways in autoimmunity or enhance antiviral responses by blocking viral IFN antagonists. Challenges include optimizing binding affinity, stability, and delivery. Recent studies explore fusion designs (e.g., Fc fusion for prolonged half-life) and preclinical models to validate efficacy. This protein represents a tailored tool bridging basic research and targeted therapy development in immunology and virology.
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