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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IFNA7 |
| Uniprot No | P01567 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-189aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D |
| 预测分子量 | 22 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IFNA7重组蛋白的模拟参考文献示例(注：部分内容为假设性概括，实际文献需通过学术数据库验证)：
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1. **文献名称**：*Cloning and Expression of Human Interferon Alpha-7 in E. coli*
**作者**：Smith J, et al.
**摘要**：本研究成功克隆了人IFNA7基因，并利用大肠杆菌系统实现重组表达。纯化的蛋白在体外实验中显示出抗病毒活性，为后续干扰素亚型功能研究奠定基础。
2. **文献名称**：*Structural and Functional Characterization of Recombinant IFNA7*
**作者**：Zhang Y, et al.
**摘要**：通过哺乳动物细胞表达系统获得糖基化修饰的IFNA7重组蛋白，分析其三维结构及受体结合特性，发现其与IFNAR受体的亲和力与其他α亚型存在差异。
3. **文献名称**：*IFNA7 Recombinant Protein Enhances Antitumor Immunity in Murine Models*
**作者**：Brown K, et al.
**摘要**：在小鼠肿瘤模型中，重组IFNA7通过激活NK细胞和增强MHC-I抗原呈递，显著抑制肿瘤生长，提示其潜在的免疫治疗应用价值。
4. **文献名称**：*Comparative Analysis of IFNA7 and IFNA2 Signaling Pathways*
**作者**：Lee S, et al.
**摘要**：比较重组IFNA7与IFNA2对JAK-STAT信号通路的激活差异，发现IFNA7诱导独特的基因表达谱，可能与其抗病毒特异性相关。
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建议通过PubMed或Web of Science搜索关键词“Recombinant IFNA7”或“Interferon alpha-7”获取真实文献数据。
Interferon alpha-7 (IFNA7) is a member of the type I interferon (IFN) family, a group of cytokines critical in mediating innate immune responses against viral infections and modulating adaptive immunity. Encoded by the *IFNA7* gene in humans, it shares structural homology with other IFN-α subtypes, featuring a conserved alpha-helical structure and binding to the same heterodimeric receptor complex (IFNAR1/IFNAR2). However, subtle sequence variations among subtypes, including IFNA7. may influence receptor affinity, signaling dynamics, and biological activity.
Recombinant IFNA7 protein is produced using biotechnological platforms, often via expression in *E. coli* or mammalian cell systems. Bacterial systems yield non-glycosylated proteins, while mammalian expression preserves post-translational modifications, potentially affecting stability and activity. Its production enables studies on subtype-specific functions, as individual IFN-α variants exhibit differences in antiviral potency, immunomodulatory effects, and therapeutic efficacy.
Research on recombinant IFNA7 has explored its role in antiviral defense, particularly against hepatitis B/C viruses and certain cancers. Like other type I IFNs, it activates JAK-STAT signaling, inducing interferon-stimulated genes (ISGs) that inhibit viral replication and promote immune cell activation. However, clinical applications face challenges, including short half-life and systemic toxicity. Current studies focus on engineering IFNA7 variants or delivery systems to enhance specificity and reduce side effects.
While less studied compared to IFN-alpha-2 or IFN-beta, IFNA7 remains a subject of interest for understanding interferon diversity and developing targeted immunotherapies. Its recombinant form serves as a tool for dissecting signaling mechanisms and optimizing therapeutic strategies in virology and oncology.
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