首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IFNG |
| Uniprot No | P01579 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-166aa |
| 氨基酸序列 | QDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ |
| 预测分子量 | 40.0 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IFNG(干扰素γ)重组蛋白的3篇代表性文献及其摘要概述：
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1. **文献名称**：*Cloning and expression of the human immune interferon gene*
**作者**：Gray, P.W., Goeddel, D.V.
**摘要**：该研究首次报道了人类IFN-γ基因的克隆及在大肠杆菌中的重组表达，证实重组蛋白具有与天然IFN-γ相似的抗病毒和免疫调节活性，为后续研究奠定基础。
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2. **文献名称**：*Interferon gamma-1b in the treatment of chronic granulomatous disease*
**作者**：International Chronic Granulomatous Disease Cooperative Study Group
**摘要**：通过临床试验验证重组IFN-γ对慢性肉芽肿病患者的疗效，证明其可显著减少严重感染发生率，并推动其作为免疫调节疗法的临床应用。
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3. **文献名称**：*Structural basis of receptor recognition by human interferon-γ*
**作者**：Thiel, D.J., et al.
**摘要**：解析了重组人IFN-γ与其受体的复合物晶体结构，揭示了关键结合位点，为优化重组蛋白的靶向治疗设计提供分子基础。
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**扩展方向**：IFN-γ重组蛋白的研究还可关注其在肿瘤免疫治疗(如联合检查点抑制剂)、自身免疫疾病模型中的双重作用，或新型表达系统(如哺乳动物细胞系)的优化生产。
Interferon-gamma (IFN-γ), encoded by the IFNG gene, is a pleiotropic cytokine central to innate and adaptive immunity. Primarily produced by activated T lymphocytes and natural killer (NK) cells, it plays critical roles in host defense against intracellular pathogens, tumor surveillance, and immune regulation. IFN-γ binds to a heterodimeric receptor (IFNGR1/IFNGR2), triggering JAK-STAT signaling pathways that drive the expression of genes involved in macrophage activation, antigen presentation, and Th1 immune responses. Its functions include enhancing microbial killing, promoting MHC class I/II expression, and modulating angiogenesis and apoptosis.
Recombinant IFN-γ (rIFN-γ) is produced via genetic engineering in expression systems such as *E. coli* or mammalian cell lines. Bacterial systems yield non-glycosylated proteins, while mammalian cells (e.g., CHO) produce glycosylated forms closer to native human IFN-γ. The recombinant protein retains bioactivity, enabling research and therapeutic applications. Clinically, rIFN-γ has been explored as an immunotherapy for chronic infections (e.g., tuberculosis), certain cancers, and immunodeficiencies. It is also used as an adjuvant to enhance vaccine efficacy or to counteract immunosuppression.
In research, rIFN-γ is pivotal for studying immune cell interactions, inflammatory pathways, and autoimmune diseases like rheumatoid arthritis or Crohn’s disease. However, challenges in production include ensuring proper protein folding, stability, and batch-to-batch consistency. Quality control involves bioassays (e.g., antiviral activity tests) and analytical methods (SDS-PAGE, HPLC) to verify purity and potency. Despite its therapeutic promise, clinical use is limited by side effects like fever and fatigue, underscoring the need for targeted delivery systems. Overall, rIFN-γ remains a vital tool in immunology and translational medicine. (Word count: 398)
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