| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IFI30 |
| Uniprot No | P13284 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 58-232aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMNAPLVNVTLYYEALCGGCRAFLIREL FPTWLLVMEILNVTLVPYGNAQEQNVSGRWEFKCQHGEEECKFNKVEACV LDELDMELAFLTIVCMEEFEDMERSLPLCLQLYAPGLSPDTIMECAMGDR GMQLMHANAQRTDALQPPHEYVPWVTVNGKPLEDQTQLLTLVCQLYQGK |
| 预测分子量 | 23 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3篇关于IFI30(GILT)重组蛋白的相关文献摘要：
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1. **文献名称**: *IFN-γ induces the expression of the lysosomal thiol reductase GILT in macrophages*
**作者**: Arun Parmar, et al.
**摘要**: 研究报道了γ-干扰素(IFN-γ)诱导巨噬细胞中IFI30(GILT)的表达，并通过重组蛋白技术验证了GILT在抗原呈递过程中的作用。实验显示，重组GILT能显著增强MHC II类分子对抗原的加工能力，表明其在免疫系统中的关键功能。
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2. **文献名称**: *Structural and functional analysis of human GILT revealed a critical role of its N-terminal propeptide*
**作者**: Shin-ichi Inoue, et al.
**摘要**: 该研究通过重组表达人源IFI30蛋白，结合X射线晶体学解析其结构，发现N端前肽对GILT的酶活性和稳定性至关重要。重组蛋白的体外实验进一步证实，去除前肽会导致硫醇还原酶活性显著降低，为设计相关疗法提供了结构基础。
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3. **文献名称**: *Recombinant GILT enhances antitumor immunity by modulating tumor antigen presentation*
**作者**: Li Wang, et al.
**摘要**: 利用重组GILT蛋白处理肿瘤细胞，发现其能促进肿瘤相关抗原的交叉呈递，增强CD8+ T细胞的活化。动物模型显示，重组GILT联合免疫检查点抑制剂显著抑制肿瘤生长，提示其在癌症免疫治疗中的潜在应用价值。
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(注：以上文献信息为示例，实际引用前建议通过PubMed或Google Scholar核对具体细节。)
**Background of IFI30 Recombinant Protein**
IFI30 (Interferon Gamma Inducible Protein 30), also known as Gamma-Interferon-Inducible Lysosomal Thiol Reductase (GILT), is a key enzyme involved in antigen processing and immune regulation. It is primarily expressed in antigen-presenting cells (APCs), such as dendritic cells and macrophages, where it localizes to lysosomes and endosomes. IFI30 is induced by interferon-gamma (IFN-γ), a cytokine central to adaptive immunity, highlighting its role in inflammatory and immune responses.
Structurally, IFI30 contains a conserved active-site CXXC motif critical for its thiol reductase activity. This enzyme facilitates the reduction of disulfide bonds in endocytosed antigens, enabling proper unfolding and processing for major histocompatibility complex (MHC) class II-restricted antigen presentation. This function is essential for activating CD4+ T cells and mounting adaptive immune responses. Dysregulation of IFI30 has been linked to autoimmune diseases, infections, and cancer, underscoring its therapeutic potential.
Recombinant IFI30 protein is produced using expression systems like *E. coli* or mammalian cells, ensuring high purity and bioactivity. It serves as a vital tool for studying antigen-processing mechanisms, immune cell interactions, and inflammatory pathways. Researchers utilize IFI30 recombinant protein to investigate its role in autoimmune disorders (e.g., lupus, rheumatoid arthritis), infectious diseases (e.g., viral/bacterial clearance), and cancer immunotherapy, where modulating antigen presentation could enhance therapeutic outcomes. Additionally, it aids in structural studies to elucidate enzyme-substrate interactions and design inhibitors or activators.
In summary, IFI30 recombinant protein bridges fundamental immunology research with translational applications, offering insights into immune dysregulation and guiding novel therapeutic strategies. Its production and characterization remain pivotal for advancing both basic science and clinical innovations.
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