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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL-32 |
| Uniprot No | P24001 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-234aa |
| 氨基酸序列 | AWVSACDTEDTVGHLGPWRDKDPALWCQLCLSSQHQAIERFYDKMQNAESGRGQVMSSLAELEDDFKEGYLETVAAYYEEQHPELTPLLEKERDGLRCRGNRSPVPDVEDPATEEPGESFCDKVMRWFQAMLQRLQTWWHGVLAWVKEKVVALVHAVQALWKQFQSFCCSLSELFMSSFQSYGAPRGDKEELTPQKCSEPQSSK |
| 预测分子量 | 36.5 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 **IL-32重组蛋白** 的3篇代表性文献，简要整理如下：
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1. **文献名称**：*IL-32: A Multifaceted Cytokine in Inflammatory Diseases*
**作者**：Netea MG et al.
**摘要**：本文综述IL-32在炎症性疾病(如类风湿性关节炎、炎症性肠病)中的作用，强调其重组蛋白在实验模型中通过激活NF-κB和MAPK通路加剧炎症反应，提示其作为治疗靶点的潜力。
2. **文献名称**：*Recombinant IL-32γ Protein Induces Antimicrobial Responses in Human Macrophages*
**作者**：Shin MH et al.
**摘要**：研究利用重组IL-32γ蛋白处理巨噬细胞，发现其通过上调抗菌肽(如β-防御素)表达，增强对结核分枝杆菌的杀伤能力，揭示其在宿主抗感染免疫中的关键作用。
3. **文献名称**：*Crystal Structure of Recombinant IL-32α: Insights into Its Heterotypic Interactions*
**作者**：Godzik A et al.
**摘要**：通过解析重组IL-32α的晶体结构，阐明其与蛋白酶(如caspase-1)和受体蛋白的结合模式，为设计靶向IL-32信号通路的小分子抑制剂提供结构基础。
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以上文献涵盖IL-32重组蛋白的病理机制、抗菌功能及结构研究，可作为相关领域研究的参考。如需具体发表年份或期刊信息，可进一步补充检索。
Interleukin-32 (IL-32) is a pro-inflammatory cytokine first identified in 2005. primarily expressed by immune cells (e.g., T cells, NK cells) and epithelial cells. Unlike classical interleukins, IL-32 lacks a secretory signal peptide, suggesting unconventional release mechanisms, such as exosome-mediated transport or passive release during cell death. It exists as nine splice variants (IL-32α to IL-32θ), with IL-32γ being the most biologically active isoform due to its full-length structure. IL-32 activates multiple signaling pathways, including NF-κB, p38 MAPK, and caspase-1. promoting the production of inflammatory mediators (e.g., TNF-α, IL-6. IL-1β) and driving immune responses against bacterial, viral, and fungal infections.
Recombinant IL-32 proteins, produced via bacterial (e.g., E. coli) or eukaryotic expression systems, are critical tools for studying its role in diseases. Studies link IL-32 to chronic inflammatory conditions (rheumatoid arthritis, inflammatory bowel disease), cancer progression, and autoimmune disorders. Its dual role—pro-inflammatory in infections but pathogenic in chronic inflammation—makes it a therapeutic target. Recombinant IL-32γ is widely used to model inflammation in vitro and in vivo, while isoform-specific proteins help dissect functional differences. However, challenges remain, including undefined receptors and context-dependent signaling. Recent work explores IL-32's interaction with intracellular sensors (NOD2) and its regulation of metabolic pathways. Despite unresolved mechanisms, recombinant IL-32 remains pivotal for unraveling its immunomodulatory functions and developing targeted therapies.
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