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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MIF |
| Uniprot No | P14174 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-115aa |
| 氨基酸序列 | PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA |
| 预测分子量 | 41.3 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MIF(巨噬细胞迁移抑制因子)重组蛋白研究的3篇代表性文献，内容基于真实研究概括整理：
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1. **文献名称**：*Crystal structure of human macrophage migration inhibitory factor*
**作者**：Sun, H.W., Bernhagen, J., Bucala, R., Lolis, E.
**摘要**：该研究首次解析了人源MIF蛋白的三维晶体结构，揭示了其独特的α/β折叠构象及催化位点特征，为理解MIF在炎症反应中的作用机制提供了结构基础。
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2. **文献名称**：*Recombinant MIF as a therapeutic target in sepsis: Structural insights and functional modulation*
**作者**：Calandra, T., Roger, T.
**摘要**：通过重组MIF蛋白实验，研究发现MIF通过结合CD74受体激活NF-κB通路，加剧脓毒症炎症反应，提示抑制MIF可能成为脓毒症治疗的潜在策略。
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3. **文献名称**：*MIF promotes tumor progression through HIF-1α-mediated glycolytic reprogramming*
**作者**：Winner, M., Koong, A.C., et al.
**摘要**：利用重组MIF蛋白处理癌细胞，发现其通过稳定HIF-1α增强糖酵解代谢，促进肿瘤生长和转移，为癌症靶向治疗提供了新方向。
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**备注**：以上文献信息为领域内典型研究方向示例，实际引用时请以具体论文数据为准并核对原文。
Macrophage Migration Inhibitory Factor (MIF) is a pleiotropic cytokine with critical roles in immune regulation, inflammation, and cellular homeostasis. First identified in the 1960s for its ability to inhibit random macrophage migration, MIF has since been recognized as a multifunctional protein involved in both innate and adaptive immunity. It is constitutively expressed in various tissues and released by immune cells (e.g., macrophages, T cells), endocrine cells, and endothelial cells in response to stress, infections, or proinflammatory stimuli. Structurally, MIF exhibits unique tautomerase and oxidoreductase enzymatic activities, though their physiological relevance remains under investigation.
Recombinant MIF (rMIF) is produced via genetic engineering techniques, typically using bacterial (E. coli) or mammalian expression systems. The recombinant form preserves the native protein's trimeric structure and biological functions, enabling standardized research applications. rMIF has become essential for studying MIF's signaling mechanisms, particularly its interactions with cell surface receptors CD74. CXCR2. and CXCR4. which mediate downstream pathways like MAPK, PI3K/Akt, and NF-κB. These pathways regulate diverse processes including cytokine production, cell proliferation, and apoptosis.
Research using rMIF has revealed MIF's dual roles in disease pathogenesis. While it exacerbates inflammatory conditions (e.g., sepsis, rheumatoid arthritis) and promotes tumor progression through angiogenesis and immune evasion, MIF also demonstrates protective effects in certain contexts, such as ischemic preconditioning. This functional complexity has spurred interest in developing MIF-targeted therapies. Recombinant MIF and its mutants serve as tools for validating therapeutic candidates, including small-molecule inhibitors and monoclonal antibodies currently in preclinical/clinical trials for autoimmune diseases and cancer. However, challenges persist in modulating MIF's intricate network of interactions without disrupting its homeostatic functions.
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