| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MAF |
| Uniprot No | O75444-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 304-403aa |
| 氨基酸序列 | SCRFKRVQQRHVLESEKNQLLQQVDHLKQEISRLVRERDAYKEKYEKLVS SGFRENGSSSDNPSSPEFFITEPTRKLEPSVGYATFWKPQHRVLTSVFTK |
| 预测分子量 | 37 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. |
以下为关于MAF重组蛋白的参考文献示例(内容为模拟，仅供参考)：
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1. **文献名称**：*Recombinant MAF Protein Enhances Macrophage Activation in Tumor Microenvironments*
**作者**：Smith J, et al.
**摘要**：本研究通过大肠杆菌系统成功表达并纯化了重组MAF蛋白，证实其可显著增强巨噬细胞的吞噬活性和炎性因子分泌，在体外实验中抑制肿瘤细胞增殖，为免疫治疗提供潜在策略。
2. **文献名称**：*Structural Analysis of c-MAF Recombinant Protein and Its Role in T Cell Differentiation*
**作者**：Li X, Wang Y.
**摘要**：利用X射线晶体学解析了c-MAF重组蛋白的三维结构，揭示其与DNA结合的关键结构域，并通过基因敲除实验证明c-MAF调控Th17细胞分化，为自身免疫疾病治疗提供理论依据。
3. **文献名称**：*Therapeutic Efficacy of Recombinant MAF in Colitis-Associated Cancer Models*
**作者**：Garcia R, et al.
**摘要**：在小鼠结肠炎相关癌模型中，腹腔注射重组MAF蛋白可减少肠道炎症并抑制肿瘤生长，机制涉及巨噬细胞极化及NF-κB通路调控，提示其作为新型生物制剂的潜力。
4. **文献名称**：*Production of Bioactive MAF Recombinant Protein Using Plant Expression Systems*
**作者**：Chen L, et al.
**摘要**：首次通过植物瞬时表达系统高效生产重组MAF蛋白，验证其与哺乳动物来源的蛋白具有等效的免疫刺激活性，为低成本大规模生产奠定基础。
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注：以上内容为学术示例，实际引用时请查询真实文献并核对信息准确性。如需真实文献，建议在PubMed或Web of Science中检索关键词“recombinant MAF protein”或“c-MAF recombinant”。
**Background of MAF Recombinant Protein**
The MAF (musculoaponeurotic fibrosarcoma) family of transcription factors plays a critical role in regulating gene expression during cellular differentiation, proliferation, and development. These proteins belong to the basic leucine zipper (bZIP) superfamily, characterized by a conserved DNA-binding domain and a leucine zipper motif for dimerization. The MAF subgroup includes both large (e.g., c-MAF, MAFA, MAFB) and small (e.g., MAFF, MAFG, MAFK) members, each modulating distinct biological pathways. Among these, c-MAF is notably implicated in oncogenesis, particularly in multiple myeloma and other cancers, where its overexpression drives tumor survival and drug resistance.
Recombinant MAF proteins are engineered in vitro using expression systems like *E. coli* or mammalian cells to produce purified, functional proteins for research and therapeutic applications. These proteins retain the ability to bind specific DNA sequences (e.g., MARE motifs) and regulate target genes, making them valuable tools for studying MAF-mediated transcriptional mechanisms. Researchers utilize MAF recombinant proteins to investigate their roles in immune regulation, cellular stress responses, and developmental processes, as well as to screen potential inhibitors for cancer therapy.
In disease contexts, MAF proteins are linked to pathologies beyond cancer, including diabetes (MAFA in pancreatic β-cells) and autoimmune disorders. The development of recombinant MAF variants with mutations or tags (e.g., His-tag, GFP) has further enabled structural studies, protein interaction assays, and high-throughput drug discovery. By elucidating MAF’s molecular interactions and downstream effects, recombinant MAF proteins contribute to advancing both basic science and translational medicine, offering insights into targeted therapies for MAF-driven diseases.
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