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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPGN |
| Uniprot No | Q6UW88 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-95aa |
| 氨基酸序列 | AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA |
| 预测分子量 | 7.9 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EPGN(表皮调节素)重组蛋白的3篇参考文献的简要信息(注：以下内容基于模拟生成，实际文献需通过学术数据库查询确认)：
1. **文献名称**: "Recombinant Epigen (EPGN) promotes epidermal regeneration through EGFR signaling"
**作者**: Smith J, et al.
**摘要**: 本研究成功在大肠杆菌中表达了具有生物活性的重组EPGN蛋白，并证明其通过激活EGFR信号通路促进表皮细胞增殖和迁移，提示其在皮肤修复中的潜在应用价值。
2. **文献名称**: "Expression and purification of bioactive EPGN in mammalian cells for cancer research"
**作者**: Lee H, et al.
**摘要**: 作者利用哺乳动物表达系统制备了高纯度重组EPGN蛋白，发现其能显著增强乳腺癌细胞的侵袭能力，提示EPGN可能作为肿瘤治疗的潜在靶点。
3. **文献名称**: "Structural characterization of recombinant EPGN and its role in inflammatory response"
**作者**: Gonzalez R, et al.
**摘要**: 通过X射线晶体学解析了重组EPGN的三维结构，并证明该蛋白通过调控NF-κB通路加剧炎症反应，为开发相关抑制剂提供了结构基础。
(提示：以上文献信息为示例性质，实际研究中建议通过PubMed/Web of Science等平台以"EPGN recombinant protein"或"recombinant Epigen"为关键词检索最新文献。)
**Background of EPGN Recombinant Protein**
EPGN (Epigen), a member of the epidermal growth factor (EGF) family, is a secreted protein that plays a role in cell proliferation, differentiation, and tissue repair. Initially identified in the early 2000s, it shares structural homology with EGF and binds to the epidermal growth factor receptor (EGFR), though with distinct functional properties. Unlike EGF, EPGN exhibits a unique receptor activation profile, potentially influencing specific downstream signaling pathways, such as MAPK/ERK and PI3K/AKT, which are critical for cellular growth and survival.
Structurally, recombinant EPGN is produced via genetic engineering, typically using mammalian or bacterial expression systems to ensure proper folding and post-translational modifications. The recombinant protein retains the functional domains necessary for receptor binding and activation, making it a valuable tool for studying EGFR-mediated processes. Its smaller molecular weight (~19 kDa) and single EGF-like domain differentiate it from other EGF family members like transforming growth factor-alpha (TGF-α).
EPGN has garnered attention in biomedical research for its potential therapeutic applications. Studies suggest it may promote wound healing, epithelial regeneration, and mucosal repair, particularly in contexts where traditional EGF signaling is impaired. Additionally, its role in cancer biology is being explored, as aberrant EGFR signaling is linked to tumor progression. However, EPGN's precise mechanisms and therapeutic efficacy remain under investigation, with some evidence pointing to context-dependent effects that vary across tissue types or disease states.
Research on EPGN recombinant protein also addresses challenges such as stability, bioavailability, and targeted delivery. Advances in protein engineering, including PEGylation or fusion proteins, aim to enhance its pharmacokinetic properties. While preclinical data are promising, further clinical validation is needed to define its safety and efficacy in humans. Overall, EPGN represents a versatile molecule bridging basic science and translational medicine, with implications for oncology, regenerative therapies, and beyond.
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