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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EREG |
| Uniprot No | O14944 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 60-108aa |
| 氨基酸序列 | MVAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL |
| 预测分子量 | 19 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EREG(Epiregulin)重组蛋白的文献摘要示例(注：文献为虚拟示例，实际引用需核实)：
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1. **《Recombinant Human Epiregulin Promotes Wound Healing via EGFR Signaling》**
- **作者**: Tanaka et al., *Journal of Biological Chemistry*
- **摘要**: 本研究通过哺乳动物细胞系统表达并纯化重组人源EREG蛋白，发现其通过激活表皮生长因子受体(EGFR)信号通路，显著促进体外上皮细胞迁移和体内小鼠皮肤伤口修复，为EREG在再生医学中的应用提供依据。
2. **《Epiregulin Enhances Colorectal Cancer Metastasis through EMT Induction》**
- **作者**: Chen et al., *Oncogene*
- **摘要**: 利用重组EREG蛋白处理结肠癌细胞，证实其通过上调Snail和Twist等转录因子诱导上皮-间质转化(EMT)，增强癌细胞侵袭能力，提示EREG可作为结直肠癌治疗的潜在靶点。
3. **《Structural and Functional Characterization of Epiregulin-HER1 Interaction》**
- **作者**: Müller et al., *Nature Structural & Molecular Biology*
- **摘要**: 通过X射线晶体学解析重组EREG蛋白与EGFR(HER1)的复合物结构，揭示其结合模式与亲和力差异，阐明EREG相较于EGF家族其他成员(如EGF、TGF-α)的独特受体激活机制。
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如需真实文献，建议在PubMed或Google Scholar中检索关键词：*"Recombinant Epiregulin"、"Epiregulin function"* 或 *"EREG EGFR signaling"*。
**Background of EREG Recombinant Protein**
Epiregulin (EREG), a member of the epidermal growth factor (EGF) family, is a secreted protein that plays critical roles in cell proliferation, differentiation, and tissue repair by binding to epidermal growth factor receptor (EGFR) and other ErbB receptor tyrosine kinases. Initially identified for its mitogenic activity, EREG is involved in diverse physiological and pathological processes, including wound healing, inflammation, and cancer progression. Unlike other EGF family members, EREG exhibits dual functionality, acting as both a growth promoter and a modulator of cellular responses depending on context and receptor interaction.
Recombinant EREG protein is engineered through genetic manipulation, typically using bacterial, yeast, or mammalian expression systems. Mammalian systems (e.g., CHO or HEK293 cells) are preferred for producing functional EREG due to their ability to perform post-translational modifications, such as glycosylation, essential for receptor binding and bioactivity. The recombinant protein is purified via affinity chromatography, often tagged with sequences like His-tag for isolation, followed by rigorous quality checks (e.g., SDS-PAGE, Western blot, and bioassays) to ensure purity and biological activity.
In research, recombinant EREG is widely used to study EGFR/ErbB signaling pathways, cancer biology (e.g., tumor growth, metastasis, and drug resistance), and regenerative mechanisms. It also holds therapeutic potential, particularly in tissue regeneration and as a target in oncology, though its dual role in cancer—promoting or suppressing tumors—requires careful exploration. Challenges remain in optimizing production yields, stability, and delivery systems for clinical applications. Overall, EREG recombinant protein serves as a vital tool for dissecting cellular mechanisms and developing targeted therapies.
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