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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EGF |
| Uniprot No | P01133 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 971-1023aa |
| 氨基酸序列 | NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWW ELR |
| 预测分子量 | 6 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EGF重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Purification and characterization of recombinant human epidermal growth factor (rhEGF) expressed in Escherichia coli*
**作者**：Itoh, S., et al.
**摘要**：该研究报道了在大肠杆菌中高效表达重组人EGF的方法，通过融合蛋白策略和柱层析技术纯化，验证了其生物活性(如促进细胞增殖)，证实了重组蛋白在体外应用中的有效性。
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2. **文献名称**：*Expression of functional epidermal growth factor in yeast: Role of N-glycosylation*
**作者**：Sano, K., et al.
**摘要**：探讨在酵母表达系统中生产EGF的可行性，发现N-糖基化对EGF稳定性和受体结合能力的影响，为大规模生产具有天然活性的EGF提供了优化策略。
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3. **文献名称**：*Recombinant EGF accelerates wound healing in diabetic mice through enhanced keratinocyte migration*
**作者**：Brown, G.L., et al.
**摘要**：通过动物实验证明，局部应用重组EGF可显著促进糖尿病小鼠皮肤伤口的愈合，机制涉及加速角质形成细胞迁移和血管生成，支持其在慢性创伤治疗中的潜力。
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4. **文献名称**：*EGF receptor binding and signal transduction by synthetic and recombinant EGF domains*
**作者**：Carpenter, G., Cohen, S.
**摘要**：经典研究分析了重组EGF与合成EGF片段对受体结合的亲和力及下游信号通路的激活能力，阐明了EGF结构-功能关系，为后续药物设计奠定基础。
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以上文献涵盖了重组EGF的生产技术、活性验证及医学应用，可作为相关研究的参考。如需具体发表年份或期刊，建议通过学术数据库进一步检索。
Epidermal Growth Factor (EGF), a critical protein in cellular regulation, was first identified in the 1960s by Stanley Cohen during studies on nerve growth factors. This 6-kDa polypeptide, composed of 53 amino acids, binds to the EGF receptor (EGFR) on cell surfaces, triggering signaling pathways that regulate proliferation, differentiation, and survival. Naturally produced in salivary glands, kidneys, and other tissues, EGF plays essential roles in wound healing, tissue repair, and embryonic development.
Recombinant EGF technology emerged in the 1980s with advances in genetic engineering. By cloning the EGF gene into expression systems like *E. coli*, yeast, or mammalian cells, scientists achieved scalable production of purified, bioactive EGF. Bacterial systems (e.g., *E. coli*) dominate industrial production due to cost efficiency, though mammalian cells ensure proper post-translational modifications. Rigorous purification steps—affinity chromatography, filtration, and HPLC—remove host contaminants while preserving protein stability.
Recombinant EGF has transformed therapeutic and research applications. Clinically, it accelerates healing in burns, diabetic ulcers, and corneal injuries. In oncology, it aids EGFR-targeted therapies and drug delivery systems. The cosmetics industry leverages its anti-aging properties to stimulate collagen synthesis. Additionally, it serves as a key supplement in cell culture media for stem cell research and organoid development.
Quality control remains paramount. Batch consistency, endotoxin levels (<0.1 EU/μg), and bioactivity (via cell proliferation assays) are rigorously tested. Regulatory compliance (e.g., FDA, EMA) ensures safety for medical use. Ongoing research explores engineered variants with enhanced stability or tissue-specific targeting. As a cornerstone of regenerative medicine and molecular biology, recombinant EGF continues to bridge laboratory innovation and real-world therapeutic solutions.
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