首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Reg3γ |
| Uniprot No | Q96PJ0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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3-4条关于重组蛋白的经典文献及其摘要概括：
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1. **文献名称**：*Production of human insulin in E. coli*
**作者**：Goeddel, D.V., et al.
**摘要**：该研究首次利用重组DNA技术在大肠杆菌中成功表达人胰岛素，开创了重组蛋白工业化生产的先河，为糖尿病治疗提供了新途径。
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2. **文献名称**：*Biopharmaceutical benchmarks: Approved recombinant proteins*
**作者**：Walsh, G.
**摘要**：综述了重组蛋白药物的开发历程、生产技术和临床应用，涵盖干扰素、抗体、疫苗等，强调其在现代生物医药中的核心地位。
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3. **文献名称**：*Recombinant protein secretion in Escherichia coli*
**作者**：Sorensen, H.P., et al.
**摘要**：系统探讨了大肠杆菌中重组蛋白分泌表达的策略，包括信号肽优化和宿主工程，旨在提高可溶性和简化下游纯化流程。
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4. **文献名称**：*Protein therapeutics: A summary and pharmacological classification*
**作者**：Leader, B., et al.
**摘要**：分类总结了重组蛋白药物的药理机制(如酶替代疗法、靶向治疗等)，并讨论了其在癌症、免疫疾病等领域的前景。
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这些文献涵盖了重组蛋白的基础技术、生产优化和医学应用，适合快速了解该领域的关键进展。如需具体论文年份或期刊，可进一步补充说明!
**Background of Recombinant Proteins**
Recombinant proteins are genetically engineered molecules produced by introducing specific DNA sequences into host organisms, enabling them to synthesize proteins that are otherwise inaccessible or scarce in nature. This technology emerged in the 1970s with advancements in recombinant DNA techniques, revolutionizing biotechnology and medicine. The process involves isolating a target gene, inserting it into a vector (e.g., plasmid), and transferring it into a host system—such as bacteria, yeast, insect, or mammalian cells—where the gene is expressed to produce the desired protein.
The choice of host depends on the protein’s complexity. For instance, *E. coli* is cost-effective for simple proteins, while mammalian cells are preferred for post-translationally modified proteins (e.g., antibodies). Recombinant proteins have transformed therapeutics, with examples like insulin for diabetes, monoclonal antibodies for cancer, and vaccines (e.g., hepatitis B). Beyond medicine, they are used in industrial enzymes, research tools, and diagnostics.
Key advantages include scalability, purity, and reduced reliance on animal-derived proteins, minimizing contamination risks. Innovations in expression systems, purification methods (e.g., affinity tags), and protein engineering (e.g., site-directed mutagenesis) continue to enhance yield and functionality. Challenges remain, such as optimizing folding in prokaryotic systems or managing glycosylation variations.
Overall, recombinant protein technology underpins modern biologics, driving progress in drug development, synthetic biology, and personalized medicine, with ongoing research expanding its applications in addressing global health and industrial challenges.
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