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 | ES |
| Uniprot No | Q8TE68 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-723aa |
| 氨基酸序列 | MSTATGPEAA PKPSAKSIYE QRKRYSTVVM ADVSQYPVNH LVTFCLGEDD GVHTVEDASR KLAVMDSQGR VWAQEMLLRV SPDHVTLLDP ASKEELESYP LGAIVRCDAV MPPGRSRSLL LLVCQEPERA QPDVHFFQGL RLGAELIRED IQGALHNYRS GRGERRAAAL RATQEELQRD RSPAAETPPL QRRPSVRAVI STVERGAGRG RPQAKPIPEA EEAQRPEPVG TSSNADSASP DLGPRGPDLA VLQAEREVDI LNHVFDDVES FVSRLQKSAE AARVLEHRER GRRSRRRAAG EGLLTLRAKP PSEAEYTDVL QKIKYAFSLL ARLRGNIADP SSPELLHFLF GPLQMIVNTS GGPEFASSVR RPHLTSDAVA LLRDNVTPRE NELWTSLGDS WTRPGLELSP EEGPPYRPEF FSGWEPPVTD PQSRAWEDPV EKQLQHERRR RQQSAPQVAV NGHRDLEPES EPQLESETAG KWVLCNYDFQ ARNSSELSVK QRDVLEVLDD SRKWWKVRDP AGQEGYVPYN ILTPYPGPRL HHSQSPARSL NSTPPPPPAP APAPPPALAR PRWDRPRWDS CDSLNGLDPS EKEKFSQMLI VNEELQARLA QGRSGPSRAV PGPRAPEPQL SPGSDASEVR AWLQAKGFSS GTVDALGVLT GAQLFSLQKE ELRAVSPEEG ARVYSQVTVQ RSLLEDKEKV SELEAVMEKQ KKKVEGEVEM EVI |
| 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篇关于重组蛋白表达系统的代表性文献概览(注：内容基于领域知识整合，非真实文献)：
---
1. **文献名称**：*Recombinant protein expression in Escherichia coli: advances and challenges*
**作者**：Rosano GL, Ceccarelli EA
**摘要**：系统综述了大肠杆菌表达体系中重组蛋白生产的优化策略，包括启动子选择、融合标签设计、密码子优化及胞内折叠调控技术，并探讨了包涵体复性难题的解决方案。
2. **文献名称**：*Optimizing protein expression in mammalian cells: Current strategies and future perspectives*
**作者**：Butler M, Meneses-Acosta A
**摘要**：聚焦哺乳动物细胞(如CHO细胞)表达系统，分析载体设计、培养基优化及基因编辑技术(如CRISPR)对重组蛋白产量、糖基化修饰及药物稳定性的提升作用。
3. **文献名称**：*Yeast systems for recombinant protein production: From toolkit to glycoengineering*
**作者**：Ahmad M et al.
**摘要**：探讨毕赤酵母和酿酒酵母系统在重组蛋白生产中的应用，重点介绍糖基化工程改造技术以实现人源化蛋白翻译后修饰，推动治疗性蛋白开发。
---
**附注**：如需引用真实文献，建议通过PubMed或Web of Science检索关键词“recombinant protein expression optimization”“E. coli/Pichia/mammalian expression systems”获取最新研究。
**Background of Recombinant Proteins in Embryryonic Stem Cell Research**
Recombinant proteins, engineered through genetic recombination technology, are pivotal tools in modern biotechnology and regenerative medicine. These proteins are produced by inserting target gene sequences into host organisms (e.g., bacteria, yeast, or mammalian cells) to express specific proteins with high purity and consistency. Their development revolutionized biomedical research by enabling large-scale production of proteins that are otherwise difficult to isolate from natural sources, such as growth factors, cytokines, and signaling molecules.
In embryonic stem (ES) cell research, recombinant proteins play a critical role in maintaining pluripotency and directing differentiation. Early ES cell culture systems relied on serum-containing media or feeder layers, which introduced variability due to undefined components. Recombinant proteins like basic fibroblast growth factor (FGF2) and leukemia inhibitory factor (LIF) replaced these undefined elements, enabling serum-free, feeder-free culture conditions. This advancement improved reproducibility and compliance with regulatory standards for clinical applications.
Moreover, recombinant proteins are essential for manipulating signaling pathways (e.g., Wnt, BMP, or Activin/Nodal) to guide ES cell differentiation into specific lineages, such as neurons, cardiomyocytes, or pancreatic cells. They also facilitate the development of organoids and disease models, aiding drug screening and mechanistic studies. For example, recombinant Activin A and BMP4 are widely used to simulate embryonic patterning in vitro.
Recent innovations include engineered variants with enhanced stability or modified functions, such as thermostable growth factors or fusion proteins targeting specific receptors. However, challenges remain, including high production costs, potential immunogenicity, and the need for precise post-translational modifications in certain applications.
Overall, recombinant proteins continue to drive progress in ES cell research, bridging basic science and therapeutic development. Their scalability and versatility make them indispensable for advancing personalized medicine, tissue engineering, and understanding early human development. Future directions may integrate synthetic biology and AI-driven design to optimize protein functionality and reduce manufacturing barriers.
×
