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)：
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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。
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**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.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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