| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FURIN |
| Uniprot No | P09958 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-794aa |
| 氨基酸序列 | KVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL |
| 分子量 | 110.22 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人FURIN蛋白的示例参考文献(需注意：以下信息为示例模拟，具体文献请以实际数据库检索结果为准)：
---
1. **文献名称**: *"Production and characterization of recombinant human FURIN protease in HEK293 cells"*
**作者**: Braun A., Sällberg M.
**摘要**: 描述了在HEK293哺乳动物细胞中高效表达重组人FURIN蛋白的方法，通过亲和层析纯化获得高纯度蛋白，并验证其在体外切割前体蛋白(如VEGF-C)的活性。
2. **文献名称**: *"Furin-mediated cleavage of SARS-CoV-2 spike protein and its role in viral infectivity"*
**作者**: Staubach D., Yoshida Y.
**摘要**: 研究重组人FURIN蛋白对新冠病毒S蛋白的切割机制，证明FURIN酶活性是病毒激活的关键步骤，为开发靶向抑制剂提供理论基础。
3. **文献名称**: *"Structural insights into the substrate specificity of human FURIN protease"*
**作者**: Zhang L., Hansen S.
**摘要**: 通过X射线晶体学解析重组人FURIN蛋白的3D结构，揭示其底物识别和催化的分子机制，并探索其与疾病相关突变的功能关联。
4. **文献名称**: *"Recombinant FURIN as a tool for studying proprotein convertase dysregulation in cancer"*
**作者**: Li J., Seidah N.G.
**摘要**: 利用重组FURIN分析其在肿瘤微环境中的异常表达，发现其通过激活金属蛋白酶促进癌细胞迁移和侵袭的病理机制。
---
建议通过PubMed、Web of Science或Google Scholar检索真实文献时，使用关键词如 **"recombinant human FURIN"** 或 **"Furin protease in vitro characterization"**。部分研究可能涉及药物开发或病毒学交叉领域。
Recombinant human FURIN protein is a engineered version of the endogenous proprotein convertase subtilisin/kexin type 3 (PCSK3), a calcium-dependent serine endoprotease crucial for proteolytic processing of proproteins. Expressed predominantly in the Golgi apparatus, FURIN cleaves precursor proteins at polybasic motifs (e.g., RX(K/R)R↓), activating diverse substrates including growth factors, hormones, viral glycoproteins (e.g., SARS-CoV-2 Spike protein), and extracellular matrix proteins. Its role in cellular homeostasis, viral pathogenesis, and disease progression (e.g., cancer, neurodegenerative disorders) has driven interest in producing recombinant FURIN for research and therapeutic development.
Produced via heterologous expression systems (e.g., mammalian cells, bacteria), recombinant FURIN retains catalytic activity while enabling scalable purification and functional studies. Structural studies using recombinant protein have elucidated substrate specificity and regulatory mechanisms, such as pH-dependent autocatalytic activation. Inhibitors targeting FURIN are being explored for antiviral and anticancer therapies. Current applications span in vitro proteolytic assays, protein processing studies, and screening for therapeutic modulators. However, challenges remain in maintaining stability and avoiding premature self-activation during production. Advances in protein engineering and glycoform optimization continue to enhance its utility in biomedical research.
×
