纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | FCN1 |
Uniprot No | O00602 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-326aa |
氨基酸序列 | MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL RGCPGLPGAP GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG EKGDAGQSQS CATGPRNCKD LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG SQLGEFWLGN DNIHALTAQG SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV GGSAGNSLTG HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY ANGINWSAAK GYKYSYKVSE MKVRPA |
预测分子量 | 34 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FCN1重组蛋白的3篇参考文献概览:
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1. **标题**:*Recombinant Ficolin-1 Triggers Inflammation via Lectin Complement Pathway Activation*
**作者**:Smith A, et al.
**摘要**:研究通过大肠杆菌表达系统成功制备重组FCN1蛋白,并证实其可激活补体凝集素途径,促进炎症因子释放。实验表明重组FCN1能结合病原体表面多糖,提示其在先天免疫中的病原识别作用。
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2. **标题**:*Structural Insights into FCN1 Oligomerization and Pathogen Binding*
**作者**:Li Y, et al.
**摘要**:通过冷冻电镜解析重组人源FCN1蛋白的寡聚结构,揭示其胶原样区域和纤维蛋白原结构域的空间构象。研究证明重组FCN1通过多聚化增强对细菌脂多糖的亲和力,为设计免疫调节药物提供结构基础。
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3. **标题**:*Glycosylation Modulates the Immunological Functions of Recombinant Ficolin-1*
**作者**:Wang H, et al.
**摘要**:利用哺乳动物细胞系统表达糖基化重组FCN1.发现糖链修饰显著影响其与凋亡细胞的结合能力及补体激活效率,强调生产系统对重组蛋白功能研究的重要性。
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(注:上述文献为示例性概括,实际文献需通过数据库检索获取具体信息。)建议使用PubMed或Web of Science以“recombinant FCN1”或“Ficolin-1 expression”为关键词查找最新研究。
**Background of FCN1 Recombinant Protein**
Ficolin-1 (FCN1), a member of the fibrinogen-collagen lectin family, is a pattern recognition molecule critical in innate immunity. It is primarily produced by monocytes, granulocytes, and epithelial cells, functioning as a soluble effector protein. FCN1 binds to pathogen-associated molecular patterns (PAMPs) on microbial surfaces, such as acetylated carbohydrates or lipoteichoic acids, through its fibrinogen-like domain. This interaction triggers the activation of the lectin complement pathway via association with MASPs (MBL-associated serine proteases), leading to pathogen opsonization, phagocytosis, or lysis.
Recombinant FCN1 protein is engineered through genetic cloning and expression systems (e.g., mammalian or bacterial cells) to mimic native FCN1’s structural and functional properties. It retains the ability to recognize specific ligands and activate complement, making it a valuable tool for studying immune responses, host-pathogen interactions, and complement regulation. Researchers utilize recombinant FCN1 to investigate its role in diseases like infections, autoimmune disorders, and chronic inflammation. Additionally, it aids in developing diagnostic assays or therapeutic strategies targeting lectin pathway dysregulation.
The production of recombinant FCN1 overcomes challenges in isolating the protein from natural sources, ensuring high purity and scalability. Its applications extend to structural studies, antibody development, and screening for inhibitors or enhancers of lectin pathway activity. By elucidating FCN1’s mechanisms, this recombinant protein contributes to advancing immunology research and therapeutic innovation.
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