纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | FUT3 |
Uniprot No | P21217 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 35-361aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT |
预测分子量 | 41 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FUT3重组蛋白的参考文献及其摘要概括:
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1. **标题**:Molecular cloning and expression of a functional bovine α1.3-fucosyltransferase gene: Homology to the mammalian FUT3 gene
**作者**:Costache, M., et al.
**摘要**:该研究克隆了牛FUT3基因,并在哺乳动物细胞中成功表达重组蛋白,证实其具有α1.3/4-岩藻糖基转移酶活性,参与Lewis抗原合成,为研究FUT3的底物特异性提供基础。
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2. **标题**:Characterization of the enzymatic activity of human recombinant α1.3/4-fucosyltransferase (FUT3)
**作者**:Cheng, P.W., et al.
**摘要**:通过昆虫细胞系统表达并纯化重组人FUT3蛋白,分析其酶动力学参数及糖基化修饰对活性的影响,揭示了其在肿瘤相关糖链合成中的关键作用。
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3. **标题**:Biosynthesis of tumor-related sialyl Lewis X antigen in engineered mammalian cells expressing FUT3
**作者**:Dumic, J., et al.
**摘要**:通过基因工程在CHO细胞中表达重组FUT3.研究其与肿瘤转移标志物sLeX抗原合成的关联,证实FUT3重组蛋白可增强细胞表面糖链的岩藻糖基化修饰。
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注:上述文献为示例性内容,实际引用时请核对真实文献信息。如需具体文章,建议通过PubMed或Sci-Hub检索关键词“FUT3 recombinant expression”或联系相关领域数据库。
**Background of FUT3 Recombinant Protein**
The FUT3 (Fucosyltransferase 3) gene encodes a key enzyme, α1.3/4-fucosyltransferase, responsible for catalyzing the transfer of fucose residues to glycan chains on glycoproteins and glycolipids. This post-translational modification generates Lewis blood group antigens, such as Lewis a (Lea) and Lewis b (Leb), which play critical roles in cell-cell recognition, immune response modulation, and pathogen adhesion. FUT3-mediated fucosylation is essential in various biological processes, including embryogenesis, inflammation, and cancer metastasis.
Recombinant FUT3 protein is produced using biotechnological platforms, such as bacterial (e.g., *E. coli*) or mammalian expression systems, to ensure high purity and functional activity. Its production enables detailed studies of enzyme kinetics, substrate specificity, and interactions with inhibitors or therapeutic antibodies. Dysregulation of FUT3 is linked to diseases like cancer (e.g., colorectal, pancreatic), inflammatory bowel disease, and certain infections, where aberrant fucosylation patterns serve as diagnostic or prognostic biomarkers.
Research on FUT3 recombinant protein also supports the development of diagnostic tools, such as ELISA-based assays for detecting Lewis antigens in clinical samples, and the exploration of targeted therapies to block aberrant fucosylation in tumors. Structural analyses using recombinant FUT3 have elucidated mechanisms underlying its dual α1.3/4-fucosyltransferase activity, guiding the design of enzyme-specific inhibitors. Overall, FUT3 recombinant protein serves as a vital tool for advancing glycobiology research and translational applications in precision medicine.
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