| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUT1 |
| Uniprot No | P19526 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-365aa |
| 氨基酸序列 | MWLRSHRQLCLAFLLVCVLSVIFFLHIHQDSFPHGLGLSILCPDRRLVTPPVAIFCLPGTAMGPNASSSCPQHPASLSGTWTVYPNGRFGNQMGQYATLLALAQLNGRRAFILPAMHAALAPVFRITLPVLAPEVDSRTPWRELQLHDWMSEEYADLRDPFLKLSGFPCSWTFFHHLREQIRREFTLHDHLREEAQSVLGQLRLGRTGDRPRTFVGVHVRRGDYLQVMPQRWKGVVGDSAYLRQAMDWFRARHEAPVFVVTSNGMEWCKENIDTSQGDVTFAGDGQEATPWKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFKPEAAFLPEWVGINADLSPLWTLAKP |
| 预测分子量 | 41,2 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FUT1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: *"Expression and characterization of recombinant human α1.2-fucosyltransferase (FUT1) in mammalian cells"*
**作者**: Smith A, et al.
**摘要**: 本研究在HEK293哺乳动物细胞中成功表达并纯化了重组人源FUT1蛋白，验证了其在体外催化H抗原合成的酶活性，为血型抗原研究提供了工具。
2. **文献名称**: *"Cloning and functional analysis of FUT1 in Escherichia coli for glycoengineering applications"*
**作者**: Zhang L, et al.
**摘要**: 通过在大肠杆菌中优化表达条件，实现了FUT1重组蛋白的高效生产，并证明其可用于细菌表面糖基化工程，拓展了其在合成生物学中的应用。
3. **文献名称**: *"Structural insights into the substrate specificity of FUT1 through recombinant protein crystallography"*
**作者**: Tanaka K, et al.
**摘要**: 利用重组FUT1蛋白的晶体结构解析，揭示了其底物结合域的关键氨基酸残基，阐明了α-1.2-岩藻糖转移反应的分子机制。
注：以上文献信息为示例性质，实际引用需根据具体研究通过学术数据库检索确认。
FUT1 (Fucosyltransferase 1) is a Golgi-resident enzyme encoded by the *FUT1* gene in humans, located on chromosome 19q13.33. It catalyzes the transfer of fucose to terminal galactose residues via α-1.2-linkages, forming the H antigen—a critical precursor for ABO blood group antigens on red blood cells and mucosal surfaces. This glycosylation process is vital for cell-cell interactions, immune responses, and microbial adhesion.
Recombinant FUT1 protein is engineered using heterologous expression systems (e.g., mammalian cells, bacteria, or yeast) to produce the enzymatically active form for research and biotechnological applications. Its recombinant production enables studies on blood group biochemistry, host-pathogen interactions (e.g., *Helicobacter pylori* binding to H antigen), and cancer biology, as aberrant FUT1-mediated fucosylation is linked to tumor metastasis and immune evasion.
Structural analysis of recombinant FUT1 has revealed insights into its substrate-binding domains and catalytic mechanisms, guiding the development of inhibitors for therapeutic purposes. Additionally, it serves as a tool for synthesizing H antigen-containing glycoconjugates in vitro. Mutations in *FUT1* cause the rare Bombay phenotype (lack of H antigen), underscoring its clinical relevance. Current research leverages recombinant FUT1 to explore glycosylation disorders, glycoengineering of therapeutic proteins, and glycan-based vaccine design.
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