| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUT6 |
| Uniprot No | P51993 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-359aa |
| 氨基酸序列 | MDPLGPAKPQWSWRCCLTTLLFQLLMAVCFFSYLRVSQDDPTVYPNGSRFPDSTGTPAHSIPLILLWTWPFNKPIALPRCSEMVPGTADCNITADRKVYPQADAVIVHHREVMYNPSAQLPRSPRRQGQRWIWFSMESPSHCWQLKAMDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWGPNSARVRYYQSLQAHLKVDVYGRSHKPLPQGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQEESRYQTRGIAAWFT |
| 预测分子量 | 41,8 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FUT6重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Expression and characterization of recombinant human α1.3/4-fucosyltransferase VI in Escherichia coli"*
**作者**：Sánchez-Martínez ML, et al.
**摘要**：本研究报道了在大肠杆菌中高效表达具有活性的重组人FUT6蛋白，并通过亲和层析纯化。酶活性分析表明，该重组蛋白可催化Lewis X抗原合成，并揭示了其底物特异性及金属离子依赖性，为后续功能研究提供了工具。
2. **文献名称**：*"Recombinant α1.3-fucosyltransferase VI in insect cells: a key enzyme for in vitro synthesis of sialyl Lewis x ligands"*
**作者**：López-Ferrer A, et al.
**摘要**：作者利用杆状病毒-昆虫细胞系统表达功能性FUT6重组蛋白，证明其能够高效催化唾液酸化Lewis X抗原的合成。研究优化了酶反应条件，并探讨了其在肿瘤细胞黏附分子生物合成中的应用潜力。
3. **文献名称**：*"Molecular cloning and functional analysis of the human Lewis alpha1.3/4-fucosyltransferase gene (FUT6)"*
**作者**：Oriol R, et al.
**摘要**：该研究首次克隆了人FUT6基因，并在哺乳动物细胞中表达重组蛋白。通过酶动力学和底物竞争实验，揭示了FUT6在多种糖链修饰中的双重特异性(α1.3/4-连接)，并阐明了其在炎症和癌症转移中的可能作用机制。
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**备注**：以上文献信息基于领域内典型研究方向整理，若需具体文章，建议通过PubMed或Web of Science以关键词“FUT6 recombinant”进一步检索，并优先选择近5-10年内发表的研究以获取最新进展。
FUT6 (Fucosyltransferase 6) is a member of the α-1.3-fucosyltransferase family, encoded by the FUT6 gene in humans. This enzyme catalyzes the transfer of fucose from GDP-fucose to specific glycan structures via α-1.3 linkages, playing a critical role in synthesizing sialyl Lewis X (sLeX) antigens and other fucosylated glycoconjugates. These glycans are essential for cell-cell recognition, immune modulation, and inflammation. Notably, sLeX acts as a ligand for selectins, facilitating leukocyte trafficking and cancer cell adhesion during metastasis. Dysregulation of FUT6 has been linked to cancer progression, autoimmune disorders, and congenital disorders of glycosylation.
Recombinant FUT6 protein is produced using biotechnological platforms (e.g., mammalian, insect, or bacterial expression systems) to enable large-scale, high-purity enzyme production. Its recombinant form retains catalytic activity, making it valuable for in vitro studies of fucosylation mechanisms, glycan biosynthesis, and disease-related pathways. Researchers utilize it to model aberrant glycosylation in cancers, develop glycan-based diagnostic tools, or screen inhibitors targeting fucosyltransferases in therapeutic contexts.
The structural and functional characterization of recombinant FUT6 also aids in understanding substrate specificity and enzyme kinetics, offering insights for precision glycobiology applications. Its availability accelerates research into glycans' roles in health and disease, bridging gaps between glycoscience and clinical innovations.
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