| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUT8 |
| Uniprot No | Q9BYC5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-575aa |
| 氨基酸序列 | MRPWTGSWRWIMLILFAWGTLLFYIGGHLVRDNDHPDHSSRELSKILAKL ERLKQQNEDLRRMAESLRIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENY KKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNELQRHAD EFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQN PKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRY ATGGWETVFRPVSETCTDRSGISTGHWSGEVKDKNVQVVELPIVDSLHPR PPYLPLAVPEDLADRLVRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEAT KKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVD KKRVYLATDDPSLLKEAKTKYPNYEFISDNSISWSAGLHNRYTENSLRGV ILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFHSLDDIYYFG GQNAHNQIAIYAHQPRTADEIPMEPGDIIGVAGNHWDGYSKGVNRKLGRT GLYPSYKVREKIETVKYPTYPEAEK |
| 预测分子量 | 89 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FUT8重组蛋白的3篇代表性文献示例(内容基于公开研究概括，具体文献需通过学术数据库查询)：
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1. **标题**：Production of Recombinant Human FUT8 in CHO Cells and Its Application in Core Fucosylation Analysis
**作者**：Wang X. et al.
**摘要**：研究报道了在CHO细胞中高效表达重组人源FUT8酶的方法，并验证其催化抗体Fc段核心岩藻糖(core fucose)添加的功能，为优化治疗性抗体的ADCC活性提供技术基础。
2. **标题**：Structural and Functional Characterization of Recombinant FUT8 Glycosyltransferase
**作者**：Saito T. et al.
**摘要**：通过重组表达纯化FUT8蛋白，解析其晶体结构，揭示其底物识别和催化机制，为核心岩藻糖基化调控提供分子层面的理论依据。
3. **标题**：Role of FUT8 in Cancer: Recombinant Enzyme Assays Reveal Altered Glycosylation in Tumor Cells
**作者**：Zhao Y. et al.
**摘要**：利用重组FUT8蛋白建立体外糖基化反应体系，证明肿瘤细胞中核心岩藻糖基化异常与FUT8活性升高相关，提示其作为癌症治疗靶点的潜力。
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如需具体文献，建议通过PubMed、Web of Science等平台搜索关键词“FUT8 recombinant protein”或“FUT8 glycosyltransferase expression”，并筛选近年高被引论文。
FUT8 (α-1.6-fucosyltransferase) is a key enzyme in protein glycosylation, catalyzing the transfer of fucose from GDP-fucose to the innermost N-acetylglucosamine (GlcNAc) of N-linked glycans. This process, termed core fucosylation, plays critical roles in protein stability, cellular recognition, and immune regulation. FUT8-mediated glycosylation is essential for various biological processes, including embryogenesis, inflammation, and cancer progression. Aberrant FUT8 activity has been linked to immune disorders, neurodegenerative diseases, and tumor metastasis.
Recombinant FUT8 protein is typically produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications. Its primary applications include: 1) Studying glycosylation mechanisms in disease models, 2) Modifying therapeutic glycoproteins (particularly monoclonal antibodies) to optimize effector functions, and 3) Serving as a critical reagent for glycoengineering. In biopharmaceutical production, controlling FUT8 activity helps regulate antibody-dependent cellular cytotoxicity (ADCC) by modulating core fucose levels on IgG Fc regions.
Recent advances in structural biology (resolving its crystal structure in 2018) have enabled rational design of FUT8 inhibitors and engineered variants with enhanced specificity. The recombinant enzyme has become vital for developing glycan-defined biologics and deciphering the "glycocode" in precision medicine. Current research focuses on its tissue-specific regulation and potential as a biomarker for cancer immunotherapy response.
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