| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUT10 |
| Uniprot No | Q6P4F1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-479aa |
| 氨基酸序列 | LGKFERKEFK SSSLQDGHTK MEEAPTHLNS FLKKEGLTFN RKRKWELDSY PIMLWWSPLT GETGRLGQCG ADACFFTINR TYLHHHMTKA FLFYGTDFNI DSLPLPRKAH HDWAVFHEES PKNNYKLFHK PVITLFNYTA TFSRHSHLPL TTQYLESIEV LKSLRYLVPL QSKNKLRKRL APLVYVQSDC DPPSDRDSYV RELMTYIEVD SYGECLRNKD LPQQLKNPAS MDADGFYRII AQYKFILAFE NAVCDDYITE KFWRPLKLGV VPVYYGSPSI TDWLPSNKSA ILVSEFSHPR ELASYIRRLD SDDRLYEAYV EWKLKGEISN QRLLTALRER KWGVQDVNQD NYIDAFECMV CTKVWANIRL QEKGLPPKRW EAEDTHLSCP EPTVFAFSPL RTPPLSSLRE MWISSFEQSK KEAQALRWLV DRNQNFSSQE FWGLVFKD |
| 预测分子量 | 55 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FUT10重组蛋白的3篇参考文献示例(注：文献信息为模拟示例，实际引用需核实)：
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1. **文献名称**: *"Expression and characterization of recombinant human FUT10 in mammalian cells: Role in core fucosylation"*
**作者**: Smith A, et al.
**摘要**: 本研究利用HEK293细胞成功表达了重组人源FUT10蛋白，并验证其α-1.3-岩藻糖基转移酶活性。实验表明，FUT10可催化N-连接糖链的核心岩藻糖基化，可能影响细胞表面受体(如TGF-β受体)的功能，为癌症中异常糖基化研究提供工具。
2. **文献名称**: *"Bacterial expression and purification of FUT10 for structural analysis"*
**作者**: Zhang L, et al.
**摘要**: 通过优化大肠杆菌表达系统，成功获得可溶性重组FUT10蛋白，并利用亲和层析纯化。晶体结构分析揭示了其底物结合域的关键氨基酸残基，为设计FUT10酶活性抑制剂奠定基础。
3. **文献名称**: *"FUT10-mediated fucosylation promotes cancer cell adhesion via integrin signaling"*
**作者**: Lee H, et al.
**摘要**: 通过重组FUT10蛋白功能实验，发现其介导的岩藻糖修饰可增强整合素依赖的细胞黏附和迁移能力，提示FUT10在肿瘤转移中的潜在作用。研究采用体外糖基化活性检测和细胞模型验证。
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如需具体文献，建议在PubMed或Web of Science中检索关键词 **"FUT10 recombinant protein"** 或 **"FUT10 fucosyltransferase"**，并筛选近年研究。
FUT10 (Fucosyltransferase 10) is a member of the fucosyltransferase family, enzymes that catalyze the transfer of fucose from GDP-fucose to acceptor substrates, playing critical roles in glycosylation processes. Specifically, FUT10 is an α1.3-fucosyltransferase involved in synthesizing glycoconjugates such as Lewis antigens and other fucosylated structures. These modifications are essential for cell-cell recognition, immune responses, and pathogen interactions. The FUT10 gene is located on human chromosome 8 (8p11.21) and encodes a type II transmembrane protein localized to the Golgi apparatus. Unlike other fucosyltransferases (e.g., FUT8 or FUT9), FUT10 exhibits unique substrate preferences, targeting N-glycans and O-glycans on proteins like heparan sulfate proteoglycans, influencing cellular signaling and adhesion.
Recombinant FUT10 protein is produced using expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications and enzymatic activity. Its recombinant form enables detailed studies of fucosylation mechanisms, substrate specificity, and interactions with acceptor molecules. Research highlights its role in cancer progression, where aberrant FUT10 expression correlates with metastasis and poor prognosis, potentially through modulating glycosylation of cell surface receptors like integrins or growth factor receptors. Additionally, FUT10-mediated fucosylation impacts immune regulation, as fucosylated glycans are ligands for selectins involved in leukocyte trafficking.
The development of recombinant FUT10 facilitates drug discovery, particularly for therapies targeting glycosylation-related diseases. Inhibitors or modulators of FUT10 could offer novel strategies against cancer or inflammatory disorders. However, challenges remain in elucidating its precise biological functions due to overlapping activities with other fucosyltransferases and tissue-specific expression patterns. Ongoing studies aim to decode its structural motifs and regulatory mechanisms, advancing glycobiology and therapeutic applications.
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