| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUT7 |
| Uniprot No | Q11130 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-342aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSPRGTPAPQPTITILVWHWPFTDQPPEL PSDTCTRYGIARCHLSANRSLLASADAVVFHHRELQTRRSHLPLAQRPRG QPWVWASMESPSHTHGLSHLRGIFNWVLSYRRDSDIFVPYGRLEPHWGPS PPLPAKSRVAAWVVSNFQERQLRARLYRQLAPHLRVDVFGRANGRPLCAS CLVPTVAQYRFYLSFENSQHRDYITEKFWRNALVAGTVPVVLGPPRATYE AFVPADAFVHVDDFGSARELAAFLTGMNESRYQRFFAWRDRLRVRLFTDW RERFCAICDRYPHLPRSQVYEDLEGWFQA |
| 预测分子量 | 38 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FUT7重组蛋白的参考文献示例(注：以下为假设文献，实际引用需核实真实论文信息)：
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1. **文献名称**：*"Expression and Characterization of Recombinant Human FUT7 in Insect Cells: Role in Sialyl Lewis X Synthesis"*
**作者**：Tanaka Y, et al.
**摘要**：研究利用杆状病毒-昆虫细胞系统表达功能性FUT7重组蛋白，证实其催化合成sLeX(Sialyl Lewis X)的能力，并分析其底物特异性及在炎症中的潜在应用。
2. **文献名称**：*"Functional Analysis of FUT7 Mutants Reveals Critical Residues for α1.3-Fucosyltransferase Activity"*
**作者**：Smith JL, et al.
**摘要**：通过定点突变技术研究重组FUT7的酶活性，鉴定出多个关键氨基酸残基(如Arg112和Glu189)对底物结合和催化效率的影响。
3. **文献名称**：*"High-Yield Production of Soluble Recombinant FUT7 in E. coli for Glycan Remodeling Studies"*
**作者**：Kim H, Park S.
**摘要**：优化大肠杆菌表达系统，成功获得高纯度可溶性FUT7重组蛋白，并用于体外糖链修饰实验，证明其在合成治疗性糖蛋白中的实用性。
4. **文献名称**：*"Crystal Structure of FUT7 in Complex with GDP-Fucose Provides Insights into Substrate Recognition"*
**作者**：Wang X, et al.
**摘要**：解析FUT7重组蛋白与GDP-岩藻糖的复合物晶体结构，揭示其底物结合口袋的构象特征，为设计特异性抑制剂奠定基础。
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**提示**：实际研究中建议通过PubMed或Google Scholar检索关键词“FUT7 recombinant protein”或“FUT7 fucosyltransferase expression”获取真实文献，并优先选择近五年内发表的论文以反映最新进展。
**Background of FUT7 Recombinant Protein**
FUT7 (Fucosyltransferase 7) is a key enzyme in the biosynthesis of selectin ligands, which are carbohydrate structures critical for leukocyte adhesion and inflammatory responses. This α1.3-fucosyltransferase catalyzes the transfer of fucose to sialylated glycans, forming sialyl Lewis X (sLeX) and related epitopes. These glycoconjugates serve as ligands for selectins (E-, P-, and L-selectin), mediating rolling and extravasation of immune cells during inflammation, immune surveillance, and cancer metastasis. The *FUT7* gene, located on human chromosome 9q34.3. is highly expressed in leukocytes and endothelial cells.
Recombinant FUT7 protein is produced using biotechnological platforms (e.g., mammalian, insect, or bacterial expression systems) to enable functional and structural studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate glycan biosynthesis, cell-cell interactions, and the role of sLeX in diseases such as chronic inflammation, autoimmune disorders, and tumor metastasis.
Interest in FUT7 spans therapeutic and diagnostic applications. Inhibiting FUT7 activity could potentially reduce pathological inflammation or block cancer cell dissemination. Conversely, recombinant FUT7 is used *in vitro* to engineer cell surfaces with sLeX for immunotherapy research or to improve homing of therapeutic cells. Additionally, it serves as a tool for glycoengineering biologics, optimizing drug efficacy by modulating glycosylation patterns.
Despite its significance, FUT7 regulation remains complex, involving transcriptional, epigenetic, and metabolic factors. Studies using recombinant FUT7 continue to clarify its substrate specificity, kinetics, and interplay with other fucosyltransferases. Overall, FUT7 recombinant protein is a vital resource for advancing glycobiology and developing targeted therapies in inflammation and oncology.
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