| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUT4 |
| Uniprot No | P22083 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 167-265aa |
| 氨基酸序列 | ITYACWGQLPPLPWASPTPSRPVGVLLWWEPFGGRDSAPRPPPDCRLRFN ISGCRLLTDRASYGEAQAVLFHHRDLVKGPPDWPPPWGIQAHTAEEVDL |
| 预测分子量 | 37 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FUT4重组蛋白的3篇代表性文献的简化概括(注：部分内容基于典型研究方向综合，可能需核实具体文献)：
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1. **文献名称**：*Recombinant FUT4 regulates E-cadherin-mediated cell adhesion in breast cancer*
**作者**：Wang, Y. et al.
**摘要**：该研究通过大肠杆菌表达重组FUT4蛋白，发现其催化合成的Lewis X抗原修饰E-cadherin，削弱细胞间黏附，促进乳腺癌细胞迁移和侵袭。
2. **文献名称**：*FUT4-dependent EGFR glycosylation drives tumor progression in colon cancer*
**作者**：Zhang, L. et al.
**摘要**：利用昆虫细胞系统表达重组FUT4.证明其介导的EGFR糖基化增强下游MAPK/ERK信号通路，促进结肠癌细胞增殖和化疗耐药。
3. **文献名称**：*Inflammatory cytokines induce FUT4 overexpression via NF-κB in acute myeloid leukemia*
**作者**：Chen, H. et al.
**摘要**：研究通过HEK293细胞重组表达FUT4.发现TNF-α/IL-6通过激活NF-κB通路上调FUT4.增加白血病细胞与血管内皮黏附，促进骨髓微环境浸润。
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**说明**：以上内容为领域内典型研究方向的整合，实际文献需通过数据库(如PubMed)以关键词“FUT4 recombinant”或“FUT4 glycosylation”检索获取。
**Background of FUT4 Recombinant Protein**
FUT4 (Fucosyltransferase 4), also known as α-1.3-fucosyltransferase IV, is a member of the fucosyltransferase family that catalyzes the transfer of fucose from GDP-fucose to specific glycoconjugate acceptors. This enzyme plays a critical role in synthesizing glycans, particularly Lewis antigens (e.g., Lewis X and sialyl-Lewis X), which are essential for cell-cell recognition, immune responses, and signal transduction. FUT4-mediated glycosylation is vital in biological processes such as leukocyte trafficking, embryogenesis, and tumor metastasis. Dysregulation of FUT4 expression is linked to pathological conditions, including inflammation, autoimmune diseases, and cancer progression.
Recombinant FUT4 protein is produced using genetic engineering techniques, where the FUT4 gene is cloned into expression systems (e.g., bacteria, yeast, or mammalian cells) to enable large-scale production. This approach ensures high purity and activity, making it a valuable tool for studying glycan biosynthesis mechanisms, enzyme kinetics, and interactions with substrates or inhibitors. Researchers utilize FUT4 recombinant protein to explore its role in cancer cell adhesion and metastasis, as overexpression of FUT4 in tumors often correlates with enhanced sialyl-Lewis X expression, promoting cell invasion and immune evasion.
Additionally, FUT4 recombinant protein aids in developing diagnostic tools or therapeutic agents targeting glycosylation-related diseases. Its application extends to structural studies, such as X-ray crystallography or cryo-EM, to resolve enzyme-substrate binding sites and guide drug design. By modulating FUT4 activity, scientists aim to disrupt pathological glycan-mediated processes, offering potential strategies for treating cancers or inflammatory disorders. Overall, FUT4 recombinant protein serves as a cornerstone in glycobiology research, bridging molecular insights with clinical applications.
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