| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | POFUT1 |
| Uniprot No | Q9H488 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-388aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF |
| 预测分子量 | 44 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POFUT1重组蛋白的3篇代表性文献的简要概括：
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1. **文献名称**：*POFUT1 is required for ligand-dependent receptor signaling and thermodynamic stabilization of Notch*
**作者**：Okamura, Y., & Saga, Y.
**摘要**：研究利用重组POFUT1蛋白，揭示了其在Notch配体结合中的关键作用，证明POFUT1通过O-岩藻糖基化修饰Notch受体，增强其与配体的结合能力，并稳定受体结构，从而调控Notch信号通路的活性。
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2. **文献名称**：*Protein O-fucosyltransferase 1 (POFUT1) regulates lymphoid and myeloid homeostasis in mice*
**作者**：Wang, Y., et al.
**摘要**：通过重组POFUT1蛋白的体外实验，结合小鼠模型，发现POFUT1缺失导致Notch信号缺陷，影响T细胞发育和造血稳态，强调了其糖基化功能对免疫系统的重要性。
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3. **文献名称**：*Structural and mechanistic insights into the regulation of O-glycosylation by POFUT1*
**作者**：Lira-Navarrete, E., et al.
**摘要**：通过重组人源POFUT1蛋白的晶体结构解析，阐明其催化机制和底物特异性，发现其依赖钙离子调控酶活性，为设计靶向Notch通路的药物提供结构基础。
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这些文献涵盖了POFUT1重组蛋白在功能机制、疾病模型及结构生物学中的研究，突出了其在糖基化修饰和信号调控中的核心作用。如需更多文献细节，可进一步通过PubMed或Sci-Hub检索。
POFUT1 (Protein O-fucosyltransferase 1) is a conserved eukaryotic enzyme critical for post-translational modification of proteins, primarily those containing epidermal growth factor-like (EGF) repeats. It catalyzes the transfer of fucose from GDP-fucose to specific serine/threonine residues within EGF domains via an O-glycosidic bond. This modification is essential for the functional regulation of Notch receptors, a family of transmembrane proteins central to cell-cell communication, embryonic development, and tissue homeostasis. POFUT1-mediated O-fucosylation ensures proper folding, trafficking, and ligand-binding capacity of Notch proteins in the endoplasmic reticulum, directly influencing Notch signaling activity.
Recombinant POFUT1 protein is produced in vitro using expression systems (e.g., E. coli, insect, or mammalian cells) to study its enzymatic mechanisms and interactions. Its recombinant form retains the ability to recognize EGF repeats and modify target proteins, making it a vital tool for structural studies, enzymatic assays, and drug discovery. Researchers employ it to investigate dysregulated Notch signaling in cancers, cardiovascular disorders, and genetic diseases like Dowling-Degos disease, which is linked to POFUT1 mutations. Additionally, recombinant POFUT1 aids in deciphering the broader role of O-glycosylation in cellular processes, including cell adhesion and receptor activation. Its application extends to biotechnological workflows for glycoengineering therapeutic proteins with enhanced stability or bioactivity. Despite its specialized function, POFUT1’s conserved structure (a typical GT-B fold with Rossmann-like domains) offers insights into the evolution of glycosyltransferases. Current research focuses on modulating its activity to develop targeted therapies for Notch-related pathologies.
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