| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Eogt |
| Uniprot No | Q5NDL2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-527aa |
| 氨基酸序列 | GQN EAPPNTHSIP GEPLYNYASI RLPEEHIPFF LHNNRHIATV CRKDSLCPYK KHLEKLKYCW GYEKSCKPEF RFGYPVCSYV DMGWTDTLES AEDIFWKQAD FGYARERLEE MHVLCQPKET SDSSLVCSRY LQYCRATNLY LDLRNIKRNH DRFKEDFFQS GEIGGHCKLD IRTLTSEGQR KSPLQSWFAE LQSYTQLNFR PIEDAKCDIV IEKPTYFMKL DAGVNMYHHF CDFINLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW NAFTDYDVIH LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFAQHVL HRLNITQEGP KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV DYKYRELGFL DQLRITHNTD IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKHDEL |
| 预测分子量 | 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 **Eogt重组蛋白** 的3篇参考文献及其摘要概括：
1. **文献名称**: *"Epidermal growth factor-like repeats of the Notch receptor require EOGT for O-GlcNAcylation"*
**作者**: Sakaidani Y, et al.
**摘要**: 该研究利用重组表达的EOGT蛋白，证明其在体外和细胞中催化Notch受体表皮生长因子样(EGF)重复序列的特异性O-GlcNAc修饰，并揭示了这种修饰对Notch信号通路活性的调控作用。
2. **文献名称**: *"Expression and characterization of recombinant human EOGT in insect cells"*
**作者**: Yamamoto K, et al.
**摘要**: 作者通过杆状病毒-昆虫细胞系统成功表达并纯化了重组人源EOGT蛋白，系统分析了其酶学特性(如最适pH、金属离子依赖性)，并验证了其对EGF结构域底物的修饰能力。
3. **文献名称**: *"Structural insights into the mechanism of EOGT-mediated O-GlcNAcylation"*
**作者**: Li Z, et al.
**摘要**: 本研究通过X射线晶体学解析了重组EOGT蛋白的三维结构，揭示了其底物识别和催化的分子机制，特别是其与UDP-GlcNAc供体及EGF重复序列结合的活性位点特征。
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**备注**：上述文献为示例，实际引用时需核实具体来源及细节。EOGT相关研究可重点关注其与Notch信号、糖基化机制及疾病模型的关联。
Epidermal Growth Factor domain-specific O-linked N-acetylglucosamine Transferase (Eogt) is a specialized glycosyltransferase that catalyzes the addition of O-linked N-acetylglucosamine (O-GlcNAc) modifications to proteins containing epidermal growth factor (EGF)-like domains. Discovered in 2011. Eogt differs from the broader O-GlcNAc transferase (OGT) by its substrate specificity, targeting extracellular EGF-repeat proteins rather than intracellular nucleocytoplasmic proteins. This post-translational modification, termed EGF-O-GlcNAcylation, plays critical roles in regulating protein folding, trafficking, and signaling, particularly in the Notch signaling pathway—a key regulator of cell differentiation and development.
Recombinant Eogt proteins are engineered to study its enzymatic activity, substrate interactions, and structural mechanisms. These proteins are typically produced in heterologous expression systems (e.g., bacterial or mammalian cells) using gene cloning techniques. Purified recombinant Eogt enables in vitro studies to map O-GlcNAc sites, characterize enzyme kinetics, and explore its interplay with other glycosyltransferases. Research highlights its importance in development, as Eogt knockout models display embryonic lethality in mice and developmental defects resembling Adams-Oliver syndrome in humans. Additionally, aberrant Eogt activity is implicated in cancer metastasis and cardiovascular diseases, making it a potential therapeutic target.
The development of recombinant Eogt has advanced tools for probing O-GlcNAc biology, offering insights into extracellular glycosylation’s role in cellular communication and disease. Further studies aim to unravel its tissue-specific functions and therapeutic applications in glycosylation-related disorders.
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