| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NAE1 |
| Uniprot No | Q13564 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-534aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAAIYGG VEGGGTRSEV LLVSEDGKIL AEADGLSTNH WLIGTDKCVE RINEMVNRAK RKAGVDPLVP LRSLGLSLSG GDQEDAGRIL IEELRDRFPY LSESYLITTD AAGSIATATP DGGVVLISGT GSNCRLINPD GSESGCGGWG HMMGDEGSAY WIAHQAVKIV FDSIDNLEAA PHDIGYVKQA MFHYFQVPDR LGILTHLYRD FDKCRFAGFC RKIAEGAQQG DPLSRYIFRK AGEMLGRHIV AVLPEIDPVL FQGKIGLPIL CVGSVWKSWE LLKEGFLLAL TQGREIQAQN FFSSFTLMKL RHSSALGGAS LGARHIGHLL PMDYSANAIA FYSYTFS |
| 预测分子量 | 63 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NAE1重组蛋白的3篇代表性文献摘要概括(文献信息为模拟生成，仅供示例参考)：
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1. **文献名称**: *Structural basis for NEDD8 activation by the NAE1-UBA3 heterodimer*
**作者**: Walden H, et al.
**摘要**: 该研究解析了NAE1与UBA3形成的异源二聚体复合物的晶体结构，揭示了其催化NEDD8激活的分子机制。通过重组蛋白表达和生化实验，阐明了NAE1在NEDDylation通路中的关键作用及底物特异性识别机制。
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2. **文献名称**: *Development of a high-throughput assay for NAE1 enzymatic activity using recombinant protein*
**作者**: Brownell JE, et al.
**摘要**: 作者利用重组NAE1蛋白建立了一种基于荧光信号的酶活性高通量筛选平台，用于筛选NAE1抑制剂。该研究优化了重组蛋白纯化条件，验证了其在药物开发中的应用潜力。
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3. **文献名称**: *NAE1 knockdown and recombinant protein rescue experiments define its role in cell cycle regulation*
**作者**: Soucy TA, et al.
**摘要**: 通过基因敲除和重组NAE1蛋白回补实验，证明NAE1通过调控Cullin蛋白的NEDDylation修饰影响细胞周期进程。重组蛋白成功恢复了敲除细胞中异常的S期停滞表型。
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注：以上文献信息为基于领域内典型研究方向的人工概括，实际引用请以具体论文内容为准。
**Background of NAE1 Recombinant Protein**
NAE1 (NEDD8 Activating Enzyme E1 Subunit 1), a critical component of the NEDD8 activation enzyme, plays a pivotal role in the post-translational modification pathway known as neddylation. This process involves the covalent attachment of NEDD8 (Neural Precursor Cell Expressed Developmentally Downregulated Protein 8) to specific substrate proteins, primarily targeting cullin family members. Neddylation regulates the activity of cullin-RING E3 ubiquitin ligases (CRLs), which are essential for ubiquitin-mediated proteasomal degradation of proteins involved in cell cycle progression, DNA repair, and signal transduction. Dysregulation of NAE1 has been implicated in various pathologies, including cancer, neurodegenerative disorders, and immune dysfunction, making it a promising therapeutic target.
Recombinant NAE1 protein is produced using biotechnological methods, such as expression in *E. coli* or mammalian cell systems, followed by purification to ensure high specificity and activity. This engineered protein retains the functional domains required for NEDD8 activation, including the ATP-binding site and NEDD8 recognition motifs. Researchers utilize recombinant NAE1 to study neddylation mechanisms, screen inhibitors, and explore its structural and biochemical properties.
In cancer research, NAE1 inhibition has gained attention due to the overexpression of neddylation pathways in tumors. Small-molecule inhibitors, like MLN4924 (Pevonedistat), which targets NAE1. have shown preclinical efficacy by inducing apoptosis and cell cycle arrest. Recombinant NAE1 is instrumental in elucidating inhibitor binding modes and optimizing drug candidates.
Moreover, structural studies using recombinant NAE1. such as X-ray crystallography or cryo-EM, have revealed conformational changes during NEDD8 activation, aiding in the design of next-generation therapeutics. Despite progress, challenges like off-target effects and resistance mechanisms necessitate further exploration.
Overall, NAE1 recombinant protein serves as a vital tool for advancing our understanding of neddylation biology and developing targeted therapies for diseases linked to ubiquitin-proteasome dysregulation.
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