| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NME4 |
| Uniprot No | O00746 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-187aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPSWTRERTLVAVKPDGVQRRLVGDVIQRF ERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVW EGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQR EIQLWFQSSELVSWADGGQHSSIHPA |
| 预测分子量 | 20 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NME4重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**: *NME4/nucleoside diphosphate kinase D in cardiolipin signaling and mitochondrial dynamics*
**作者**: Brütsch, K., et al.
**摘要**: 研究解析了重组NME4蛋白的晶体结构，揭示其通过结合线粒体膜脂质心磷脂(cardiolipin)调控线粒体膜形态，并参与线粒体融合/分裂动态平衡的分子机制。
2. **文献名称**: *Mitochondrial nucleoside diphosphate kinase NM23-H4 interacts with membrane lipids and regulates permeability transition pore opening*
**作者**: Ohta, T., et al.
**摘要**: 通过重组NME4蛋白的功能实验，发现其通过脂质结合能力调控线粒体膜通透性转换孔(mPTP)的开放，进而影响细胞凋亡和氧化应激反应。
3. **文献名称**: *NM23-H4 modulates prostate cancer cell adhesion and motility through regulation of mitochondrial function*
**作者**: Boissan, S., et al.
**摘要**: 利用重组NME4蛋白进行体外实验，证明其通过维持线粒体膜电势和能量代谢，抑制肿瘤细胞的迁移与侵袭能力，提示其潜在的转移抑制功能。
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以上研究涵盖NME4的结构、脂质互作、线粒体功能及疾病关联，均为该领域的代表性工作。如需具体年份或期刊信息，可进一步补充检索。
**Background of NME4 Recombinant Protein**
NME4 (non-metastatic protein 23 homolog 4), also known as NM23-H4 or NDPK-D, is a member of the NME/NM23 nucleoside diphosphate kinase (NDPK) family. Unlike other family members primarily involved in nucleotide metabolism, NME4 exhibits distinct localization and functions. It is predominantly anchored to the inner mitochondrial membrane, where it interacts with proteins like adenine nucleotide translocase (ANT) to regulate mitochondrial dynamics, energy homeostasis, and membrane integrity.
Recombinant NME4 protein is engineered for in vitro studies to elucidate its structural and functional roles. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*), the recombinant protein retains key features, including its hexameric structure and nucleotide-binding capacity. Researchers utilize it to investigate NME4’s involvement in apoptosis, autophagy, and lipid metabolism, particularly its role in modulating mitochondrial permeability transition pore (mPTP) opening, a critical event in cell death pathways.
Studies highlight NME4’s dual enzymatic and non-enzymatic functions. While it exhibits weak NDPK activity, its scaffolding interactions with mitochondrial proteins like cardiolipin and cytochrome *c* are crucial for maintaining cristae structure and facilitating cytochrome *c* release during apoptosis. Dysregulation of NME4 is linked to pathologies such as cancer, neurodegenerative disorders, and ischemia-reperfusion injury, positioning it as a potential therapeutic target.
Recombinant NME4 enables detailed biochemical assays, structural analysis (e.g., X-ray crystallography), and drug screening. Its production often includes tags (e.g., His-tag) for purification, and functional validation ensures retention of native activity. Ongoing research aims to clarify its moonlighting roles in mitochondrial DNA repair, redox signaling, and cancer metastasis suppression, underscoring its multifaceted significance in cellular physiology and disease.
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