| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NME3 |
| Uniprot No | Q13232 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-169aa |
| 氨基酸序列 | MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGF KLVALKLVQASEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDV VRTSRALIGATNPADAPPGTIRGDFCIEVGKNLIHGSDSVESARREIALW FRADELLCWEDSAGHWLYE |
| 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NME3重组蛋白的模拟参考文献(内容为示例，建议通过学术数据库核实)：
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1. **文献名称**：*Structural and functional characterization of recombinant human NME3 protein*
**作者**：Smith A, et al.
**摘要**：本研究通过大肠杆菌系统表达并纯化了重组人NME3蛋白，利用X射线晶体学解析其三维结构。结果表明，NME3具有典型的核苷二磷酸激酶活性，并揭示了其ATP结合位点的关键氨基酸残基，为研究其与线粒体功能的关联提供了结构基础。
2. **文献名称**：*NME3 regulates mitochondrial dynamics via interaction with DRP1: Insights from recombinant protein assays*
**作者**：Chen L, et al.
**摘要**：通过重组NME3蛋白的体外实验，发现其与线粒体分裂蛋白DRP1直接结合，并增强DRP1的GTP酶活性。该研究揭示了NME3在调控线粒体形态和细胞凋亡中的新机制，提示其在神经退行性疾病中的潜在作用。
3. **文献名称**：*Recombinant NME3 suppresses tumor cell migration by modulating Rho-GTPase signaling pathways*
**作者**：Wang Y, et al.
**摘要**：在乳腺癌细胞模型中，外源性重组NME3蛋白显著抑制细胞迁移和侵袭。机制研究表明，NME3通过调控RhoA/ROCK信号通路影响细胞骨架重塑，为开发基于NME3的抗肿瘤策略提供了实验依据。
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**注意**：以上文献信息为模拟生成，实际研究请通过PubMed、Web of Science等平台检索确认。
**Background of NME3 Recombinant Protein**
NME3 (non-metastatic protein 3), also known as NM23-H3. is a member of the NME/NM23 nucleoside diphosphate kinase (NDPK) family, which plays multifaceted roles in cellular metabolism, signal transduction, and disease progression. Initially identified for its metastasis-suppressing properties in certain cancers, the NME family has expanded to include isoforms with diverse functions. NME3. in particular, is implicated in mitochondrial dynamics, energy homeostasis, and apoptosis regulation, distinguishing it from other family members.
Structurally, NME3 contains a conserved NDPK domain critical for catalyzing the transfer of phosphate groups between nucleoside diphosphates and triphosphates, supporting nucleotide pool balance. Unlike NME1/2. NME3 possesses an N-terminal extension that facilitates its localization to mitochondria, where it interacts with proteins like OPA1 to regulate mitochondrial fusion and cristae structure. This mitochondrial association links NME3 to cellular stress responses and metabolic adaptations.
Recombinant NME3 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for research. Its production enables detailed biochemical studies, such as enzymatic activity assays, protein-protein interaction mapping, and structural analyses. Researchers leverage recombinant NME3 to explore its role in diseases like cancer, neurodegenerative disorders, and cardiovascular conditions, where mitochondrial dysfunction or altered nucleotide metabolism is implicated.
Emerging evidence suggests NME3's dual role in cancer—acting as both a tumor suppressor and a context-dependent promoter of survival—highlights its therapeutic potential. Recombinant NME3 also serves as a tool for drug screening, aiming to modulate its activity in pathological states. Ongoing studies focus on clarifying its mechanisms in mitochondrial dynamics and apoptosis, which may unlock novel strategies for targeting metabolic or stress-related diseases.
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