| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPM1 |
| Uniprot No | P06748 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-294aa |
| 氨基酸序列 | MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL |
| 预测分子量 | 36.7 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NPM1重组蛋白的3篇代表性文献(注：文献信息为模拟示例，具体内容需根据实际研究补充)：
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1. **文献名称**：*Mutant nucleophosmin (NPM1) induces AML progression by altering chromatin accessibility and nuclear phase separation*
**作者**：Falini, B., et al.
**摘要**：研究揭示了NPM1突变体(NPM1c)通过破坏核仁结构，导致异常的染色质可及性和液-液相分离(LLPS)，促进急性髓系白血病(AML)的发生。突变NPM1重组蛋白的核质穿梭异常是其致癌的关键机制。
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2. **文献名称**：*Structural basis of NPM1 mutant recognition by export receptors and therapeutic targeting*
**作者**：Grill, S.W., et al.
**摘要**：通过冷冻电镜解析突变NPM1重组蛋白与核输出受体XPO1的复合物结构，阐明其异常核输出的分子机制，并提出靶向该互作的小分子抑制剂可恢复NPM1核定位，抑制白血病细胞增殖。
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3. **文献名称**：*NPM1 interacts with ARF to regulate p53-dependent apoptosis in leukemia*
**作者**：Colombo, E., et al.
**摘要**：研究发现野生型NPM1通过与ARF蛋白结合稳定p53.而突变NPM1重组蛋白失去此功能，导致p53降解和细胞凋亡逃逸，揭示了NPM1突变促进白血病耐药性的分子途径。
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**提示**：以上为模拟摘要，实际文献需通过PubMed或Google Scholar搜索关键词“NPM1 recombinant protein”“NPM1 mutation leukemia”获取。建议优先选择高影响力期刊(如*Blood*、*Nature Cancer*)及领域内权威团队(如Falini, B.)的研究。
NPM1 (Nucleophosmin 1) is a multifunctional nucleolar protein encoded by the *NPM1* gene located on chromosome 5q35. It plays critical roles in ribosome biogenesis, centrosome duplication, cell cycle regulation, and stress response. Structurally, NPM1 contains a conserved N-terminal oligomerization domain, a central histone-binding region, and a C-terminal nucleic acid-binding domain. Under physiological conditions, NPM1 shuttles between the nucleolus and nucleoplasm, maintaining genomic stability and regulating apoptosis.
In hematological malignancies, particularly acute myeloid leukemia (AML), recurrent *NPM1* mutations (commonly exon 12 frameshifts) result in cytoplasmic mislocalization of the mutant protein (NPM1c+). These mutations create a novel nuclear export signal and disrupt nucleolar localization signals, causing aberrant accumulation in the cytoplasm. This mislocalization is recognized as a key driver of leukemogenesis, often cooperating with other genetic alterations like *FLT3*-ITD. NPM1 mutations occur in approximately 30% of AML cases and define a distinct WHO classification category.
Recombinant NPM1 proteins, produced through bacterial (e.g., *E. coli*) or eukaryotic expression systems, are essential tools for studying these mechanisms. They enable biochemical characterization of mutant vs. wild-type protein interactions, particularly with binding partners like ARF, p53. and chromatin. Researchers use recombinant NPM1 to investigate structural consequences of mutations, develop targeted therapies (e.g., nuclear export inhibitors), and create diagnostic assays. Recent applications include CRISPR-based correction studies and drug screening platforms to identify compounds that reverse NPM1c+ mislocalization. The protein's chaperone-like properties and role in liquid-liquid phase separation also make it relevant to broader cancer and neurodegenerative disease research.
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