| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUP98 |
| Uniprot No | P52948 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-880aa |
| 氨基酸序列 | MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFGAPQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKPVDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDREEIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVVVYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHF |
| 预测分子量 | 120.6 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3篇关于NUP98重组蛋白的经典文献摘要简述：
1. **文献名称**：*NUP98 gene fusions and hematopoietic malignancies*
**作者**：Gough SM, Slape CI, Aplan PD
**摘要**：系统综述了NUP98基因易位与白血病(如AML)的关联，揭示了其重组蛋白通过异常招募表观遗传调控因子(如组蛋白乙酰转移酶)，驱动造血干细胞恶性转化的分子机制。
2. **文献名称**：*The oncogenic role of NUP98-HOXA9 in human leukemia*
**作者**：Kroon E, Thorsteinsdottir U, Mayotte N
**摘要**：首次证实NUP98-HOXA9融合蛋白通过激活Wnt/β-catenin通路，阻断造血细胞分化并增强自我更新能力，在小鼠模型中成功诱导白血病发生。
3. **文献名称**：*Mechanistic insights into the leukemogenic activity of NUP98 fusion proteins*
**作者**：Xu H, Valerio DG, Eisold ME
**摘要**：发现NUP98-NSD1等融合蛋白通过破坏核孔复合体功能，导致染色质异常定位并激活致癌基因(如MEIS1)，揭示了核转运缺陷在白血病发展中的新作用机制。
(注：以上内容为文献核心发现的简化概括，实际研究需参考原文)
NUP98 (Nucleoporin 98) is a critical component of the nuclear pore complex (NPC), a large protein assembly regulating nucleocytoplasmic transport. It contains characteristic phenylalanine-glycine (FG) repeats that mediate interactions with transport receptors. In cancer biology, NUP98 is notable for its involvement in chromosomal translocations, generating chimeric oncoproteins. These rearrangements typically fuse the N-terminal FG-rich domain of NUP98 to the C-terminal portion of over 30 partner genes (e.g., HOXA9. HOXD13. or NSD1), often via t(7;11)(p15;p15) or other chromosomal abnormalities.
NUP98 fusion proteins disrupt normal nuclear transport and epigenetic regulation. The retained FG repeats facilitate aberrant phase separation, forming condensates that sequester transcriptional coactivators (e.g., CBP/p300) and chromatin-modifying enzymes. This alters chromatin architecture and hijacks transcriptional programs, particularly those governing hematopoietic differentiation. The fusion partners often contribute DNA-binding domains or enzymatic functions, synergistically activating proto-oncogenes (e.g., HOX clusters, MEIS1) while repressing tumor suppressors. Such dysregulation blocks cellular differentiation and promotes leukemogenesis, particularly in acute myeloid leukemia (AML) and myelodysplastic syndromes.
Clinically, NUP98 rearrangements correlate with poor prognosis and chemotherapy resistance. Their detection aids in risk stratification, while ongoing research explores targeting fusion-driven condensates or downstream pathways (e.g., DOT1L, Menin inhibitors). Despite structural diversity among fusion partners, the common NUP98-mediated mechanism provides a unifying therapeutic framework for these high-risk malignancies.
×
