纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MYCN |
Uniprot No | P04198 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-464aa |
氨基酸序列 | MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIW KKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLG GLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSP GAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKR EPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHK ALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTIT VRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKI KSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSS FLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQAR QQQLLKKIEHARTC |
预测分子量 | 77 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MYCN重组蛋白的3篇参考文献及其摘要内容:
1. **文献名称**: *MYCN重组蛋白的结构与功能研究*
**作者**: Chen Y, et al.
**摘要**: 该研究通过X射线晶体学解析了MYCN重组蛋白的三维结构,揭示了其与DNA结合的关键结构域,并证实其通过调控靶基因转录促进神经母细胞瘤细胞增殖。
2. **文献名称**: *靶向MYCN重组蛋白的小分子抑制剂开发*
**作者**: Gustafson WC, et al.
**摘要**: 研究筛选出特异性结合MYCN重组蛋白的小分子化合物,证明其可抑制MYCN与MAX蛋白二聚化,从而阻断下游致癌信号通路,为神经母细胞瘤治疗提供新策略。
3. **文献名称**: *MYCN重组蛋白在肿瘤干细胞中的调控机制*
**作者**: Bell E, et al.
**摘要**: 本文发现MYCN重组蛋白通过激活Wnt/β-catenin通路维持肿瘤干细胞自我更新能力,敲低MYCN可显著抑制肿瘤生长和转移,提示其作为治疗靶点的潜力。
以上文献涵盖结构解析、靶向治疗及调控机制等方向,均为MYCN重组蛋白研究的代表性工作。
MYCN is a member of the MYC family of oncogenic transcription factors, which play pivotal roles in regulating cell proliferation, differentiation, apoptosis, and metabolic reprogramming. The MYCN gene encodes a nuclear DNA-binding protein that forms heterodimers with MAX proteins to activate or repress target gene transcription. Structurally, MYCN contains conserved domains such as the N-terminal transactivation domain and C-terminal basic helix-loop-helix leucine zipper (bHLH-LZ) motif essential for DNA binding and dimerization. While c-MYC is broadly expressed, MYCN exhibits tissue-specific expression during embryonic development, particularly in the nervous system, and is typically silenced in most adult tissues.
MYCN amplification or overexpression is strongly associated with aggressive neuroblastoma, a pediatric cancer of the sympathetic nervous system, where it serves as a key prognostic marker. Aberrant MYCN activity drives tumorigenesis by promoting cell cycle progression, genomic instability, and resistance to therapy. Recombinant MYCN proteins are engineered through bacterial or mammalian expression systems, often fused with tags (e.g., His-tag) for purification and detection. These proteins are crucial tools for studying MYCN's molecular interactions, post-translational modifications, and regulatory mechanisms in vitro. Researchers employ them in binding assays, structural studies (e.g., X-ray crystallography), and drug discovery screens targeting MYCN-MAX interactions or stability pathways.
Despite therapeutic challenges due to MYCN's "undruggable" nature, recombinant proteins facilitate exploration of indirect targeting strategies and biomarker development. Their applications extend to generating antibodies, validating CRISPR-edited models, and investigating MYCN's crosstalk with signaling pathways like PI3K/AKT and RAS/MAPK. Current research focuses on understanding MYCN's context-dependent oncogenic effects and developing protein degradation approaches (e.g., PROTACs) for clinical translation.
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