| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYC |
| Uniprot No | P01106-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-454aa |
| 氨基酸序列 | MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQ QQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGD NDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMW SGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAA SECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSP EPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAG GHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQ ISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELE NNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLR NSCAESGGGGSPGRRRRRRRRRRR |
| 预测分子量 | 53 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. |
1. **"MYC on the Path to Cancer"** by Dang, C.V. (2012)
- 摘要：综述了MYC蛋白在调控细胞代谢、增殖和凋亡中的核心作用，探讨其异常表达如何导致肿瘤发生，并提及重组MYC蛋白在机制研究中的应用。
2. **"Structural analysis of the MYC/MAX complex using recombinant proteins"** by Nair, S.K. & Burley, S.K. (2003)
- 摘要：通过重组表达纯化的MYC和MAX蛋白，解析了二者形成异源二聚体的晶体结构，揭示了MYC结合DNA的关键结构域。
3. **"Regulation of MYC protein stability by post-translational modifications"** by Conacci-Sorrell, M. et al. (2014)
- 摘要：研究重组MYC蛋白的翻译后修饰(如磷酸化、泛素化)对其稳定性及致癌活性的调控，阐明相关通路对MYC降解的影响。
4. **"Recombinant MYC protein expression systems in E. coli: Challenges and optimization"** by Ji, H. et al. (2018)
- 摘要：探讨在大肠杆菌中高效表达可溶性重组MYC蛋白的技术难点，提出优化策略以提升产量，支持体外功能研究。
(注：以上文献信息为示例，实际引用需根据具体论文内容调整。)
MYC recombinant proteins are engineered versions of the MYC family of transcription factors (c-MYC, MYCN, and MYCL), which play pivotal roles in regulating cell proliferation, differentiation, apoptosis, and metabolism. The MYC genes are proto-oncogenes, and their dysregulation—often via overexpression or amplification—is implicated in numerous cancers. However, targeting MYC directly has been challenging due to its disordered protein structure and lack of conventional drug-binding pockets. Recombinant MYC proteins are produced using genetic engineering techniques, such as bacterial or mammalian expression systems, to study MYC's molecular mechanisms, interactions, and therapeutic potential.
Structurally, MYC proteins contain conserved domains, including the N-terminal transactivation domain and the C-terminal basic helix-loop-helix (bHLH) domain, which mediates dimerization with MAX to bind DNA and regulate target gene expression. Recombinant MYC enables researchers to dissect these domains, map binding partners (e.g., MAX, Miz1), and explore post-translational modifications (e.g., phosphorylation, ubiquitination) that modulate MYC stability and activity.
In cancer research, MYC recombinant proteins aid in screening small molecules or peptides that disrupt MYC-MAX interactions or stabilize inhibitory proteins like MAD. They also serve as antigens for antibody development or tools in structural studies (e.g., crystallography, cryo-EM) to visualize MYC complexes. Despite challenges, recent advances in proteolysis-targeting chimeras (PROTACs) or MYC degradation pathways highlight MYC's therapeutic relevance. Recombinant MYC thus remains a critical resource for unraveling oncogenic signaling and advancing targeted cancer therapies.
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