| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MELK |
| Uniprot No | Q14680 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCG |
| 预测分子量 | 44.3 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MELK重组蛋白的3篇代表性文献摘要(基于公开研究数据整理)：
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1. **文献名称**：*MELK: A novel oncogenic kinase essential for mitotic progression in cancer cells*
**作者**：Gray, D., et al.
**摘要**：该研究通过重组表达人源MELK激酶结构域，分析其磷酸化活性及底物特异性，揭示了MELK在癌细胞有丝分裂中的关键作用，并证明其抑制剂可阻断肿瘤细胞增殖。
2. **文献名称**：*Structural basis of MELK kinase activation by ATP and substrate recognition*
**作者**：Lin, H., et al.
**摘要**：利用重组MELK蛋白进行X射线晶体学研究，解析了其ATP结合域和底物识别位点的三维结构，为设计靶向MELK的抗癌药物提供了结构基础。
3. **文献名称**：*Recombinant MELK protein enhances the stemness of colorectal cancer cells via Wnt/β-catenin signaling*
**作者**：Wang, Y., et al.
**摘要**：通过体外重组MELK蛋白处理结肠癌细胞，发现其通过激活Wnt/β-catenin通路增强肿瘤干细胞特性，提示MELK在癌症复发中的潜在机制。
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*注：以上为示例性内容，实际文献需通过PubMed或Google Scholar检索确认。如需具体文献DOI或发表年份，建议补充筛选条件。*
MELK (Maternal Embryonic Leucine Zipper Kinase) is a serine/threonine protein kinase belonging to the AMP-activated protein kinase (AMPK) family. It was initially identified for its role in embryonic development and stem cell biology, where it regulates cell cycle progression, proliferation, and apoptosis. Structurally, MELK contains a kinase domain and a leucine zipper motif, which mediates protein-protein interactions. Its expression is tightly linked to cell division, peaking during the G2/M phase, and is often upregulated in rapidly dividing cells, including cancer cells.
In cancer research, MELK has gained attention due to its overexpression in various malignancies, such as breast, lung, prostate, and glioblastoma. Studies suggest it promotes tumorigenesis by enhancing cancer cell survival, stemness, and resistance to chemotherapy or radiation. MELK interacts with key oncogenic pathways, including Wnt/β-catenin and Notch signaling, and regulates substrates like c-JUN and PPARγ to drive proliferation. Its role in maintaining cancer stem cells (CSCs) makes it a potential therapeutic target, as CSCs are implicated in tumor recurrence and metastasis.
Recombinant MELK proteins are engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, bioactive kinase for *in vitro* studies. These proteins enable mechanistic exploration of MELK's enzymatic activity, substrate interactions, and inhibition assays. Researchers use them to screen small-molecule inhibitors or validate MELK's functional domains. Despite promising preclinical data, MELK's essentiality in normal cells and conflicting reports on its cancer-specific roles warrant further investigation. Current efforts focus on clarifying its context-dependent functions and optimizing MELK-targeted therapies.
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