纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MULK |
Uniprot No | Q53H12 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-422 aa |
活性数据 | MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ |
分子量 | 47.1 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | 0 |
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. |
以下为模拟的参考示例(若"MULK蛋白"名称有误或需具体领域文献,请进一步核实):
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1. **文献名称**: *Expression and Purification of Recombinant Human MULK Protein in E. coli*
**作者**: Zhang L., et al.
**摘要**: 研究利用大肠杆菌系统高效表达重组人MULK蛋白,通过优化诱导条件和纯化步骤(如His标签亲和层析),获得高纯度蛋白,并验证其体外酶活性。
2. **文献名称**: *Structural Analysis of MULK Protein and Its Role in Cellular Signaling*
**作者**: Gupta R., et al.
**摘要**: 采用X射线晶体学解析MULK蛋白三维结构,发现其催化结构域与MAPK家族相似;功能实验表明MULK通过磷酸化下游靶点参与细胞增殖调控。
3. **文献名称**: *MULK as a Potential Therapeutic Target in Cancer: Recombinant Protein-based Drug Screening*
**作者**: Kim S., et al.
**摘要**: 利用重组MULK蛋白进行高通量药物筛选,发现小分子抑制剂X可显著降低肿瘤细胞中MULK活性,提示其在癌症靶向治疗中的潜力。
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**提示**:以上为示例文献,实际研究中建议通过 **PubMed/Google Scholar** 检索准确关键词(如“recombinant MULK protein”、“human MULK function”),并确认蛋白名称拼写(如是否应为MULK、MUL1、MAPK等)。
Recombinant human MULK (Multifunctional Ubiquitin-like protein Kinase) is a genetically engineered protein produced using recombinant DNA technology, designed to mimic the native human MULK involved in critical cellular processes. MULK belongs to the ubiquitin-like kinase family, playing dual roles in ubiquitination and phosphorylation pathways, which are essential for protein degradation, signal transduction, and stress response regulation. Its recombinant form is typically expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian HEK293 cells) to ensure proper folding and post-translational modifications, depending on downstream applications.
The production of recombinant MULK enables scalable, high-purity protein yields for biochemical and biomedical research. It serves as a vital tool for studying its involvement in cellular homeostasis, autophagy, and disease mechanisms, such as cancer progression and neurodegenerative disorders. Researchers utilize recombinant MULK to investigate substrate interactions, enzyme kinetics, and regulatory networks in controlled experimental settings. Additionally, it has potential therapeutic applications, including targeted drug development and gene therapy. However, challenges persist in optimizing expression systems to maintain functional activity and mimic native conformational states. Ongoing studies aim to refine production protocols and expand its utility in structural biology (e.g., crystallography) and high-throughput screening platforms. Recombinant MULK thus represents a cornerstone protein for advancing both fundamental and translational research in molecular biology.
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