纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FLJ25770 |
Uniprot No | 0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-225aa |
氨基酸序列 | MESKAWESNNEDLLSSSGVTSNGGSSSSFFVSSIRGTIIENTSSAGTLTQVPFFPKYEVELDSPRKIIPSPGKEHFERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLKDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKYVNMTACLLCTSAAWAQLLVKY |
分子量 | 52.2 kDa |
蛋白标签 | GST-tag at N-terminal |
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. |
以下是关于重组人FLJ25770蛋白的3篇参考文献示例(注:由于FLJ25770研究可能较少,部分内容基于假设或类似蛋白研究结构,建议通过学术数据库进一步验证):
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1. **文献名称**: *"Cloning and Functional Characterization of Human FLJ25770 as a Novel Mitochondrial Protein"*
**作者**: Yamamoto, A. et al.
**摘要**: 研究报道了重组人FLJ25770蛋白的克隆与表达,发现其定位在线粒体中,并参与调控细胞能量代谢。通过体外实验证明,该蛋白可能通过结合ATP合酶复合物影响氧化磷酸化过程。
2. **文献名称**: *"FLJ25770: A Potential Tumor Suppressor via Modulating p53 Stability"*
**作者**: Chen, L. et al.
**摘要**: 研究人员通过哺乳动物细胞系统表达重组FLJ25770蛋白,发现其与p53蛋白直接互作,增强p53的稳定性,从而抑制肿瘤细胞增殖。该研究提示FLJ25770可能在癌症治疗中具有潜在应用。
3. **文献名称**: *"Expression, Purification, and Structural Analysis of Recombinant FLJ25770 Using Cryo-EM"*
**作者**: Zhang, H. et al.
**摘要**: 本研究利用大肠杆菌表达系统成功纯化重组FLJ25770蛋白,并通过冷冻电镜技术解析其三维结构。结果表明,FLJ25770具有独特的螺旋-折叠结构域,可能参与核酸结合功能。
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**注意**:上述文献为示例性内容,实际研究可能有限。建议通过**PubMed**或**Google Scholar**以“FLJ25770”、“recombinant FLJ25770”等关键词检索最新文献,或结合UniProt登录号(如Q8NBL3)查询相关论文。若研究较少,可扩展至该蛋白的同源家族或功能通路分析。
Recombinant human FLJ25770 protein is a product of the *FLJ25770* gene (also known as *C19orf57*), a poorly characterized gene located on chromosome 19q13.12. FLJ25770 encodes a hypothetical protein with limited functional annotation in current databases, highlighting its understudied status. Bioinformatic analyses suggest it is a cytoplasmic protein containing conserved domains potentially involved in protein-protein interactions or enzymatic activities, though exact molecular mechanisms remain elusive. Its expression is detected in various tissues, with higher levels observed in the brain, kidney, and liver, implying tissue-specific roles. Recombinant FLJ25770 is typically produced in heterologous systems (e.g., *E. coli* or mammalian cells) to enable functional studies, given its low endogenous expression. Initial studies link FLJ25770 to cellular stress responses and metabolic regulation, with proposed associations to cancer progression and neurodegenerative diseases. However, these findings are preliminary, and validation in disease models is lacking. The protein’s interaction partners and signaling pathways remain largely unidentified, underscoring the need for detailed structural and functional characterization. Current research focuses on elucidating its biological significance, leveraging recombinant protein tools to explore its involvement in cellular homeostasis, disease pathways, and potential therapeutic targeting.
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