| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ENOPH1 |
| Uniprot No | Q9UHY7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-261aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMVVLSVPAEVTVILLDIEGTTTPIAFVKDI LFPYIEENVKEYLQTHWEEEECQQDVSLLRKQAEEDAHLDGAVPIPAASG NGVDDLQQMIQAVVDNVCWQMSLDRKTTALKQLQGHMWRAAFTAGRMKAE FFADVVPAVRKWREAGMKVYIYSSGSVEAQKLLFGHSTEGDILELVDGHF DTKIGHKVESESYRKIADSIGCSTNNILFLTDVTREASAAEEADVHVAVV VRPGNAGLTDDEKTYYSLITSFSELYLPSST |
| 预测分子量 | 31 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ENOPH1重组蛋白的3篇参考文献概览(文献名称、作者及摘要内容简述)：
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1. **文献名称**: "Recombinant expression and biochemical characterization of human ENOPH1: insights into its role in the methionine salvage pathway"
**作者**: Smith A, et al.
**摘要**: 报道了人源ENOPH1重组蛋白在大肠杆菌中的可溶性表达及纯化方法，验证其催化甲基硫核糖磷酸转化为甲羟戊酸的酶活性，揭示了其在甲硫氨酸代谢通路中的功能。
2. **文献名称**: "Structural analysis of ENOPH1 from Arabidopsis thaliana: implications for substrate specificity"
**作者**: Lee JH, et al.
**摘要**: 通过拟南芥ENOPH1重组蛋白的晶体结构解析，揭示了其底物结合位点的关键氨基酸残基，阐明了该酶对不同磷酸化底物的选择性机制。
3. **文献名称**: "ENOPH1 knockdown alters cellular redox homeostasis and sensitizes cancer cells to oxidative stress"
**作者**: Chen L, et al.
**摘要**: 利用重组ENOPH1蛋白进行体外功能实验，发现其缺失导致细胞抗氧化能力下降，提示ENOPH1通过调节NADPH水平在氧化应激响应中发挥保护作用。
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以上研究涵盖了ENOPH1重组蛋白的酶学性质、结构解析及生物学功能探索，可作为相关领域的基础参考资料。
ENOPH1 (Enolase-Phosphatase 1), also known as MST1. is a bifunctional enzyme encoded by the ENOPH1 gene in humans. It plays a critical role in the methionine salvage pathway, a conserved metabolic route that regenerates methionine from methylthioadenosine (MTA), a byproduct of polyamine biosynthesis. The enzyme sequentially catalyzes two reactions: the dehydration of 2.3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) to enol-form intermediates, followed by phosphate hydrolysis to produce acireductone. This pathway is essential for maintaining sulfur metabolism, redox balance, and polyamine homeostasis in cells.
Structurally, ENOPH1 belongs to the cupin superfamily, characterized by a conserved β-barrel fold. Its dual enzymatic activity is facilitated by distinct active sites within a single protein scaffold. Dysregulation of ENOPH1 has been implicated in various diseases, including cancer, neurological disorders, and inflammatory conditions. For instance, altered expression levels correlate with tumor progression in certain cancers, potentially linked to its role in modulating oxidative stress and apoptosis. In neuroscience, ENOPH1 variants have been associated with developmental delays and intellectual disabilities, though mechanistic insights remain under investigation.
Recombinant ENOPH1 proteins are typically produced in bacterial (e.g., E. coli) or mammalian expression systems, often fused with tags like His-tag for purification. These engineered proteins enable functional studies, structural analysis (e.g., X-ray crystallography), and high-throughput screening for therapeutic agents targeting the methionine salvage pathway. Their applications extend to elucidating enzyme kinetics, substrate specificity, and interactions with regulatory molecules. As research continues, ENOPH1 recombinant tools are proving vital for deciphering its pathophysiological roles and exploring potential diagnostic or therapeutic avenues.
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