纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PSAT1 |
Uniprot No | Q99K85 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-370aa |
氨基酸序列 | MEATKQVVNFGPGPAKLPHSVLLEIQKQLLDYRGLGISVLEMSHRSSDFAKIIGNTENLVRELLAVPNNYKVIFVQGGGSGQFSAVPLNLIGLKAGRSADYVVTGAWSAKAAEEAKKFGTVNIVHPKLGSYTKIPDPSTWNLNPDASYVYFCANETVHGVEFDFVPDVKGAVLVCDMSSNFLSRPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFSLRECPSVLDYKVQAGNNSLYNTPPCFSIYVMGMVLEWIKNNGGAAAMEKLSSIKSQMIYEIIDNSQGFYVCPVERQNRSRMNIPFRIGNAKGDEALEKRFLDKAVELNMISLKGHRSVGGIRASLYNAVTTEDVEKLAAFMKNFLEMHQL |
预测分子量 | 56.5kDa |
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3条模拟生成的关于PSAT1重组蛋白的参考文献示例:
1. **文献名称**:重组人PSAT1蛋白在大肠杆菌中的高效表达及酶活性研究
**作者**:李明等
**摘要**:本研究成功构建了pET28a-PSAT1重组质粒,通过大肠杆菌表达系统实现可溶性表达,并利用镍柱纯化获得高纯度蛋白。酶动力学实验表明该重组蛋白具有磷酸丝氨酸氨基转移酶活性,为后续肿瘤代谢研究提供工具。
2. **文献名称**:PSAT1重组蛋白在非小细胞肺癌细胞代谢调控中的作用机制
**作者**:Chen Y, Wang X
**摘要**:通过体外表达纯化的PSAT1重组蛋白处理肺癌细胞,发现其显著增强丝氨酸合成通路活性,促进细胞增殖。蛋白质互作实验揭示PSAT1与PHGDH形成复合物,协同调控肿瘤代谢重编程。
3. **文献名称**:晶体结构解析揭示PSAT1催化机制及其抑制剂筛选
**作者**:Zhang R et al.
**摘要**:利用昆虫细胞系统表达并纯化人源PSAT1重组蛋白,通过X射线衍射获得2.1Å分辨率晶体结构。基于结构筛选获得小分子抑制剂,在体外实验中有效阻断酶活性,为靶向治疗提供新策略。
注:以上为模拟文献,实际研究需通过PubMed/Google Scholar检索关键词"PSAT1 recombinant protein"、"phosphoserine aminotransferase expression"等获取真实文献。
**Background of PSAT1 Recombinant Protein**
Phosphoserine Aminotransferase 1 (PSAT1) is a key enzyme in the serine biosynthesis pathway, catalyzing the conversion of 3-phosphohydroxypyruvate to 3-phosphoserine using glutamate as an amino donor. This metabolic pathway is critical for producing serine, a non-essential amino acid vital for cellular processes such as nucleotide synthesis, redox homeostasis, and methylation reactions. PSAT1’s role in serine metabolism has drawn significant attention due to its implications in cancer biology, neurological disorders, and developmental defects. Overexpression of PSAT1 is observed in various cancers, where it supports tumor proliferation by fueling serine-dependent anabolic pathways, making it a potential therapeutic target.
Recombinant PSAT1 protein is engineered through molecular cloning, typically expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. The purified protein retains enzymatic activity, enabling functional studies to dissect its kinetic properties, substrate specificity, and regulatory mechanisms. Researchers utilize PSAT1 recombinant protein to investigate its structural dynamics via X-ray crystallography or cryo-EM, unraveling insights into active-site interactions and allosteric regulation.
Additionally, this tool aids in drug discovery, facilitating high-throughput screens for inhibitors that could disrupt serine metabolism in cancers. It also serves as an antigen for antibody development, supporting diagnostic and therapeutic research. Studies linking PSAT1 mutations to neurological conditions, such as serine deficiency disorders, further underscore its biomedical relevance. By providing a reliable, scalable source of functional PSAT1. recombinant protein technology accelerates mechanistic and translational research, bridging gaps between metabolic dysregulation and disease pathology.
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