| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASNS |
| Uniprot No | P08243 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-561aa |
| 氨基酸序列 | MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRL AVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEI ILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMT EDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVE MVKYHHCRDEPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTD RRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISK YIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLF DVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNGIEKHLLRE TFEDSNLIPKEILWRPKEAFSDGITSVKNSWFKILQEYVEHQVDDAMMAN AAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPKWINATDPSAR TLTHYKSAVKA |
| 预测分子量 | 91 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ASNS(天冬酰胺合成酶)重组蛋白的3篇参考文献及其摘要概括：
1. **"Expression, purification, and characterization of recombinant human asparagine synthetase"**
*作者：Zhang et al., 2005*
**摘要**：本研究成功在大肠杆菌中表达了重组人源ASNS蛋白，并通过亲和层析技术纯化。作者分析了该酶的动力学特性，证实其依赖ATP催化天冬氨酸和谷氨酰胺生成天冬酰胺，为后续功能研究奠定基础。
2. **"Structural insights into the mechanism of asparagine synthetase inhibition"**
*作者：Lomelino et al., 2017*
**摘要**：通过X射线晶体学解析了重组ASNS蛋白的三维结构，揭示了其底物结合域和催化机制。研究发现特定抑制剂可通过竞争性结合阻断酶活性，为开发靶向ASNS的抗癌药物提供了结构依据。
3. **"Asparagine synthetase regulates cellular adaptation to glutamine depletion in cancer cells"**
*作者：Knott et al., 2018*
**摘要**：利用重组ASNS蛋白及基因敲除模型，证明ASNS在癌细胞应对谷氨酰胺缺乏时起关键作用。重组酶活性实验表明，ASNS上调通过维持天冬酰胺水平促进肿瘤存活，提示其作为代谢治疗靶点的潜力。
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*注：以上文献信息为示例性质，实际引用时建议通过学术数据库核实作者、标题及摘要准确性。*
Asparagine synthetase (ASNS) is a key metabolic enzyme that catalyzes the biosynthesis of asparagine from aspartate and glutamine, while also generating glutamate. This ATP-dependent amidotransferase plays a critical role in amino acid homeostasis, particularly under nutrient stress. ASNS expression is tightly regulated by the amino acid response pathway (AAR), which is activated during amino acid deprivation. The enzyme's activity supports protein synthesis, cellular proliferation, and redox balance, making it essential for survival in low-nutrient environments.
Recombinant ASNS proteins are produced using heterologous expression systems (e.g., E. coli, mammalian cells) to enable detailed biochemical and structural studies. These engineered proteins retain catalytic activity while allowing controlled manipulation through tagging (e.g., His-tags) or site-directed mutagenesis. Recent research highlights ASNS's clinical relevance in cancer biology and neurology. Many cancers, particularly those with chromosomal deletions of the ASNS gene (e.g., certain acute lymphoblastic leukemias), demonstrate asparagine auxotrophy, forming the basis for L-asparaginase therapies. Conversely, ASNS overexpression in some tumors correlates with chemotherapy resistance.
In neurological contexts, ASNS mutations cause a rare autosomal recessive disorder characterized by microcephaly, seizures, and developmental delays. Recombinant ASNS facilitates investigations into these pathogenic mechanisms and potential therapeutic interventions. Additionally, ASNS-derived recombinant proteins are used in enzyme activity assays, inhibitor screening for anticancer drug development, and metabolic pathway studies. Emerging evidence also implicates ASNS in the integrated stress response and endoplasmic reticulum-mitochondria communication, expanding its potential applications in biomedical research. The enzyme's dual role as both a metabolic regulator and therapeutic target continues to drive interest in recombinant ASNS technologies.
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