本文選題：Stathmin + 磷酸化��； 參考：《新鄉(xiāng)醫(yī)學院學報》2016年11期

【摘要】：目的構建Stathmin基因磷酸化位點突變載體,為Stathmin磷酸化功能的進一步研究提供實驗基礎。方法通過設計磷酸化位點突變引物,運用聚合酶鏈反應分別將人Stathmin基因片段中4個絲氨酸磷酸化位點Ser16、Ser25、Ser38、Ser63突變?yōu)椴荒苓M行磷酸化的丙氨酸,插入真核表達載體pc DNA3.1,分別構建重組載體pc DNA3.1/Stathmin Ser16/A、pc DNA3.1/Stathmin Ser25/A、pc DNA3.1/Stathmin Ser38/A、pc DNA3.1/Stathmin Ser63/A,并進行基因測序鑒定。結果基因測序鑒定重組載體結果表明,分別將Stathmin基因中Ser16、Ser25、Ser38、Ser63突變?yōu)楸彼�。結論成功構建了Stathmin磷酸化位點突變載體,為進一步研究Stathmin磷酸化的作用機制和功能奠定了基礎。
[Abstract]:Objective to construct Stathmin gene phosphorylation site mutant vector and provide experimental basis for further study of Stathmin phosphorylation function. Methods four serine phosphorylation sites Ser16 Ser25Ser25Ser38 Ser63 in human Stathmin gene fragments were mutated to alanine which could not be phosphorylated by polymerase chain reaction (PCR). The eukaryotic expression vector pcDNA3.1 was inserted into the eukaryotic expression vector, and the recombinant vector PC DNA3.1/Stathmin Ser16% APC DNA3.1/Stathmin Ser25% APC DNA3.1/Stathmin Ser38% APC DNA3.1/Stathmin Ser63 / A was constructed, and the gene was sequenced. Results the recombinant vector was identified by gene sequencing. The results showed that the Ser16Con Ser25Ser25Ser38 Ser63 gene was mutated to alanine in the Stathmin gene. Conclusion the mutant vector of Stathmin phosphorylation site was successfully constructed, which laid a foundation for further study on the mechanism and function of Stathmin phosphorylation.
【作者單位】： 第四軍醫(yī)大學唐都醫(yī)院臨床實驗與檢驗科;
【基金】：國家自然科學基金資助項目(編號:81372836)
【分類號】：R73-36
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本文編號：1801060