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观察Trim6是否与接头蛋白TAB2存在蛋白相互作用,进而影响TAB2介导的NF-κB荧光素酶报告基因的活化。在HEK293T细胞中共转染Trim6及TAB2的真核表达载体,免疫共沉淀法验证两者是否存在蛋白相互作用;用蛋白印迹法验证Trim6是否能降解TAB2;同时用双荧光素酶报告基因系统检测Trim6是否影响TAB2介导的NF-κB荧光素酶报告基因活化。免疫共沉淀结果证明Trim6与TAB2存在蛋白相互作用;蛋白印迹检测发现Trim6能显著降解TAB2,进而明显抑制TAB2介导的NFκB荧光素酶报告基因的活化。
To investigate whether Trim6 interacts with the TAB2 adapter protein, thereby affecting TAB2-mediated NF-κB luciferase reporter gene activation. The eukaryotic expression vectors of Trim6 and TAB2 were co-transfected into HEK293T cells, and the co-immunoprecipitation assay was used to verify the interaction of Trim6 and TAB2. Western blotting was performed to determine whether Trim6 could degrade TAB2. Simultaneously, Trim6 reporter gene system was used to detect Trim6 and TAB2. Affects TAB2-mediated NF-κB luciferase reporter gene activation. Coimmunoprecipitation results showed that there was protein interaction between Trim6 and TAB2. Western blotting showed that Trim6 could significantly degrade TAB2, and then significantly inhibited TAB2-mediated NFκB luciferase reporter gene activation.