首页> 外文期刊>Bioscience, Biotechnology, and Biochemistry >Expression and One-Step Purification of Recombinant Proteins Using an Alternative Episomal Vector for the Expression of N-Tagged Heterologous Proteins in Pichia pastoris
【24h】

Expression and One-Step Purification of Recombinant Proteins Using an Alternative Episomal Vector for the Expression of N-Tagged Heterologous Proteins in Pichia pastoris

机译:使用替代再生载体的重组蛋白的表达和一步纯化用于表达N标记的异源蛋白在Pichia Pastoris中的表达

获取原文
获取原文并翻译 | 示例
           

摘要

Here we report the construction of an alternative episomal vector, pBGP3, which allows the expression of heterologous proteins with N-terminal hexahistidine and myc-epitope tags in Pichia pastoris. To test the usefulness of pBGP3, four cellulases from termites were expressed. Production was confirmed by activity assays and Western blot using anti-c-Myc antibody. Purification was performed by single-step Ni~(2+)-affinity chromatography, which confirmed the efficiency of pBGP3.
机译:在这里,我们报告了替代的重组载体PBGP3的构建,其允许在毕赤酵母中用N-末端六三氨基和Myc-epitope标签表达异源蛋白。 为了测试PBGP3的有用性,表达了来自白蚁的四种纤维素酶。 使用抗C-MYC抗体的活性测定和Western印迹确认生产。 通过单步Ni〜(2 +) - 亲和色谱法进行纯化,证实了PBGP3的效率。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号