To carry out the secretive expression of human 67kD laminin receptor (67LR),recombinant expression plasmid pPIC9K-67LR was constructed by inserting of 67LR cDNA into yeast expression vector pPIC9K. The 67LR protein was expressed in Pichia pastoris after induced by methanol,and about 12.56mg electrophoresis purity 67LR could be obtained after the purification of 1L culture using affinity chromatograph column. In vitro competitive binding assay showed that target protein has an excellent biological activity. The successful expression of 67LR has placed a solid foundation for the research on structure and functions of 67LR.
连继勤,戴旭芳,甘立霞,何凤田. 人67kD层粘连蛋白受体在毕赤酵母中的表达及活性分析[J]. Chinese Journal of Biotechnology, 2007, 23(4):
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