Expression and solubilization of a recombinant human neurokinin-1 receptor in insect cells.

K E Mazina, C D Strader, T M Fong
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引用次数: 18

Abstract

The human neurokinin-1 receptor has been expressed in insect cells using a recombinant baculovirus. The expression level is about 10 times higher than that obtained in mammalian cells. The recombinant receptor was solubilized with CHAPS, and a PEG precipitation procedure was shown to be effective in regaining high affinity substance P binding. This system should allow large scale purification of the human neurokinin-1 receptor.

重组人神经激肽-1受体在昆虫细胞中的表达与溶解。
利用重组杆状病毒在昆虫细胞中表达了人神经激肽-1受体。其表达量是在哺乳动物细胞中表达量的10倍左右。重组受体用CHAPS溶解,聚乙二醇沉淀程序被证明可以有效地恢复高亲和力的P物质结合。该系统应该允许大规模纯化人类神经激肽-1受体。
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