Expression and solubilization of a recombinant human neurokinin-1 receptor in insect cells.
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.
Mazina
K E
KE
Department of Molecular Pharmacology and Biochemistry, Merck Research Laboratories, Rahway, NJ 07065.
Strader
C D
CD
Fong
T M
TM
D000818:Animals; D001483:Base Sequence; D002793:Cholic Acids; D003001:Cloning, Molecular; D003902:Detergents; D005822:Genetic Vectors; D006801:Humans; D007313:Insecta / Q000166:cytology / Q000378:metabolism*; D008969:Molecular Sequence Data; D017924:Nucleopolyhedroviruses / Q000235:genetics*; D018040:Receptors, Neurokinin-1 / Q000096:biosynthesis / Q000235:genetics*; D011994:Recombinant Proteins / Q000096:biosynthesis; D012995:Solubility
D002793:Cholic Acids; D003902:Detergents; D018040:Receptors, Neurokinin-1; D011994:Recombinant Proteins; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate