title: Recombinant protein expression in the baculovirus-infected insect cell system.
abstract: Over the last two decades, the use of eukaryotic cells for expression of recombinant proteins has become the preferred choice for many applications. This is primarily the case when posttranslational modifications and correct disulfide-bond formation are necessary for protein folding and activity. Among the eukaryotic expression systems, the baculovirus-infected insect cell platform has gained particular attention, resulting in the development and implementation of multiple strategies for protein expression. Here, we present baculovirus-infected insect cells as an efficient expression system for eukaryotic proteins. We demonstrate a simplified and a shortened procedure for recombinant virus production that is sufficient for large-scale production of proteins in insect cells.
authors.affiliation: Israel Structural Proteomics Center, Faculty of Biochemistry, Weizmann Institute of Science, Meyer Building, Rehovot, Israel. tamar.unger@weizmann.ac.il
authors.forename: Tamar
authors.initials: T
authors.lastname: Unger
authors.forename: Yoav
authors.initials: Y
authors.lastname: Peleg
mesh_terms: D000818:Animals; D016367:Baculoviridae / Q000235:genetics* / Q000502:physiology*; D002460:Cell Line; D003001:Cloning, Molecular; D004274:DNA, Recombinant / Q000235:genetics; D015870:Gene Expression; D005822:Genetic Vectors / Q000235:genetics; D042541:Intracellular Space / Q000378:metabolism; D008863:Microspheres; D009532:Nickel / Q000737:chemistry; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D018411:Spodoptera / Q000166:cytology* / Q000235:genetics / Q000821:virology*; D013535:Suspensions; D013997:Time Factors; D014162:Transfection
chemical_list: D004274:DNA, Recombinant; D011994:Recombinant Proteins; D013535:Suspensions; D009532:Nickel