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Curr Opin Struct Biol. 2014 Jun;26:39-43. doi: 10.1016/j.sbi.2014.03.006. Epub 2014 Apr 12.

Better and faster: improvements and optimization for mammalian recombinant protein production.

Author information

1
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, United States.
2
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, United States. Electronic address: James.love@einstein.yu.edu.

Abstract

Thanks to numerous technological advances, the production of recombinant proteins in mammalian cell lines has become an increasingly routine task that is no longer viewed as a heroic enterprise. While production in prokaryotic or lower eukaryotic systems may be more rapid and economical, the advantages of producing large amounts of protein that closely resembles the native form is often advantageous and may be essential for the realization of functionally active material for biological studies or biopharmaceuticals. The correct folding, processing and post-translational modifications conferred by expression in a mammalian cell is relevant to all classes of proteins, including cytoplasmic, secreted or integral membrane proteins. Therefore considerable efforts have focused on the development of growth media, cell lines, transformation methods and selection techniques that enable the production of grams of functional protein in weeks, rather than months. This review will focus on a plethora of methods that are broadly applicable to the high yield production of any class of protein (cytoplasmic, secreted or integral membrane) from mammalian cells.

PMID:
24721463
PMCID:
PMC4766836
DOI:
10.1016/j.sbi.2014.03.006
[Indexed for MEDLINE]
Free PMC Article

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