Mouse Dual Ig Domain Containing Cell Adhesion Molecule Protein Expression and Purification Using the Baculovirus Expression Vector System.
10.4167/jbv.2010.40.3.123
- Author:
Seung Won PARK
1
;
Ji Hyun CHOI
;
Tae Won GOO
;
Seong Ryul KIM
;
Gwang Gill LEE
;
Seok Woo KANG
Author Information
1. Department of Agricultural Biology, National Academy of Agricultural Science, Rural Development Administration, Suwon, Korea. microsw@korea.kr
- Publication Type:Original Article
- Keywords:
Baculovirus expression vector system;
Dual Ig domain containing cell adhesion molecule;
Recombinant protein
- MeSH:
Amino Acids;
Animals;
Baculoviridae;
Cell Adhesion;
Cytoplasm;
Insects;
Mice;
Protein Sorting Signals;
Proteins;
Recombinant Proteins;
Sf9 Cells
- From:Journal of Bacteriology and Virology
2010;40(3):123-130
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
A baculovirus expression vector system (BEVS) is used routinely to produce recombinant proteins in the milligram scale. Dual Ig domain containing cell adhesion molecule (DICAM) belongs to the type I class of transmembrane proteins. It consists of a signal peptide, two V-type Ig domains in the extracellular region, and a short cytoplasmic tail of 442 amino acids. To purify the recombinant DICAM protein from cells overexpressing the mouse full-length DICAM gene, recombinant baculovirus is infected and recovered in the Sf9 cells. As a result, mouse DICAM protein was efficiently expressed and extracted from the insect cells using the BEVS. This recombinant protein can be used in further studies for functional test of DICAM protein in the cells.
