Expression of chicken interleukin-2 in insect cells.
Full-length chicken interleukin-2 (ChIL-2) protein was successfully expressed using the recombinant baculovirus/Sf9 insect cell system. The expressed protein was soluble and reached approximately 12 microg/ml. Similarly to native ChIL-2, baculovirus expressed ChIL-2 revealed two main bands corresponding to molecular masses of 22 and 20 kD as detected by SDS-PAGE and Western blot. Treatment of the expressed protein with N-endoglycosidase F for 2 h caused the complete disappearance of the 22 kD band, while the 20 kD band (which is close to the molecular weight predicted from the cloned cDNA sequence) remained unchanged. Together with results on native ChIL-2, it can be concluded that ChIL-2 is an N-glycosylated protein.
Cao
Min-Jie
MJ
College of Biological Engineering, Jimei University, Jimei, Xiamen, 361021, China. caomj@suntar.com
Wu
Guo-Ping
GP
Guo
Chuan
C
Su
Wen-Jin
WJ
D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D002460:Cell Line; D002645:Chickens; D003001:Cloning, Molecular; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D007376:Interleukin-2 / Q000235:genetics*; D011994:Recombinant Proteins / Q000235:genetics; D018411:Spodoptera
D017931:DNA Primers; D007376:Interleukin-2; D011994:Recombinant Proteins