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OJVRTM
Online Journal of
Veterinary Research©
Volume 17 (1): 28-33, 2013. Extensively Redacted 2017.
Expression of constant region
of bovine IgG1 heavy chain in E. coli
Abdolhossein Jangeran
Nejad1, Atefeh Ashtary1, Masoud Ghorbanpoor2 and Masoudreza
Seyfi Abad Shapouri2
1DVM, 2DVM, PhD, Department of Pathobiology,
School of Veterinary Medicine, Shahid Chamran University, Ahvaz, Iran
ABSTRACT
Nejad AJ, Ashtary
A, Ghorbanpoor M, Seyfi M, Shapouri A., Expression of the constant region of bovine
IgG1 heavy chain in E. coli, Online J Vet Res., 17 (1): 28-33, 2013.
We describe expression of constant region of bovine IgG1 heavy chain in E. coli for antibody production. Specific primers were used to amplify constant region of G1 chain mRNA by RT-PCR. The resulting
DNA fragment was cloned in pMal-C2X expression plasmid and expressed in TG1 and BL strains
of E. coli. Expression of an expected fusion protein (MBP-G1),
comprising Maltose binding protein (MBP), encoded by the plasmid and the
constant region of G1 chain (CH1-CH3) was confirmed by SDS-PAGE and Western
blot. The protein was found to be insoluble
in BL21(DE3) strain but partially soluble in TG1, when
expressed at room temperature. Our results
suggest that the constant region of bovine IgG1 heavy chain can be expressed as
a partially soluble fusion protein in E. coli. This strategy is simple
and when established, eliminates the time consuming steps of immunoglobulin purification.
Moreover, by this strategy it is possible to express the isotype specific
sequences of immunoglobulins and facilitate the production of isotype specific anti antibodies.
Key Words: Bovine, IgG1,
constant region, expression, E. coli
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