Please use this identifier to cite or link to this item:
|Title:||Neutralizing chimeric mouse-human antibodies against Burkholderia pseudomallei protease: Expression, purification and characterization|
|Authors:||Chan, S.-W. |
Recombinant monoclonal antibodies
|Source:||Chan, S.-W., Ong, G.-I., Nathan, S. (2004-09). Neutralizing chimeric mouse-human antibodies against Burkholderia pseudomallei protease: Expression, purification and characterization. Journal of Biochemistry and Molecular Biology 37 (5) : 556-564. ScholarBank@NUS Repository.|
|Abstract:||A recombinant Fab monoclonal antibody (Fab) C37, previously obtained by phage display and biopanning of a random antibody fragment library against Burkholderia pseudomallei protease, was expressed in different strains of Escherichia coli. E. coli strain HB2151 was deemed a more suitable host for Fab expression than other E. coli strains when grown in media supplemented with 0.2% glycerol. The expressed Fab fragment was purified by affinity chromatography on a Protein G-Sepharose column, and the specificity of the recombinant Fab C37 towards B. pseudomallei protease was proven by Western blotting, enzyme-linked immunosorbent assay (ELISA) and by proteolytic activity neutralization. In addition, polyclonal antibodies against B. pseudomallei protease were produced in rabbits immunized with the protease. These were isolated from high titer serum by affinity chromatography on recombinant-Protein A-Sepharose. Purified polyclonal antibody specificity towards B. pseudomallei protease was proven by Western blotting and ELISA. © KSBMB & Springer-Verlag 2004.|
|Source Title:||Journal of Biochemistry and Molecular Biology|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 14, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.