Transient expression and purification of chimeric heavy chain antibodies

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DOIResolve DOI: http://doi.org/10.1016/j.pep.2008.10.011
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TypeArticle
Journal titleProtein Expression and Purification
Volume65
Issue1
Pages7782; # of pages: 6
Subject(Chimeric) Heavy chain antibody; Antibody expression; Single domain antibody; Transient expression; Animal; bio; Human; In Vitro; Protein; Proteins; Glycosylation; Animal; Animals; Antibodies; Antibodies,Monoclonal; antibody; assay; biosynthesis; Camelids,New World; Canada; Cell Line,Tumor; CHAIN; CHAINS; DOMAIN; EFFICIENT; EXPRESSION; Gene Expression; genetics; Human; Humans; Immunoglobulin Heavy Chains; MONOCLONAL-ANTIBODIES; MONOCLONAL-ANTIBODY; Recombinant Fusion Proteins; SYSTEM
AbstractMonoclonal antibodies have been successfully engineered as approved therapeutics. However, their large size is considered a major factor preventing them from having a more efficient tissue penetration. As the first step to establish a possibly more efficient antibody platform, we present here transient expression, purification and characterization of six chimeric heavy chain antibodies (cHCAbs), or fusion of camelid single domain antibodies (sdAbs) to human fragment crystallizable (Fc). All six HCAbs have a MW of not, vert, similar80 kDa, expressed well in a HEK293 expression system and have G0, G1 and G2 types of glycosylation. The transient expression also provided a very fast way to generate high milligram to low gram amount of proteins for in vitro assays and preliminary animal studies.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences; NRC Biotechnology Research Institute
Peer reviewedYes
NRC numberZHANG2009A
47831
NPARC number15329265
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Record identifierf0c1afa1-4615-44af-860d-1c805cbb1943
Record created2010-05-21
Record modified2016-05-09
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