Transient expression and purification of chimeric heavy chain antibodies.
Monoclonal 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 approximately 80 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.
Zhang
Jianbing
J
Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Drive, Ottawa, ON K1A0R6, Canada. jianbing.zhang@nrc.gc.ca
Liu
Xin
X
Bell
Andrea
A
To
Rebecca
R
Baral
Toya Nath
TN
Azizi
Ali
A
Li
Jianjun
J
Cass
Brian
B
Durocher
Yves
Y
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis* / Q000235:genetics; D002161:Camelids, New World; D045744:Cell Line, Tumor; D015870:Gene Expression; D006031:Glycosylation; D006801:Humans; D007143:Immunoglobulin Heavy Chains / Q000096:biosynthesis* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics
D000911:Antibodies, Monoclonal; D007143:Immunoglobulin Heavy Chains; D011993:Recombinant Fusion Proteins