Single chain antibody with cleavable linker

Abstract

Disclosed are antibodies and methods for making antibodies with desired glycosylation and efficient production. Host cells transformed with a nucleic acid encoding a fusion protein comprising a signal sequence, light and heavy immunoglobulin chains, each comprising a variable region and a constant region and separated by a spacer peptide comprising at least one proteolytic cleavage site are cultured to express the nucleic acids and are cleaved by appropriate proteases to produce antibodies.

Description

[0001] Cross References to Related Applications [0001] This application is a non-provisional application of 60 / 675,218 filed April 26, 2005, which is hereby incorporated by reference in its entirety for all and all purposes. Background technique [0002] Although mammalian cell systems have been successfully used to manufacture antibodies for medical use, their development is expensive and there is currently insufficient production capacity to meet the anticipated future demand for antibodies. Cellular systems for expressing proteins from lower eukaryotes and bacteria are cheaper and easier to work with, but involve additional difficulties in making antibodies. In these cell types, most previous work has been limited to the expression of antibody fragments rather than intact antibodies due to poor folding and / or yields of intact antibodies in these systems (see, e.g., Better et al., Science 240, 1041 -1043(1988)). However, antibody fragments are only useful if binding of t...

AI Technical Summary

Problems solved by technology

These molecules include a light chain variable region separated from a heavy chain variable region by a spacer peptide, but typically lack part, often all, of the constant region

Images