Abstract
Single chain Fv-170 (scFv-170) was constructed and expressed in the methylotrophic yeast Pichia pastoris. Recombinant scFv-170 was highly expressed in an aF-signal based expression vector and sufficiently secreted from the cells in protein-free medium. Further, the scFv-170 maintained the intrinsic binding activity and exhibited the same binding pattern as that of MAb 170H.82, as measured in competitive radioimmunoassay (RIA) experiments.
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