Isolation of a new human scFv antibody recognizing a cell surface binding site to CEACAM1. Large yield production, purification and characterization in E. coli expression system.

Protein Expression and Purification(2014)

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摘要
•Optimal purification strategy for a high yield production of scFv anti-CEACAM1.•scFv shows a high binding reactivity in ELISA, IF an flow cytometry studies.•scFv is a naturally occurring mixture of monomer and dimer fully characterized.•scFv at 37°C shows the dimer behaves as a reservoir converting slowly into monomer.•scFv at 37°C has a t½ for binding CEACAM1 of 12h as demonstrated by ELISA.
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关键词
CEACAM1,Single chain variable fragment (scFv),Purification,Dimer,Aggregates,Thermal stability
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