期刊
PROTEIN SCIENCE
卷 17, 期 12, 页码 2120-2126出版社
WILEY
DOI: 10.1110/ps.038299.108
关键词
affinity tag; purification; monoclonal antibody; X-ray crystallography; Fab fragment; scFv fragment; F-spondin; reelin
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT)
Biologically important human proteins often require mammalian cell expression for structural studies, presenting technical and economical problems in the production/purification processes. We introduce a novel affinity peptide tagging system that uses a low affinity anti-peptide monoclonal antibody. Concatenation of the short recognition sequence enabled the successful engineering of an 18-residue affinity tag with ideal solution binding kinetics, providing a low-cost purification means when combined with nondenaturing elution by water-miscible organic solvents. Three-dimensional information provides a firm structural basis for the antibody-peptide interaction, opening opportunities for further improvements/modifications.
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