{"entity": "publication", "iuid": "b10c161af6214fa9975469a2d0c9fdd1", "timestamp": "2026-09-08T10:05:27.738Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b10c161af6214fa9975469a2d0c9fdd1.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b10c161af6214fa9975469a2d0c9fdd1"}}, "title": "Selection of Affibody Affinity Proteins from Phagemid Libraries.", "authors": [{"family": "Giang", "given": "Kim Anh", "initials": "KA"}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5"}, {"family": "Nilvebrant", "given": "Johan", "initials": "J"}], "type": "journal article", "published": "2023-09-08", "journal": {"title": "Methods in molecular biology (Clifton, N.J.)", "issn": "1940-6029", "volume": "2702", "pages": "373-392", "issn-l": "1064-3745"}, "abstract": "Herein, we describe a general protocol for the selection of target-binding affinity protein molecules from a phagemid-encoded library. The protocol is based on our experience with phage display selections of non-immunoglobulin affibody affinity proteins but can in principle be applied to perform biopanning experiments from any phage-displayed affinity protein library available in a similar phagemid vector. The procedure begins with an amplification of the library from frozen bacterial glycerol stocks via cultivation and helper phage superinfection, followed by a step-by-step instruction of target protein preparation, selection cycles, and post-selection analyses. The described procedures in this standard protocol are relatively conservative and rely on ordinary reagents and equipment available in most molecular biology laboratories.", "doi": "10.1007/978-1-0716-3381-6_19", "pmid": "37679630", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T06:36:30.692Z", "modified": "2026-08-20T06:36:30.747Z"}