| Literature DB >> 3096719 |
B Löwenadler, B Nilsson, L Abrahmsén, T Moks, L Ljungqvist, E Holmgren, S Paleus, S Josephson, L Philipson, M Uhlén.
Abstract
The gene for Staphylococcal protein A was fused to the coding sequence of bacterial beta-galactosidase, alkaline phosphatase and human insulin-like growth factor I (IGF-I). The fusion proteins, expressed in bacteria, were purified by affinity chromatography on IgG-Sepharose and antibodies were raised in rabbits. All three fusion proteins elicited specific antibodies against both the inserted protein sequences and the protein A moiety. In the case of IGF-I, the protein A moiety in the fusion protein may act as an adjuvant since native IGF-I alone is a poor immunogen. The results suggest that the protein A fusion system can be used for efficient antibody production against peptides or proteins expressed from cloned or synthetic genes. To facilitate such gene fusions a set of optimized vectors have been constructed.Entities:
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Year: 1986 PMID: 3096719 PMCID: PMC1167125 DOI: 10.1002/j.1460-2075.1986.tb04509.x
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598