PubMed:24518284 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/24518284","sourcedb":"PubMed","sourceid":"24518284","source_url":"https://www.ncbi.nlm.nih.gov/pubmed/24518284","text":"Production of scFv-conjugated affinity silk film and its application to a novel enzyme-linked immunosorbent assay.\nBombyx mori (silkworm) silk proteins have been utilized as unique biomaterials for various medical applications. To develop a novel affinity silk material, we generated a transgenic silkworm that spins silk protein containing the fibroin L-chain linked with the single-chain variable fragment (scFv) as a fusion protein. Previously, the scFv-conjugated \"affinity\" silk powder specifically immunoprecipitated its target protein, Wiskott-Aldrich syndrome protein. To expand the applicability of affinity silk materials, we processed the scFv-conjugated silk protein into a thin film by dissolving it in lithium bromide, then drying it in the wells of 96-well plates. Enzyme-linked immunosorbent assay demonstrated specific detection of Wiskott-Aldrich syndrome protein, both as a recombinant protein and in its native form extracted from mouse macrophages. These findings suggest that this scFv-conjugated silk film serves as the basis for an alternative immunodetection 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