Literature DB >> 29717055

Making Weak Antigens Strong: Modifying Protein Antigens by Denaturation.

Edward A Greenfield, James DeCaprio, Mohan Brahmandam.   

Abstract

Many molecules can be made more immunogenic by denaturation. This treatment will change the structure of many compounds, particularly proteins, and expose new epitopes. In addition, heating will often cause protein antigens to aggregate, and, because aggregated antigens are often more immunogenic, this can increase the antibody response. Either heating alone or heating with sodium dodecyl sulfate (SDS) is the usual treatment. Injecting denatured antigens will be more likely to produce an antibody response against epitopes that are not found on the native antigen. If antibodies against totally denatured proteins are desired, the SDS-heat treatment is normally best. These treatments will generate antibodies that should be particularly good for immunoblots, for screening bacterial expression libraries, and for immunoprecipitation of proteins synthesized during in vitro translations.
© 2018 Cold Spring Harbor Laboratory Press.

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Year:  2018        PMID: 29717055     DOI: 10.1101/pdb.prot099960

Source DB:  PubMed          Journal:  Cold Spring Harb Protoc        ISSN: 1559-6095


  1 in total

1.  Use of recombinant Brucella outer membrane proteins 19, 25, and 31 for serodiagnosis of bovine brucellosis.

Authors:  Aitbay Bulashev; Orken Akibekov; Alfiya Syzdykova; Zhanbolat Suranshiyev; Bakytkali Ingirbay
Journal:  Vet World       Date:  2020-07-25
  1 in total

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