SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "id:"swepub:oai:DiVA.org:kth-5915" "

Search: id:"swepub:oai:DiVA.org:kth-5915"

  • Result 1-1 of 1
Sort/group result
   
EnumerationReferenceCoverFind
1.
  • Agaton, Charlotta, et al. (author)
  • Selective enrichment of monospecific polyclonal antibodies for antibody-based proteomics efforts
  • 2004
  • In: Journal of Chromatography A. - : Elsevier BV. - 0021-9673 .- 1873-3778. ; 1043, s. 33-40
  • Journal article (peer-reviewed)abstract
    • A high stringency protocol, suitable for systematic purification of polyclonal antibodies, is described. The procedure is designed to allow the generation of target protein-specific antibodies suitable for functional annotation of proteins. Antibodies were generated by immunization with recombinantly produced affinity-tagged target proteins. To obtain stringent recovery of the antibodies, a two-step affinity chromatography principle was devised to first deplete the affinity tag-specific antibodies followed by a second step for affinity capture of the target protein-specific antibodies. An analytical dot-blot array system was developed to analyze the cross-reactivity of the affinity-purified antibodies. The results suggest that the protocol can be used in a highly parallel and automated manner to generate mono-specific polyclonal antibodies for large-scale, antibody-based proteomics efforts, i.e. affinity proteomics.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-1 of 1
Type of publication
journal article (1)
Type of content
peer-reviewed (1)
Author/Editor
Uhlén, Mathias (1)
Hober, Sophia (1)
Agaton, Charlotta (1)
Falk, Ronny (1)
University
Royal Institute of Technology (1)
Language
English (1)
Research subject (UKÄ/SCB)
Engineering and Technology (1)
Year

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view