A unique epitope exposed in native complement component C9 and hidden in the terminal SC5b-9 complex enables selective detection and quantification of non-activated C9

Détails

ID Serval
serval:BIB_45C5B7FF0F15
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A unique epitope exposed in native complement component C9 and hidden in the terminal SC5b-9 complex enables selective detection and quantification of non-activated C9
Périodique
Journal of Immunological Methods
Auteur(s)
Mollnes  T. E., Tschopp  J.
ISSN
0022-1759 (Print)
Statut éditorial
Publié
Date de publication
06/1987
Volume
100
Numéro
1-2
Pages
215-21
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jun 26
Résumé
Recently, monoclonal antibodies recognizing epitopes exposed in activation products of complement but hidden in the native components have been characterized and used for selective quantification of the activated protein. We now demonstrate that an epitope in the native component C9 is hidden in the terminal SC5b-9 complex. A monoclonal antibody against this epitope enabled selective detection of C9 without influence of the amount of SC5b-9 present. This antibody recognizing native soluble C9 was used to construct a quantitative double-antibody ELISA with unique sensitivity and specificity. Combination of this assay with an assay previously described for selective quantification of the SC5b-9 complex provides an important tool for evaluating terminal pathway activation of complement.
Mots-clé
Animals Antibodies, Monoclonal/immunology Antibody Specificity Complement C9/*analysis/immunology Complement Membrane Attack Complex Complement System Proteins/*analysis Enzyme-Linked Immunosorbent Assay Epitopes/*immunology Humans Mice Multiple Sclerosis/immunology
Pubmed
Web of science
Création de la notice
24/01/2008 16:18
Dernière modification de la notice
03/03/2018 16:46
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