PURIFICATION AND DETECTION OF IMMUNOGLOBULIN USING THE AFFINITY PROTEIN RPROTEIN-L

Authors
Citation
Ml. Isaksen, PURIFICATION AND DETECTION OF IMMUNOGLOBULIN USING THE AFFINITY PROTEIN RPROTEIN-L, Nature, 1998, pp. 10-10
Citations number
1
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Year of publication
1998
Supplement
S
Pages
10 - 10
Database
ISI
SICI code
0028-0836(1998):<10:PADOIU>2.0.ZU;2-Z
Abstract
A number of immunoglobulin-binding proteins of bacterial origin have b een identified in recent years, They have become powerful tools for bi nding, detection and purification of immunoglobulin antibodies; protei n A, from Staphylococcus aureus, and the streptococcal protein G are t wo of the most widely used, However, these are both predominantly IgG Fc-binding proteins. Many monoclonal antibodies do not bind to protein A or protein G. Consequently there is a growing need for a molecule w ith broader immunoglobulin-binding activity, including affinity for va rious immunoglobulin classes as well as Fab fragments and scFv fragmen ts, Such a molecule is described here.