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.