A monoclonal antibody (SB-4) to human Clq was prepared. The equilibrium constant of the antibody for CI q was found to be greater than 10 ~° M -1. It has been shown that the antibody binds to the A-B chain dimer, probably via the B chain of Clq. Pepsin digestion of Clq at pH 4.5, which fragments the globular regions but leaves the collagenous region intact, allowed the demonstration that the antigenic site is located in the collagenous region of the molecule. The effect of the antibody on haemolytic activity has shown that it is capable of inhibiting the formation of EAC1 cells from EAClq cells plus Clr and Cls but is incapable of inhibiting the CI activity of preformed EAC1 cells. This indicates that the binding of the antibody to the collagenous portion of the B chain of Clq probably prevents interaction between Clq and the Clr2-Cls z complex.