Protein aggregation can be a major problem in the manufacturing of new biopharmaceuticals and there is a desirability for development of techniques that can predict the behaviour of new biopharmaceuticals early on in the development process. A technique that can be used to predict aggregation is self-interaction chromatography that is used to determine the second virial coefficient, B22, but one of the limitations includes the need to immobilise every protein of interest. In this study a related technique, cross interaction chromatography (CIC), is evaluated which overcomes this limitation. Three antibodies were studied across a range of NaCl concentrations with each antibody being studied as both a mobile phase and as the stationary phase - in total 6 different stationary-mobile phase combinations. The B22 values obtained for all three proteins correlated strongly with the B23 results obtained for the same protein in the mobile phase, and were significantly independent of the protein immobilised on the stationary phase. This observation allows the use of pre-prepared columns with known immobilised model proteins such as a polyclonal antibody or mAb, with other unknown monoclonal antibodies in the mobile phase. Preliminary experiments using a series of known immobilised mAbs columns with an unknown mAb in the mobile phase resulted in at least a 50 fold reduction in the amount of unknown protein needed and a rapid semi-quantitative assessment of aggregation propensity. CIC can speed up the screening process with minimum preparation time and therefore more rapidly be able to identify the aggregation stability of new antibody formulations.