Purification of Sterol Carrier Protein (SCP) from rat liver is described. Lipid binding studies indicated that the purified SCP is a fatty acid binding protein. However, no cholesterol binding by SCP was observed. Antibodies were produced in both mice and rabbits to PAG-incorporated SCP and to native SCP and the specificity and sensitivity of two of the antisera was determined to be adequate for development of an ELISA for SCP. Further treatment of the selected antisera is discussed with a view to development of a sandwich ELISA for SCP.