Aim Studies were performed to produce specificmonoclonal antibodies to bovine milk lipoprotein lipase(bLPL), to verify the specificity of the monoclonal an-tibodies for bLPL, and to characterize them.Metkods Purified lipoprotein lipase (LPL) frombovine milk-56 kDa was used as an antigen for the pro-duction of anti-LPL antibodies in mice. The spleen wasremoved from the animal having the highest titer of an-tibodies to LPL and the cells were fused with mousemyeloma cells. After cultured with hypoxanthine-aminopterin-thymidine (HAT ) culture medium, thisprocedure thus identified only those hybridomas whichproduced antibodies directed against LPL for super-natants by enzyme linked immunosorbent assay(ELISA). After cloning five monoclonal cell strainswere established, named as 2E5, 2G10, 6D7, 8D2 and7F4. The titriton of monoclonal antibodies (McAb) are5 × 10-2~2 × 10-3 for supernatants by ELISA.Results and Conclusion Contitration study showedMcAb recognized three different epitopes of LPL: 6D7and 8D2 to a close epitop; 2G10 and 7F4 to other closeepitope; 2G10 but recognized a far epitope away fromthe two of others. Western blot analysis of bovine milkwith the McAb gave a single protein band of 56 kDa;2G10 gave two protein bands of 50 kDa and 47 kDa.Dot-blot analysis of bovine milk with the McAb 2E5,8D2 and 6D7 showed specific reaction Western blot andDet-blot analysis of human milk with the McAb, hadno cross-reacted.