EXPRESSION OF OPIOID-BINDING CELL-ADHESION MOLECULE (OBCAM) AND NEUROTRIMIN (NTM) IN ESCHERICHIA-COLI AND THEIR REACTIVITY WITH MONOCLONAL ANTI-OBCAM ANTIBODY

OPIOID-BINDING cell adhesion molecule (OBCAM), neurotrimin (NTM) and l imbic system-associated membrane protein (LAMP) are homologous and are the members of the IgLON family which is a subfamily within the immun oglobulin superfamily. We cloned the cDNAs for OBCAM and NTM, prepared recombinant proteins, and examined the reactivity of the previously p repared monoclonal anti-OBCAM antibody, OBC53, with the recombinant pr oteins by immunoblotting. These experiments revealed that OBC53 recogn izes OBCAM about 1000 times as efficiently as NTM. Moreover, the NTM a nd LAMP peptides which have sequences homologous to the OBCAM peptide used for the preparation of OBC53 were 150 times less reactive to OBC5 3. Thus, the OBC53 antibody is a useful tool for specifically detectin g OBCAM in immunochemical experiments.