The 200/220 kDa antigen recognized by monoclonal antibody (MAb) UJ127.11 on neural tissues and tumors is the human L1 adhesion molecule.
MAb UJ127.11, raised against 16 week human fetal brain, recognizes an antigen present primarily on normal and tumor tissues derived from the neuroectoderm. The antigen has previously been identified as a 220/240 kDa cell surface glycoprotein as determined by immunoprecipitation studies. We show here, that the 220/240 kDa antigen is the human L1 cell adhesion molecule and by Western blot analysis actually has a calculated molecular weight of between 200-220 kDa. Immunocytochemical studies with UJ127.11 and an antibody (5G3) recently utilized to isolate human L1 from brain indicate that both reagents have very similar binding profiles. The binding of radiolabelled UJ127.11 to its target antigen can be blocked by the addition of a rabbit anti-human L1 antiserum. Furthermore, sequential immunoprecipitation and Western blot analysis shows that UJ127.11 and the rabbit anti-human L1 antiserum recognize identical proteins.