L1CAM can be detected between 200-220 kD. In brain samples it is typically seen at ~ 200 kD. When the protein is overexpressed in vitro it is often detected as a doublet with bands at 200 and 220 kD. The unglycosylated, unprocessed L1CAM is ~ 140-150 kDa. The protein has 21 putative N-glycosylation sites on the extracellular portion of the protein which, when they are all glycosylated, results in a detected MW of 200-220 kD depending upon how many residues are actually glycosylated. L1CAM can be cleaved by the metalloprotease ADAM10 resulting in fragments of 180 kD and 40 kD. L1CAM can also be cleaved by plasmin resulting in fragments of 140 kD and 80 kD. In theory, therefore, one could detect bands at ~220, 200, 180, 140, 80 and 40 kD.