The enzyme 2', 3'-cyclic nucleotide 3'-phosphodi-esterase (CNP) is expressed at high levels by oligodendrocytes in the central nervous system and by Schwann cells in the peripheral nervous system (Sprinkle, 1989). By virtue of this cell-specific expression, CNP is recognized as a characteristic marker for these two myelin-producing glial cell types (Sprinkle, 1989; Kim et al., 1984; Sheedlo & Sprinkle, 1984; McMorris et al., 1984). Beyond its enzymatic activity of cleaving the 2', 3'-cyclic terminus of nucleotides (Sprinkle, 1989), the physiological role of CNP is still under investigation. CNP activity has been correlated with myelin and myelin formation, and a dramatic decrease in CNP activity is associated with demyelinating diseases such as multiple sclerosis (Sprinkle, 1989). This enzyme is composed of two proteins, CNP1 (46 kD) and CNP2 (48 kD) (Sprinkle, 1989; Sprinkle et al., 1987). Although the ratio of CNP1/CNP2 may vary from species to species, their shared primary sequence is conserved phyIogenetically. CNP has recently been localized to human chromosome 17 by amplification of somatic cell hybrid DNA using the polymerase chain reaction (PCR) and by Southern blotting of Hind Ill genomic DNA digests (Sprinkle et al., 1991). Since anti-CNP reacts with a highly conserved region of the enzyme, it can be considered as pan-anti-CNP (Sprinkle et al., 1987). Anti-CNP can be used as a marker to identify Schwann cells and oligodendrocytes in cell cuIture and in tissue sections, as well as to localize CNP in cell membrane fractions. As CNP is expressed relatively early in postnatal development, anti-CNP is especially useful for the early identification of oligodendrocytes.