The ontogenic development of secretogranin II was studied by immunochemistry and immunohistochemistry. Extracts of brains from various developmental stages were analyzed by a radioimmunoassay for secretoneurin, a peptide derived from secretogranin II. From gestational day 13 to adulthood the levels increased from 0.1 to 94 fmol/mg wet weight. Characterization of the immunoreactivity by molecular sieve chromatography revealed that throughout all developmental stages the proprotein secretogranin II was fully processed to the free peptide secretoneurin. In immunohistochemistry secretoneurin-IR was first detected at embryonic day 13. Between embryonic days 14 and 18 a strong increase in the number of secretoneurin immunopositive cells was observed in many brain areas, notably in the amygdala, hypothalamus, olfactory bulb and several brainstem nuclei. The pattern of staining during development is quite similar to that in the adult. The present paper demonstrates that secretoneurin immunoreactivity appears early in embryonic life. Processing of the proprotein secretogranin II starts when the protein is first synthesized apparently at about the same time when the prohormone convertase PC1 and PC2 can be demonstrated.