The mouse homologue to human fetal antigen 1 (hFA1) was purified from mouse amniotic fluid by cation exchange chromatography and immunospecific affinity chromatography. Mouse FA1 (mFA1) is a single chain glycoprotein with an M(r) of 42-50 kDa (SDS-PAGE). The N-terminal amino acid sequence (39 residues) revealed 74% identity to hFA1 and 100% identity to the translated cDNAs referred to as mouse dlk, pref-1 and SCP-1. mFA1 is the secreted processed molecule encoded by the mRNA defined by these identical mouse cDNAs. Monospecific rabbit anti-mFA1 antibodies, purified by ammonium sulfate precipitation and immunospecific affinity chromatography, were used for immunohistochemical and quantitative ELISA techniques. The indirect immunoperoxidase technique demonstrated mFA1 within the endocrine structures of adult mouse pancreas, whereas the exocrine tissue remained unstained. FA1-positive staining was also seen in the pituitary gland and the mouse adrenal gland. The concentration of mFA1 in a pool of amniotic fluid was assessed at 25 micrograms ml-1 and the serum concentration in normal nonpregnant adult mice (n = 28) was 11.3 +/- 5.0 ng ml-1 (2 SD). During pregnancy the concentration of mFA1 in maternal serum increased above the nonpregnant reference value at midpregnancy, reaching a maximum concentration (> 0.35 microgram ml-1) 2 days prepartum. The maternal serum concentration was positively correlated with the number of fetuses. After delivery the rate of disappearance of mFA1 in maternal serum was very fast with a t1/2 < 1 h. The concentration of mFA1 in newborn mice was about 15 micrograms ml-1 and did not reach normal adult values until the age of > 50 days.