We cloned human activin betaE subunit cDNA from a liver cDNA library using the polymerase chain reaction (PCR) technique. The deduced amino acid sequence was 97 and 96% homologous to the mouse and rat activin betaE subunits. Human activin betaE subunit tagged with Myc and polyhistidine residues at the COOH terminus was expressed in mammalian cells and secreted into the medium as a disulphide-linked homodimer protein. We also found that the human activin betaE protein could bind to follistatin, an activin-binding protein. Northern blot analysis showed that this gene was expressed as a major transcript of 2.7 kb predominantly in human liver. These findings suggest that activin E (dimeric protein) may play a role in humans.