The StAR protein was first identified, characterized and named by Dr. Douglas Stocco at Texas Tech University Health Sciences Center in 1994.  The role of this protein in lipoid CAH was confirmed the following year in collaboration with Dr. Walter Miller at the University of California, San Francisco .  All of this work follows the initial observations of the appearance of this protein and its phosphorylated form coincident with factors that caused steroid production by Dr. Nanette Orme-Johnson while at Tufts University . 
Antibodies raised against steroid sulfatase purified from human placenta were used to follow the biosynthesis of this enzyme in human skin fibroblasts. Steroid sulfatase is synthesized as a membrane-bound M r -63 500 polypeptide with asparagine-linked oligosaccharide chains. Within 2 days, newly synthesized steroid sulfatase is processed to a mature M r -61000 form. The decrease in size is due to processing of the oligosaccharide chains, which are cleavable by endoglucosaminidase H in both the early and the mature form of steroid sulfatase. The processing involves mannosidase(s) sensitive to 1-deoxy- manno -nojirimycin. The half-life of the steroid sulfatase polypeptides is 4 days. Synthesis of steroid-sulftase-related polypeptides and steroid sulfatase activity were not detectable in fibroblasts from four patients with X-linked ichthyosis.