Anti-PSAP Antibody Picoband® Fluoro488 Conjugated

This gene encodes a highly conserved preproprotein that is proteolytically processed to generate four main cleavage products including saposins A, B, C, and D. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Mutations in this gene have been associated with Gaucher disease and metachromatic leukodystrophy. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.

High levels in cardiac and skeletal muscle. Up to 10 isoforms can be present in different amounts in different tissues. Most isoforms are ubiquitous. Isoforms that lack the N-terminus are found in leukocytes and fibroblasts, but not in heart and skeletal muscle. Some forms appear restricted to cardiac and skeletal muscle or to leukocytes.

Cancer, Cardiogenesis, Cardiovascular, Domain Families, Epigenetics and Nuclear Signaling, Oncoproteins, Oncoproteins/Suppressors, Transcription, Transcription Factors, Transcription Factors/Regulators

1. Azuma, N., O'Brien, J. S., Moser, H. W., Kishimoto, Y. Stimulation of acid ceramidase activity by saposin D. Arch. Biochem. Biophys. 311: 354-357, 1994. 2. Bar-Am, I., Avivi, L., Horowitz, M. Assignment of the human prosaposin gene (PSAP) to 10q22.1 by fluorescence in situ hybridization. Cytogenet. Cell Genet. 72: 316-318, 1996. 3. Bradova, V., Smid, F., Ulrich-Bott, B., Roggendorf, W., Paton, B. C., Harzer, K. Prosaposin deficiency: further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease. Hum. Genet. 92: 143-152, 1993.