Anti-ASAH1 Picoband® Antibody Fluoro647 Conjugated

The ASAH1 gene encodes in humans the acid ceramidase enzyme. It is mapped to 8p22. This gene encodes a member of the acid ceramidase family of proteins. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed. Processing of this preproprotein generates alpha and beta subunits that heterodimerize to form the mature lysosomal enzyme, which catalyzes the degradation of ceramide into sphingosine and free fatty acid. This enzyme is overexpressed in multiple human cancers and may play a role in cancer progression. Mutations in this gene are associated with the lysosomal storage disorder, Farber lipogranulomatosis, and a neuromuscular disorder, spinal muscular atrophy with progressive myoclonic epilepsy.

Acid ceramidase; AC; ACDase; Acid Cdase; Acylsphingosine deacylase; N-acylethanolamine hydrolase ASAH1; N-acylsphingosine amidohydrolase; Putative 32 kDa heart protein; PHP32; Acid ceramidase subunit alpha; Acid ceramidase subunit beta; ASAH1; ASAH; HSD-33; HSD33

Widely distributed throughout the CNS. Particularly abundant in kidney and intestinal microvilli, also detected in lung and liver. Weakly expressed in heart and aorta.

Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH. Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation. Has a higher catalytic efficiency towards C12-ceramides versus other ceramides. Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine. For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used. Has also an N-acylethanolamine hydrolase activity. By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes. Also inly regulates tumor necrosis factor/TNF-induced apoptosis. By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis. May ly regulate steroidogenesis by binding the nuclear receptor NR5A1 and negatively regulating its transcriptional activity.

1. Alves, M. Q., Le Trionnaire, E., Ribeiro, I., Carpentier, S., Harzer, K., Levade, T., Ribeiro, M. G. Molecular basis of acid ceramidase deficiency in a neonatal form of Farber disease: identification of the first large deletion in ASAH1 gene. Molec. Genet. Metab. 109: 276-281, 2013. 2. Souillet, G., Guibaud, P., Fensom, A. H., Maire, I., Zabot, M. T. Outcome of displacement bone marrow transplantation in Farber's disease: a report of a case.In: Hobbs, J. R. (ed.) : Correction of Certain Genetic Diseases by Transplantation. London: COGENT 1989. Pp. 137-141. 3. Zhou, J., Tawk, M., Tiziano, F. D., Veillet, J., Bayes, M., Nolent, F., Garcia, V., Servidei, S., Bertini, E., Castro-Giner, F., Renda, Y., Carpentier, S., Andrieu-Abadie, N., Gut, I., Levade, T., Topaloglu, H., Melki, J. Spinal muscular atrophy associated with progressive myoclonic epilepsy is caused by mutations in ASAH1. Am. J. Hum. Genet. 91: 5-14, 2012.