Shelf life (days): 365.0
Formulation: 20 mM Tris, 500 mM sodium chloride, with 25% glycerol, pH 7.5
Uniprot ID: P17405
Purity: ≥90% as estimated by SDS-PAGE
Formula Weight: 0.0
Notes: Acid sphingomyelinase, also known as sphingomyelin phosphodiesterase 1 (SMPD1), is a lysosomal and secretory phosphodiesterase.{68857} SMPD1, the gene encoding acid sphingomyelinase, produces three isoforms but only the full-length isoform is further processed into a precursor polypeptide, which is composed of an N-terminal signal peptide, a saposin-like (SAP) domain, a proline-rich domain, a metallophosphoesterase catalytic region, and a C-terminal domain. The precursor polypeptide is subject to post-translational modifications and alternative trafficking, which results in two enzymes: lysosomal sphingomyelinase (L-SMase), which is further cleaved to an N-terminus of Gly66, and secretory sphingomyelinase (S-SMase), which is further cleaved to an N-terminus of His60.{68857,68858} Both enzymes catalyze the hydrolysis of sphingomyelin into ceramide and phosphocholine.{68857} Acid sphingomyelinase is ubiquitously expressed and hydrolyzes sphingomyelin in the endo-lysosome, in lipoproteins, and at the outer leaflet of the plasma membrane.{68859,68857} It has roles in various cellular processes, including apoptosis, immune cell activation, and inflammation.{68858} Mutations in SMPD1 result in type A and B Niemann-Pick disease, a lysosomal storage disorder characterized by sphingomyelin accumulation in the endo-lysosome and visceral, neurological, and psychiatric symptoms.{68860,68861} Cayman's SMPD1 (human, recombinant) protein can be used for enzyme activity assay applications. This protein consists of 593 amino acids, has a calculated molecular weight of 66.3 kDa, and a predicted N-terminus of Leu47 after signal peptide cleavage.
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