Sphingomyelin phosphodiesterase 1 (SMPD1) , also known as ASM ( acid sphingomyelinase ), is a member of the acid sphingomyelinase family of enzymes. Three isoforms have been identified, isoform 1 is 631 amino acids (aa) in length as the pro form, while Isoform 2 and isoform 3 have lost catalytic activity. The active SMPD1 isoform 1 contains one saposin B-type domain that likely interacts with sphingomyelin, and a catalytic region. Human SMPD1 is 86% aa identical to mouse SMPD1. SMPD1 is a monomeric lysosomal enzyme that converts sphingomyelin (a plasma membrane lipid ) into ceramide through the removal of phosphorylcholine. This generates second messenger components that participate in signal transduction. Defects in SMPD1 are the cause of Niemann-Pick disease type A (NPA) and type B (NPB), also known as Niemann-Pick disease classical infantile form and Niemann-Pick disease visceral form. Niemann-Pick disease is a clinically and genetically heterogeneous recessive disorder. NPB has little if any neurologic involvement and patients may survive into adulthood.
Product Name:
Human SMPD1/ASM Recombinant Protein (RPES1340)
Product Code:
RPES1340
Size:
10µg
Species:
Human
Expressed Host:
Baculovirus-Insect Cells
Synonyms:
ASM,ASMASE,NPD
Accession:
NP_000534.3
Sequence:
Met 1-Cys 631
Fusion tag:
C-His
Activity:
Measured by its ability to cleave. 2-N-Hexadecanoylamino-4-nitrophenylphosphorylcholine (HNPPC). The specific activity is >1,000 pmol/min/µg.
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the full length of human SMPD1 isoform 1 (NP_000534.3) (Met 1-Cys 631) was expressed, fused with a polyhistidine tag at the C-terminus.
