Human SMPD1 (His Tag) recombinant protein

Human SMPD1 (His Tag) recombinant protein

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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.

Sphingomyelin phosphodiesterase

SMPD1; NPD; A-SMASE; ASM; ASMASE; ZN-SMASE

Q59EN6

SMPD1; ASM

Baculovirus-Insect Cells

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.

Human

The secreted recombinant human SMPD1 consists of 518 amino acids and predicts a molecular mass of 65 kDa as estimated by SDS-PAGE under reducing conditions.

> 94 % as determined by SDS-PAGE

Measured by its ability to cleave. 2-N-Hexadecanoylamino-4-nitrophenylphosphorylcholine (HNPPC). The specific activity is >1,000 pmol/min/μg.