|Detection of Human SMPD3 by Western Blot. Western blot shows lysates of RPMI 8226 human multiple myeloma cell line and CEM human T-lymphoblastoid cell line. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human SMPD3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7184) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). Specific bands were detected for SMPD3 at approximately 70 to 75 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
SMPD3 (Sphingomyelin phosphodiesterase 3; also Neutral sphingomyelinase 2/nSMase2) is a 69-74 kDa member of the neutral sphingomyelinase family of enzymes. It is a monomeric Golgi/plasma membrane enzyme that converts sphingomyelin (a plasma membrane lipid) into ceramide and phosphorylcholine. This generates second messenger components that participate in signal transduction. Human SMPD3 is a two transmembrane, 655 amino acids molecule. It contains an N-terminal luminal segment (aa 1-10), a cytoplasmic region (aa 32-64), and one catalytic domain (aa 340-646). Phosphorylation increases its MW to 78 kDa in SDS-PAGE. There is one potential isoform that possesses an Asn substitution for aa 569-587. Over aa 2-655, human SMPD3 shares 91% aa sequence identity with mouse SMPD3.
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