Anti-SMPD3 / Sphingomyelin phosphodiesterase 3 / nSMase2

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. SMPD3 antibody detects Sphingomyelin phosphodiesterase 3, a membrane-associated enzyme that hydrolyzes sphingomyelin to generate ceramide and phosphocholine. The UniProt recommended name is Sphingomyelin phosphodiesterase 3 (SMPD3). This enzyme, also known as neutral sphingomyelinase 2 (nSMase2), plays a key role in lipid metabolism, cell signaling, and exosome biogenesis.Functionally, SMPD3 antibody identifies a 655-amino-acid enzyme localized to the plasma membrane and Golgi apparatus. SMPD3 catalyzes the production of ceramide, a lipid second messenger involved in apoptosis, differentiation, and inflammation. It regulates membrane curvature and vesicle budding, particularly in exosome secretion and cell stress responses.The SMPD3 gene is located on chromosome 16p13.12 and is expressed in brain, liver, and skeletal tissue. SMPD3 activity influences cell growth, neuronal communication, and lipid raft organization. By controlling ceramide levels, SMPD3 links sphingolipid metabolism to cell fate decisions and inflammatory signaling.Pathologically, dysregulation of SMPD3 contributes to metabolic, neurodegenerative, and cardiovascular diseases. Deficiency results in skeletal abnormalities (spondyloepimetaphyseal dysplasia) and altered lipid homeostasis. Overactivation can enhance ceramide-induced apoptosis or inflammatory cascades. Research using SMPD3 antibody supports studies in lipid signaling, neurobiology, and exosome biology.SMPD3 antibody is validated for western blotting, immunofluorescence, and immunohistochemistry to detect sphingomyelinases and lipid signaling enzymes. NSJ Bioreagents provides SMPD3 antibody reagents optimized for cell signaling, metabolism, and membrane biology research.Structurally, Sphingomyelin phosphodiesterase 3 contains an N-terminal hydrophobic domain for membrane association and a C-terminal catalytic domain requiring Mg2+ for activity. This antibody enables analysis of SMPD3?s role in ceramide-mediated signal transduction and cellular stress responses.