Anti-Human SMPD3 Antibody Pair

Product Description: Sphingomyelin phosphodiesterase 3 (SMPD3), also known as neutral sphingomyelinase 2, is an enzyme encoded by the SMPD3 gene in humans. This protein plays a critical role in sphingolipid metabolism by catalyzing the hydrolysis of sphingomyelin to generate ceramide and phosphocholine, a process pivotal for regulating cellular functions such as apoptosis, cell cycle arrest, and growth control. SMPD3 is involved in several metabolic pathways, including ceramide signaling, glycosphingolipid metabolism, and lipid and lipoprotein metabolism, highlighting its importance in maintaining cellular lipid homeostasis. Structurally, SMPD3 shares a conserved catalytic domain with other sphingomyelinases, and its activity is essential for multicellular organism development and the positive regulation of ceramide biosynthesis. Dysregulation or mutations in SMPD3 have been associated with pathological conditions such as necrosis and may contribute to broader metabolic or developmental disorders. Protein Function: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:10823942, PubMed:14741383, PubMed:15051724). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location. May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity) [The Uniprot Consortium]