Anti-Smpd1 / Acid sphingomyelinase / aSMase

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Sphingomyelin phosphodiesterase 1 (SMPD1), also known as acid sphingomyelinase (ASM or aSMase), is an enzyme that in humans is encoded by the SMPD1 gene. Enables acid sphingomyelin phosphodiesterase activity and zinc ion binding activity. Involved in ceramide biosynthetic process, positive regulation of apoptotic process, and response to ionizing radiation. Acts upstream of or within ceramide metabolic process, cholesterol metabolic process, and sphingomyelin catabolic process. Located in extracellular space. Is expressed in several structures, including alimentary system, integumental system, nervous system, sensory organ, and skeleton. Used to study Niemann-Pick disease. Human ortholog(s) of this gene implicated in Niemann-Pick disease, Niemann-Pick disease type A, and Niemann-Pick disease type B. Orthologous to human SMPD1 (sphingomyelin phosphodiesterase 1). Protein function: Converts sphingomyelin to ceramide (PubMed:9660788, PubMed:8706124). Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form. [The UniProt Consortium]