SMPDL3A (human, recombinant; His-tagged)

Acid Sphingomyelinase-like Phosphodiesterase 3A|ASML3A|ASM-like Phosphodiesterase 3A|Sphingomyelin Phosphodiesterase Acid-like 3A

Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a zinc-dependent nucleotide phosphoesterase and member of the acid sphingomyelinase-like enzyme family.{67625} It is composed of an N-terminal catalytic domain and a C-terminal domain, which contains an asparagine located at position 356 (Asn356). The N-glycosylation of Asn356 is required for SMPDL3A stability, enzymatic activity, and cellular secretion.{67625,67627} SMPDL3A is expressed in, and secreted from, osteoclasts, adipocytes, astrocytes, and macrophages and reduces local inflammation induced by nucleotide tri- or diphosphates.{67626,67625} Its intracellular levels and secretion are increased by cAMP, cholesterol, and liver X receptor (LXR) activation, and it localizes to the lysosome, which provides the acidic environment required for its optimal catalytic activity.{67626,67625} SMPDL3A knockout decreases cell proliferation, colony formation, and migration, as well as induces cell cycle arrest in the G0/G1 phase and apoptosis in HepG2 hepatocellular carcinoma cells.{67628} In vivo, SMPDL3A knockout in HepG2 cells reduces tumor volume and weight in a HepG2 xenograft mouse model. SMPDL3A levels are increased in patients with hepatocellular carcinoma (HCC) and negatively correlated with prognosis. Cayman's SMPDL3A (human, recombinant; His-tagged) protein consists of 442 amino acids and has a calculated molecular weight of 50.3 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 51 kDa due to glycosylation.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥95% estimated by SDS-PAGE